ID LAMA5_HUMAN Reviewed; 3695 AA. AC O15230; Q5U4N9; Q8TDF8; Q8WZA7; Q9H1P1; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 8. DT 13-FEB-2019, entry version 197. DE RecName: Full=Laminin subunit alpha-5; DE AltName: Full=Laminin-10 subunit alpha; DE AltName: Full=Laminin-11 subunit alpha; DE AltName: Full=Laminin-15 subunit alpha; DE Flags: Precursor; GN Name=LAMA5; Synonyms=KIAA0533, KIAA1907; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-401; RP THR-1258; GLU-1367; SER-1807; MET-1900; ASN-2062 AND TRP-3079. RX PubMed=11821406; DOI=10.1074/jbc.M111228200; RA Doi M., Thyboll J., Kortesmaa J., Jansson K., Iivanainen A., RA Parvardeh M., Timpl R., Hedin U., Swedenborg J., Tryggvason K.; RT "Recombinant human laminin-10 (alpha5beta1gamma1). Production, RT purification, and migration-promoting activity on vascular endothelial RT cells."; RL J. Biol. Chem. 277:12741-12748(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT RP ALA-401. RC TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1934 (ISOFORM 1), AND RP VARIANTS MET-889; GLU-1367 AND SER-1807. RC TISSUE=Brain; RX PubMed=11572484; DOI=10.1093/dnares/8.4.179; RA Nagase T., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XXI. RT The complete sequences of 60 new cDNA clones from brain which code for RT large proteins."; RL DNA Res. 8:179-187(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2051-3695 (ISOFORM 1), AND RP VARIANTS ASN-2062 AND TRP-3079. RC TISSUE=Brain; RX PubMed=9628581; DOI=10.1093/dnares/5.1.31; RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., RA Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. IX. RT The complete sequences of 100 new cDNA clones from brain which can RT code for large proteins in vitro."; RL DNA Res. 5:31-39(1998). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2743-3695 (ISOFORM 1), AND VARIANT RP TRP-3079. RC TISSUE=Placenta; RX PubMed=9271224; DOI=10.1016/S0014-5793(97)00686-8; RA Durkin M.E., Loechel F., Mattei M.-G., Gilpin B.J., Albrechtsen R., RA Wewer U.M.; RT "Tissue-specific expression of the human laminin alpha5-chain, and RT mapping of the gene to human chromosome 20q13.2-13.3 and to distal RT mouse chromosome 2 near the locus for the ragged (Ra) mutation."; RL FEBS Lett. 411:296-300(1997). RN [7] RP EXPRESSION IN RETINA. RX PubMed=10964957; RA Libby R.T., Champliaud M.-F., Claudepierre T., Xu Y., Gibbons E.P., RA Koch M., Burgeson R.E., Hunter D.D., Brunken W.J.; RT "Laminin expression in adult and developing retinae: evidence of two RT novel CNS laminins."; RL J. Neurosci. 20:6517-6528(2000). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2209; ASN-2303; ASN-2423; RP ASN-2501; ASN-2568; ASN-2707 AND ASN-3107. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin CC is thought to mediate the attachment, migration and organization CC of cells into tissues during embryonic development by interacting CC with other extracellular matrix components. CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three CC different polypeptide chains (alpha, beta, gamma), which are bound CC to each other by disulfide bonds into a cross-shaped molecule CC comprising one long and three short arms with globules at each CC end. Alpha-5 is a subunit of laminin-10 (laminin-511), laminin-11 CC (laminin-521) and laminin-15 (laminin-523). CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. Note=Major component. