ID A2ML1_HUMAN Reviewed; 1454 AA. AC A8K2U0; B5MDD1; B7Z7V4; D3DUV3; F5H2Z2; Q2M224; Q6ZW52; Q6ZW53; AC Q8N1M4; Q96LQ8; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 13-FEB-2019, entry version 100. DE RecName: Full=Alpha-2-macroglobulin-like protein 1; DE AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 9; DE Flags: Precursor; GN Name=A2ML1 {ECO:0000312|EMBL:AAI12132.1}; GN Synonyms=CPAMD9 {ECO:0000312|HGNC:HGNC:23336}; 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] {ECO:0000312|EMBL:BAF83044.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND RP VARIANTS GLU-850; TRP-1122; ARG-1229; VAL-1257 AND MET-1312. RC TISSUE=Brain {ECO:0000312|EMBL:BAB71612.1}, Testis, and RC Tongue {ECO:0000312|EMBL:BAF83044.1}; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS RP GLU-850; TRP-1122; ARG-1229 AND VAL-1257. RC TISSUE=Cervix; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLU-850; RP TRP-1122; ARG-1229 AND VAL-1257. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1290-1454. RC TISSUE=Brain {ECO:0000312|EMBL:AAI12132.1}; 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 [6] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX PubMed=16298998; DOI=10.1074/jbc.M508017200; RA Galliano M.-F., Toulza E., Gallinaro H., Jonca N., Ishida-Yamamoto A., RA Serre G., Guerrin M.; RT "A novel protease inhibitor of the alpha2-macroglobulin family RT expressed in the human epidermis."; RL J. Biol. Chem. 281:5780-5789(2006). RN [7] RP INVOLVEMENT IN OM, AND VARIANTS 255-GLN--GLU-1454 DEL; ALA-296; RP ARG-356; 893-ARG--GLU-1454 DEL; 972-GLU--GLU-1454 DEL; TRP-1001 AND RP VAL-1431. RX PubMed=26121085; DOI=10.1038/ng.3347; RG University of Washington Center for Mendelian Genomics; RA Santos-Cortez R.L., Chiong C.M., Reyes-Quintos M.R., Tantoco M.L., RA Wang X., Acharya A., Abbe I., Giese A.P., Smith J.D., Allen E.K., RA Li B., Cutiongco-de la Paz E.M., Garcia M.C., Llanes E.G., Labra P.J., RA Gloria-Cruz T.L., Chan A.L., Wang G.T., Daly K.A., Shendure J., RA Bamshad M.J., Nickerson D.A., Patel J.A., Riazuddin S., Sale M.M., RA Chonmaitree T., Ahmed Z.M., Abes G.T., Leal S.M.; RT "Rare A2ML1 variants confer susceptibility to otitis media."; RL Nat. Genet. 47:917-920(2015). CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a CC unique 'trapping' mechanism. This protein has a peptide stretch, CC called the 'bait region' which contains specific cleavage sites CC for different proteinases. When a proteinase cleaves the bait CC region, a conformational change is induced in the protein which CC traps the proteinase. The entrapped enzyme remains active against CC low molecular weight substrates (activity against high molecular CC weight substrates is greatly reduced). Following cleavage in the CC bait region a thioester bond is hydrolyzed and mediates the CC covalent binding of the protein to the proteinase (By similarity). CC Displays inhibitory activity against chymotrypsin, papain, CC thermolysin, subtilisin A and, to a lesser extent, elastase but CC not trypsin. May play an important role during desquamation by CC inhibiting extracellular proteases. {ECO:0000250|UniProtKB:P01023, CC ECO:0000269|PubMed:16298998}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16298998}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16298998}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=A8K2U0-1; Sequence=Displayed; CC Name=2; CC IsoId=A8K2U0-2; Sequence=VSP_057135; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: In the epidermis, expressed predominantly in CC the granular layer at the apical edge of keratinocytes (at protein CC level). Also detected in placenta, testis and thymus but not in CC epithelia of kidney, lung, small intestine or colon. CC {ECO:0000269|PubMed:16298998}. CC -!- DEVELOPMENTAL STAGE: Up-regulated during keratinocyte CC differentiation. {ECO:0000269|PubMed:16298998}. CC -!- DISEASE: Otitis media (OM) [MIM:166760]: An inflammation of the CC middle ear resulting in earache, fever, hearing disturbance, and CC vertigo. {ECO:0000269|PubMed:26121085}. Note=Disease CC susceptibility is associated with variations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2- CC macroglobulin) family. {ECO:0000255}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB71612.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC04793.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC85653.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC85654.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AK057908; BAB71612.1; ALT_INIT; mRNA. DR EMBL; AK096448; BAC04793.1; ALT_INIT; mRNA. DR EMBL; AK123591; BAC85653.1; ALT_INIT; mRNA. DR EMBL; AK123592; BAC85654.1; ALT_INIT; mRNA. DR EMBL; AK290355; BAF83044.1; -; mRNA. DR EMBL; AK302555; BAH13740.1; -; mRNA. DR EMBL; AL832139; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC006513