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O15230-1; Sequence=Displayed; CC Name=2; CC IsoId=O15230-2; Sequence=VSP_057343, VSP_057344; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Expressed in heart, lung, kidney, skeletal CC muscle, pancreas, retina and placenta. Little or no expression in CC brain and liver. CC -!- DOMAIN: Domain G is globular and is part of the major cell-binding CC site located in the long arm of the laminin heterotrimer. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AF443072; AAM12527.1; -; mRNA. DR EMBL; AL354836; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC085017; AAH85017.1; -; mRNA. DR EMBL; AB067494; BAB67800.1; -; mRNA. DR EMBL; AB011105; BAA25459.1; -; mRNA. DR EMBL; Z95636; CAB09137.1; -; mRNA. DR CCDS; CCDS33502.1; -. [O15230-1] DR RefSeq; NP_005551.3; NM_005560.4. [O15230-1] DR UniGene; Hs.473256; -. DR PDB; 5XAU; X-ray; 1.80 A; A/D=2655-3327. DR PDBsum; 5XAU; -. DR ProteinModelPortal; O15230; -. DR SMR; O15230; -. DR BioGrid; 110105; 35. DR ComplexPortal; CPX-1779; Laminin-511 complex. DR ComplexPortal; CPX-1780; Laminin-521 complex. DR ComplexPortal; CPX-1783; Laminin-522 complex. DR ComplexPortal; CPX-1784; Laminin-523 complex. DR CORUM; O15230; -. DR IntAct; O15230; 21. DR MINT; O15230; -. DR STRING; 9606.ENSP00000252999; -. DR ChEMBL; CHEMBL2364187; -. DR CarbonylDB; O15230; -. DR GlyConnect; 1441; -. DR iPTMnet; O15230; -. DR PhosphoSitePlus; O15230; -. DR SwissPalm; O15230; -. DR BioMuta; LAMA5; -. DR EPD; O15230; -. DR jPOST; O15230; -. DR MaxQB; O15230; -. DR PaxDb; O15230; -. DR PeptideAtlas; O15230; -. DR PRIDE; O15230; -. DR ProteomicsDB; 48522; -. DR DNASU; 3911; -. DR Ensembl; ENST00000252999; ENSP00000252999; ENSG00000130702. [O15230-1] DR GeneID; 3911; -. DR KEGG; hsa:3911; -. DR UCSC; uc002ycq.5; human. [O15230-1] DR CTD; 3911; -. DR DisGeNET; 3911; -. DR EuPathDB; HostDB:ENSG00000130702.13; -. DR GeneCards; LAMA5; -. DR H-InvDB; HIX0015978; -. DR HGNC; HGNC:6485; LAMA5. DR HPA; CAB078157; -. DR HPA; HPA054609; -. DR MIM; 601033; gene. DR neXtProt; NX_O15230; -. DR OpenTargets; ENSG00000130702; -. DR Orphanet; 521450; LAMA5-related multisystemic syndrome. DR PharmGKB; PA30274; -. DR eggNOG; KOG1836; Eukaryota. DR eggNOG; ENOG410XRDC; LUCA. DR GeneTree; ENSGT00940000156537; -. DR HOGENOM; HOG000231235; -. DR HOVERGEN; HBG056287; -. DR InParanoid; O15230; -. DR KO; K06240; -. DR OMA; RCDCSPC; -. DR OrthoDB; 2342at2759; -. DR PhylomeDB; O15230; -. DR TreeFam; TF335359; -. DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix. DR Reactome; R-HSA-3000157; Laminin interactions. DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-HSA-8874081; MET activates PTK2 signaling. DR SIGNOR; O15230; -. DR ChiTaRS; LAMA5; human. DR GeneWiki; Laminin,_alpha_5; -. DR GenomeRNAi; 3911; -. DR PRO; PR:O15230; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; ENSG00000130702; Expressed in 211 organ(s), highest expression level in right hemisphere of cerebellum. DR ExpressionAtlas; O15230; baseline and differential. DR Genevisible; O15230; HS. DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0043259; C:laminin-10 complex; IDA:UniProtKB. DR GO; GO:0043260; C:laminin-11 complex; TAS:BHF-UCL. DR GO; GO:0005610; C:laminin-5 complex; IEA:Ensembl. DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0043083; C:synaptic cleft; IEA:Ensembl. DR GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL. DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB. DR GO; GO:0001525; P:angiogenesis; NAS:UniProtKB. DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl. DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl. DR GO; GO:0030154; P:cell differentiation; NAS:UniProtKB. DR GO; GO:0016477; P:cell migration; IDA:UniProtKB. DR GO; GO:0008283; P:cell population proliferation; NAS:UniProtKB. DR GO; GO:0008037; P:cell recognition; NAS:UniProtKB. DR GO; GO:0060271; P:cilium assembly; IEA:Ensembl. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB. DR GO; GO:0045446; P:endothelial cell differentiation; NAS:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0048041; P:focal adhesion assembly; NAS:UniProtKB. DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IEA:Ensembl. DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Ensembl. DR GO; GO:0007517; P:muscle organ development; IEA:Ensembl. DR GO; GO:0001755; P:neural crest cell migration; IEA:Ensembl. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl. DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl. DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro. DR GO; GO:0030334; P:regulation of cell migration; IEA:InterPro. DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:BHF-UCL. DR Gene3D; 2.60.120.1490; -; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR009254; Laminin_aI. DR InterPro; IPR010307; Laminin_dom_II. DR InterPro; IPR002049; Laminin_EGF. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR000034; Laminin_IV. DR InterPro; IPR008211; Laminin_N. DR InterPro; IPR038684; Laminin_N_sf. DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg. DR Pfam; PF00052; Laminin_B; 1. DR Pfam; PF00053; Laminin_EGF; 19. DR Pfam; PF02210; Laminin_G_2; 4. DR Pfam; PF06008; Laminin_I; 1. DR Pfam; PF06009; Laminin_II; 1. DR Pfam; PF00055; Laminin_N; 1. DR SMART; SM00181; EGF; 15. DR SMART; SM00180; EGF_Lam; 21. DR SMART; SM00281; LamB; 1. DR SMART; SM00282; LamG; 5. DR SMART; SM00136; LamNT; 1. DR SUPFAM; SSF49899; SSF49899; 5. DR PROSITE; PS00022; EGF_1; 19. DR PROSITE; PS01186; EGF_2; 3. DR PROSITE; PS01248; EGF_LAM_1; 19. DR PROSITE; PS50027; EGF_LAM_2; 21. DR PROSITE; PS50025; LAM_G_DOMAIN; 5. DR PROSITE; PS51115; LAMININ_IVA; 1. DR PROSITE; PS51117; LAMININ_NTER; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Basement membrane; Cell adhesion; KW Coiled coil; Complete proteome; Disulfide bond; Extracellular matrix; KW Glycoprotein; Laminin EGF-like domain; Polymorphism; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1 35 {ECO:0000255}. FT CHAIN 36 3695 Laminin subunit alpha-5. FT /FTId=PRO_0000017062. FT DOMAIN 41 299 Laminin N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00466}. FT DOMAIN 300 358 Laminin EGF-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 359 428 Laminin EGF-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 429 474 Laminin EGF-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 494 540 Laminin EGF-like 4. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 541 586 Laminin EGF-like 5. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 587 631 Laminin EGF-like 6. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 632 676 Laminin EGF-like 7. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 677 722 Laminin EGF-like 8. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 723 775 Laminin EGF-like 9. {ECO:0000255|PROSITE- FT ProRule:PRU00460}. FT DOMAIN 776 828 Laminin EGF-like 10. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 829 850 Laminin EGF-like 11; truncated. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1438 1483 Laminin EGF-like 12. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1484 1527 Laminin EGF-like 13. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1528 1576 Laminin EGF-like 14. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1577 1627 Laminin EGF-like 15. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1628 1637 Laminin EGF-like 16; first part. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1641 1830 Laminin IV type A. {ECO:0000255|PROSITE- FT ProRule:PRU00458}. FT DOMAIN 1831 1863 Laminin EGF-like 16; second part. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1864 1912 Laminin EGF-like 17. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1913 1968 Laminin EGF-like 18. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 1969 2022 Laminin EGF-like 19. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 2023 2069 Laminin EGF-like 20. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 2070 2116 Laminin EGF-like 21. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 2117 2166 Laminin EGF-like 22. FT {ECO:0000255|PROSITE-ProRule:PRU00460}. FT DOMAIN 2736 2929 Laminin G-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT DOMAIN 2941 3115 Laminin G-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT DOMAIN 3124 3292 Laminin G-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT DOMAIN 3340 3513 Laminin G-like 4. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT DOMAIN 3520 3692 Laminin G-like 5. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT REGION 851 1437 Domain IV 1 (domain IV B). FT REGION 2167 2735 Domain II and I. FT COILED 2203 2221 {ECO:0000255}. FT COILED 2335 2466 {ECO:0000255}. FT COILED 2510 2670 {ECO:0000255}. FT MOTIF 1722 1724 Cell attachment site. {ECO:0000255}. FT MOTIF 1838 1840 Cell attachment site. {ECO:0000255}. FT CARBOHYD 95 95 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 143 143 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 243 243 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 452 452 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 479 479 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 900 900 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 921 921 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 959 959 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1330 1330 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1529 1529 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1555 1555 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2196 2196 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 2209 2209 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 2303 2303 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 2423 2423 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 2501 2501 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 2568 2568 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 2707 2707 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 3107 3107 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 3209 3209 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 3257 3257 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 3287 3287 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 3626 3626 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 300 309 {ECO:0000250}. FT DISULFID 302 322 {ECO:0000250}. FT DISULFID 324 333 {ECO:0000250}. FT DISULFID 336 356 {ECO:0000250}. FT DISULFID 359 368 {ECO:0000250}. FT DISULFID 361 393 {ECO:0000250}. FT DISULFID 396 405 {ECO:0000250}. FT DISULFID 408 426 {ECO:0000250}. FT DISULFID 429 440 {ECO:0000250}. FT DISULFID 431 447 {ECO:0000250}. FT DISULFID 449 458 {ECO:0000250}. FT DISULFID 461 471 {ECO:0000250}. FT DISULFID 494 506 {ECO:0000250}. FT DISULFID 496 515 {ECO:0000250}. FT DISULFID 517 526 {ECO:0000250}. FT DISULFID 529 538 {ECO:0000250}. FT DISULFID 541 553 {ECO:0000250}. FT DISULFID 543 560 {ECO:0000250}. FT DISULFID 562 571 {ECO:0000250}. FT DISULFID 574 584 {ECO:0000250}. FT DISULFID 587 599 {ECO:0000250}. FT DISULFID 589 605 {ECO:0000250}. FT DISULFID 607 616 {ECO:0000250}. FT DISULFID 619 629 {ECO:0000250}. FT DISULFID 632 644 {ECO:0000250}. FT DISULFID 634 650 {ECO:0000250}. FT DISULFID 652 661 {ECO:0000250}. FT DISULFID 664 674 {ECO:0000250}. FT DISULFID 677 689 {ECO:0000250}. FT DISULFID 679 696 {ECO:0000250}. FT DISULFID 698 707 {ECO:0000250}. FT DISULFID 710 725 {ECO:0000250}. FT DISULFID 746 755 {ECO:0000250}. FT DISULFID 758 773 {ECO:0000250}. FT DISULFID 776 790 {ECO:0000250}. FT DISULFID 778 797 {ECO:0000250}. FT DISULFID 799 808 {ECO:0000250}. FT DISULFID 811 826 {ECO:0000250}. FT DISULFID 829 841 {ECO:0000250}. FT DISULFID 831 848 {ECO:0000250}. FT DISULFID 850 859 {ECO:0000250}. FT DISULFID 1438 1450 {ECO:0000250}. FT DISULFID 1440 1457 {ECO:0000250}. FT DISULFID 1459 1468 {ECO:0000250}. FT DISULFID 1471 1481 {ECO:0000250}. FT DISULFID 1484 1491 {ECO:0000250}. FT DISULFID 1486 1498 {ECO:0000250}. FT DISULFID 1500 1509 {ECO:0000250}. FT DISULFID 1512 1525 {ECO:0000250}. FT DISULFID 1528 1543 {ECO:0000250}. FT DISULFID 1530 1550 {ECO:0000250}. FT DISULFID 1552 1561 {ECO:0000250}. FT DISULFID 1564 1574 {ECO:0000250}. FT DISULFID 1577 1589 {ECO:0000250}. FT DISULFID 1579 1596 {ECO:0000250}. FT DISULFID 1598 1607 {ECO:0000250}. FT DISULFID 1610 1625 {ECO:0000250}. FT DISULFID 1864 1873 {ECO:0000250}. FT DISULFID 1866 1880 {ECO:0000250}. FT DISULFID 1883 1892 {ECO:0000250}. FT DISULFID 1895 1910 {ECO:0000250}. FT DISULFID 1913 1928 {ECO:0000250}. FT DISULFID 1915 1937 {ECO:0000250}. FT DISULFID 1939 1948 {ECO:0000250}. FT DISULFID 1951 1966 {ECO:0000250}. FT DISULFID 1969 1984 {ECO:0000250}. FT DISULFID 1971 1991 {ECO:0000250}. FT DISULFID 1994 2003 {ECO:0000250}. FT DISULFID 2006 2020 {ECO:0000250}. FT DISULFID 2023 2033 {ECO:0000250}. FT DISULFID 2025 2040 {ECO:0000250}. FT DISULFID 2042 2051 {ECO:0000250}. FT DISULFID 2054 2067 {ECO:0000250}. FT DISULFID 2070 2081 {ECO:0000250}. FT DISULFID 2072 2088 {ECO:0000250}. FT DISULFID 2090 2099 {ECO:0000250}. FT DISULFID 2102 2114 {ECO:0000250}. FT DISULFID 2117 2124 {ECO:0000250}. FT DISULFID 2119 2131 {ECO:0000250}. FT DISULFID 2133 2142 {ECO:0000250}. FT DISULFID 2145 2164 {ECO:0000250}. FT DISULFID 2167 2167 Interchain. {ECO:0000305}. FT DISULFID 2170 2170 Interchain. {ECO:0000305}. FT DISULFID 2899 2929 {ECO:0000250}. FT DISULFID 3090 3115 {ECO:0000250}. FT DISULFID 3261 3292 {ECO:0000250}. FT DISULFID 3490 3513 {ECO:0000250}. FT DISULFID 3664 3692 {ECO:0000250}. FT VAR_SEQ 493 561 NCDCSAAGTQGNACRKDPRVGRCLCKPNFQGTHCELCAPGF FT YGPGCQPCQCSSPGVADDRCDPDTGQCR -> SGVSLCRPG FT WSAVARSRLTSTSASWVRAILLPQSPEWLGLQAPATTPGQF FT FVFLVETGFHHVGQAGLEL (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_057343. FT VAR_SEQ 562 3695 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_057344. FT VARIANT 401 401 T -> A (in dbSNP:rs4925229). FT {ECO:0000269|PubMed:11821406, FT ECO:0000269|PubMed:15489334}. FT /FTId=VAR_047887. FT VARIANT 889 889 V -> M (in dbSNP:rs6062223). FT {ECO:0000269|PubMed:11572484}. FT /FTId=VAR_030847. FT VARIANT 1258 1258 M -> T (in dbSNP:rs3810548). FT {ECO:0000269|PubMed:11821406}. FT /FTId=VAR_030848. FT VARIANT 1367 1367 K -> E (in dbSNP:rs2427286). FT {ECO:0000269|PubMed:11572484, FT ECO:0000269|PubMed:11821406}. FT /FTId=VAR_030849. FT VARIANT 1434 1434 G -> A (in dbSNP:rs17750870). FT /FTId=VAR_030850. FT VARIANT 1667 1667 R -> W (in dbSNP:rs13039398). FT /FTId=VAR_030851. FT VARIANT 1671 1671 T -> M (in dbSNP:rs944893). FT /FTId=VAR_047888. FT VARIANT 1717 1717 H -> Y (in dbSNP:rs875379). FT /FTId=VAR_030852. FT VARIANT 1807 1807 F -> S (in dbSNP:rs2427284). FT {ECO:0000269|PubMed:11572484, FT ECO:0000269|PubMed:11821406}. FT /FTId=VAR_030853. FT VARIANT 1900 1900 V -> M (in dbSNP:rs2427283). FT {ECO:0000269|PubMed:11821406}. FT /FTId=VAR_030854. FT VARIANT 1908 1908 A -> T (in dbSNP:rs11698080). FT /FTId=VAR_030855. FT VARIANT 2036 2036 H -> R (in dbSNP:rs6143021). FT /FTId=VAR_030856. FT VARIANT 2053 2053 R -> H (in dbSNP:rs3737137). FT /FTId=VAR_030857. FT VARIANT 2062 2062 D -> N (in dbSNP:rs2274934). FT {ECO:0000269|PubMed:11821406, FT ECO:0000269|PubMed:9628581}. FT /FTId=VAR_030858. FT VARIANT 2226 2226 R -> H (in dbSNP:rs2297587). FT /FTId=VAR_030859. FT VARIANT 3079 3079 R -> W (in dbSNP:rs944895). FT {ECO:0000269|PubMed:11821406, FT ECO:0000269|PubMed:9271224, FT ECO:0000269|PubMed:9628581}. FT /FTId=VAR_030860. FT CONFLICT 956 956 T -> A (in Ref. 1; AAM12527). FT {ECO:0000305}. FT HELIX 2677 2700 {ECO:0000244|PDB:5XAU}. FT HELIX 2707 2731 {ECO:0000244|PDB:5XAU}. FT STRAND 2737 2742 {ECO:0000244|PDB:5XAU}. FT STRAND 2744 2747 {ECO:0000244|PDB:5XAU}. FT HELIX 2754 2756 {ECO:0000244|PDB:5XAU}. FT STRAND 2759 2767 {ECO:0000244|PDB:5XAU}. FT STRAND 2780 2786 {ECO:0000244|PDB:5XAU}. FT STRAND 2792 2800 {ECO:0000244|PDB:5XAU}. FT STRAND 2803 2809 {ECO:0000244|PDB:5XAU}. FT STRAND 2815 2819 {ECO:0000244|PDB:5XAU}. FT STRAND 2829 2836 {ECO:0000244|PDB:5XAU}. FT STRAND 2839 2846 {ECO:0000244|PDB:5XAU}. FT STRAND 2848 2850 {ECO:0000244|PDB:5XAU}. FT STRAND 2852 2859 {ECO:0000244|PDB:5XAU}. FT STRAND 2861 2863 {ECO:0000244|PDB:5XAU}. FT STRAND 2875 2879 {ECO:0000244|PDB:5XAU}. FT HELIX 2889 2891 {ECO:0000244|PDB:5XAU}. FT STRAND 2897 2905 {ECO:0000244|PDB:5XAU}. FT STRAND 2914 2920 {ECO:0000244|PDB:5XAU}. FT TURN 2923 2925 {ECO:0000244|PDB:5XAU}. FT HELIX 2938 2942 {ECO:0000244|PDB:5XAU}. FT STRAND 2944 2955 {ECO:0000244|PDB:5XAU}. FT STRAND 2962 2972 {ECO:0000244|PDB:5XAU}. FT STRAND 2975 2984 {ECO:0000244|PDB:5XAU}. FT STRAND 2987 2994 {ECO:0000244|PDB:5XAU}. FT STRAND 2997 3006 {ECO:0000244|PDB:5XAU}. FT STRAND 3025 3032 {ECO:0000244|PDB:5XAU}. FT STRAND 3034 3036 {ECO:0000244|PDB:5XAU}. FT STRAND 3038 3043 {ECO:0000244|PDB:5XAU}. FT STRAND 3046 3052 {ECO:0000244|PDB:5XAU}. FT HELIX 3057 3059 {ECO:0000244|PDB:5XAU}. FT STRAND 3062 3066 {ECO:0000244|PDB:5XAU}. FT HELIX 3070 3072 {ECO:0000244|PDB:5XAU}. FT HELIX 3075 3080 {ECO:0000244|PDB:5XAU}. FT STRAND 3088 3096 {ECO:0000244|PDB:5XAU}. FT HELIX 3103 3105 {ECO:0000244|PDB:5XAU}. FT STRAND 3109 3113 {ECO:0000244|PDB:5XAU}. FT HELIX 3117 3120 {ECO:0000244|PDB:5XAU}. FT STRAND 3124 3136 {ECO:0000244|PDB:5XAU}. FT STRAND 3147 3154 {ECO:0000244|PDB:5XAU}. FT STRAND 3158 3167 {ECO:0000244|PDB:5XAU}. FT STRAND 3170 3177 {ECO:0000244|PDB:5XAU}. FT STRAND 3180 3185 {ECO:0000244|PDB:5XAU}. FT STRAND 3188 3191 {ECO:0000244|PDB:5XAU}. FT STRAND 3198 3200 {ECO:0000244|PDB:5XAU}. FT STRAND 3202 3209 {ECO:0000244|PDB:5XAU}. FT STRAND 3212 3217 {ECO:0000244|PDB:5XAU}. FT STRAND 3220 3225 {ECO:0000244|PDB:5XAU}. FT STRAND 3240 3248 {ECO:0000244|PDB:5XAU}. FT STRAND 3259 3267 {ECO:0000244|PDB:5XAU}. FT STRAND 3270 3272 {ECO:0000244|PDB:5XAU}. FT STRAND 3285 3291 {ECO:0000244|PDB:5XAU}. SQ SEQUENCE 3695 AA; 399737 MW; B13C479B55282E3C CRC64; MAKRLCAGSA LCVRGPRGPA PLLLVGLALL GAARAREEAG GGFSLHPPYF NLAEGARIAA SATCGEEAPA RGSPRPTEDL YCKLVGGPVA GGDPNQTIRG QYCDICTAAN SNKAHPASNA IDGTERWWQS PPLSRGLEYN EVNVTLDLGQ VFHVAYVLIK FANSPRPDLW VLERSMDFGR TYQPWQFFAS SKRDCLERFG PQTLERITRD DAAICTTEYS RIVPLENGEI VVSLVNGRPG AMNFSYSPLL REFTKATNVR LRFLRTNTLL GHLMGKALRD PTVTRRYYYS IKDISIGGRC VCHGHADACD AKDPTDPFRL QCTCQHNTCG GTCDRCCPGF NQQPWKPATA NSANECQSCN CYGHATDCYY DPEVDRRRAS QSLDGTYQGG GVCIDCQHHT TGVNCERCLP GFYRSPNHPL DSPHVCRRCN CESDFTDGTC EDLTGRCYCR PNFSGERCDV CAEGFTGFPS CYPTPSSSND TREQVLPAGQ IVNCDCSAAG TQGNACRKDP RVGRCLCKPN FQGTHCELCA PGFYGPGCQP CQCSSPGVAD DRCDPDTGQC RCRVGFEGAT CDRCAPGYFH FPLCQLCGCS PAGTLPEGCD EAGRCLCQPE FAGPHCDRCR PGYHGFPNCQ ACTCDPRGAL DQLCGAGGLC RCRPGYTGTA CQECSPGFHG FPSCVPCHCS AEGSLHAACD PRSGQCSCRP RVTGLRCDTC VPGAYNFPYC EAGSCHPAGL APVDPALPEA QVPCMCRAHV EGPSCDRCKP GFWGLSPSNP EGCTRCSCDL RGTLGGVAEC QPGTGQCFCK PHVCGQACAS CKDGFFGLDQ ADYFGCRSCR CDIGGALGQS CEPRTGVCRC RPNTQGPTCS EPARDHYLPD LHHLRLELEE AATPEGHAVR FGFNPLEFEN FSWRGYAQMA PVQPRIVARL NLTSPDLFWL VFRYVNRGAM SVSGRVSVRE EGRSATCANC TAQSQPVAFP PSTEPAFITV PQRGFGEPFV LNPGTWALRV EAEGVLLDYV VLLPSAYYEA ALLQLRVTEA CTYRPSAQQS GDNCLLYTHL PLDGFPSAAG LEALCRQDNS LPRPCPTEQL SPSHPPLITC TGSDVDVQLQ VAVPQPGRYA LVVEYANEDA RQEVGVAVHT PQRAPQQGLL SLHPCLYSTL CRGTARDTQD HLAVFHLDSE ASVRLTAEQA RFFLHGVTLV PIEEFSPEFV EPRVSCISSH GAFGPNSAAC LPSRFPKPPQ PIILRDCQVI PLPPGLPLTH AQDLTPAMSP AGPRPRPPTA VDPDAEPTLL REPQATVVFT THVPTLGRYA FLLHGYQPAH PTFPVEVLIN AGRVWQGHAN ASFCPHGYGC RTLVVCEGQA LLDVTHSELT VTVRVPKGRW LWLDYVLVVP ENVYSFGYLR EEPLDKSYDF ISHCAAQGYH ISPSSSSLFC RNAAASLSLF YNNGARPCGC HEVGATGPTC EPFGGQCPCH AHVIGRDCSR CATGYWGFPN CRPCDCGARL CDELTGQCIC PPRTIPPDCL LCQPQTFGCH PLVGCEECNC SGPGIQELTD PTCDTDSGQC KCRPNVTGRR CDTCSPGFHG YPRCRPCDCH EAGTAPGVCD PLTGQCYCKE NVQGPKCDQC SLGTFSLDAA NPKGCTRCFC FGATERCRSS SYTRQEFVDM EGWVLLSTDR QVVPHERQPG TEMLRADLRH VPEAVPEAFP ELYWQAPPSY LGDRVSSYGG TLRYELHSET QRGDVFVPME SRPDVVLQGN QMSITFLEPA YPTPGHVHRG QLQLVEGNFR HTETRNTVSR EELMMVLASL EQLQIRALFS QISSAVFLRR VALEVASPAG QGALASNVEL CLCPASYRGD SCQECAPGFY RDVKGLFLGR CVPCQCHGHS DRCLPGSGVC VDCQHNTEGA HCERCQAGFV SSRDDPSAPC VSCPCPLSVP SNNFAEGCVL RGGRTQCLCK PGYAGASCER CAPGFFGNPL VLGSSCQPCD CSGNGDPNLL FSDCDPLTGA CRGCLRHTTG PRCEICAPGF YGNALLPGNC TRCDCTPCGT EACDPHSGHC LCKAGVTGRR CDRCQEGHFG FDGCGGCRPC ACGPAAEGSE CHPQSGQCHC RPGTMGPQCR ECAPGYWGLP EQGCRRCQCP GGRCDPHTGR CNCPPGLSGE RCDTCSQQHQ VPVPGGPVGH SIHCEVCDHC VVLLLDDLER AGALLPAIHE QLRGINASSM AWARLHRLNA SIADLQSQLR SPLGPRHETA QQLEVLEQQS TSLGQDARRL GGQAVGTRDQ ASQLLAGTEA TLGHAKTLLA AIRAVDRTLS ELMSQTGHLG LANASAPSGE QLLRTLAEVE RLLWEMRARD LGAPQAAAEA ELAAAQRLLA RVQEQLSSLW EENQALATQT RDRLAQHEAG LMDLREALNR AVDATREAQE LNSRNQERLE EALQRKQELS RDNATLQATL HAARDTLASV FRLLHSLDQA KEELERLAAS LDGARTPLLQ RMQTFSPAGS KLRLVEAAEA HAQQLGQLAL NLSSIILDVN QDRLTQRAIE ASNAYSRILQ AVQAAEDAAG QALQQADHTW ATVVRQGLVD RAQQLLANST ALEEAMLQEQ QRLGLVWAAL QGARTQLRDV RAKKDQLEAH IQAAQAMLAM DTDETSKKIA HAKAVAAEAQ DTATRVQSQL QAMQENVERW QGQYEGLRGQ DLGQAVLDAG HSVSTLEKTL PQLLAKLSIL ENRGVHNASL ALSASIGRVR ELIAQARGAA SKVKVPMKFN GRSGVQLRTP RDLADLAAYT ALKFYLQGPE PEPGQGTEDR FVMYMGSRQA TGDYMGVSLR DKKVHWVYQL GEAGPAVLSI DEDIGEQFAA VSLDRTLQFG HMSVTVERQM IQETKGDTVA PGAEGLLNLR PDDFVFYVGG YPSTFTPPPL LRFPGYRGCI EMDTLNEEVV SLYNFERTFQ LDTAVDRPCA RSKSTGDPWL TDGSYLDGTG FARISFDSQI STTKRFEQEL RLVSYSGVLF FLKQQSQFLC LAVQEGSLVL LYDFGAGLKK AVPLQPPPPL TSASKAIQVF LLGGSRKRVL VRVERATVYS VEQDNDLELA DAYYLGGVPP DQLPPSLRRL FPTGGSVRGC VKGIKALGKY VDLKRLNTTG VSAGCTADLL VGRAMTFHGH GFLRLALSNV APLTGNVYSG FGFHSAQDSA LLYYRASPDG LCQVSLQQGR VSLQLLRTEV KTQAGFADGA PHYVAFYSNA TGVWLYVDDQ LQQMKPHRGP PPELQPQPEG PPRLLLGGLP ESGTIYNFSG CISNVFVQRL LGPQRVFDLQ QNLGSVNVST GCAPALQAQT PGLGPRGLQA TARKASRRSR QPARHPACML PPHLRTTRDS YQFGGSLSSH LEFVGILARH RNWPSLSMHV LPRSSRGLLL FTARLRPGSP SLALFLSNGH FVAQMEGLGT RLRAQSRQRS RPGRWHKVSV RWEKNRILLV TDGARAWSQE GPHRQHQGAE HPQPHTLFVG GLPASSHSSK LPVTVGFSGC VKRLRLHGRP LGAPTRMAGV TPCILGPLEA GLFFPGSGGV ITLDLPGATL PDVGLELEVR PLAVTGLIFH LGQARTPPYL QLQVTEKQVL LRADDGAGEF STSVTRPSVL CDGQWHRLAV MKSGNVLRLE VDAQSNHTVG PLLAAAAGAP APLYLGGLPE PMAVQPWPPA YCGCMRRLAV NRSPVAMTRS VEVHGAVGAS GCPAA //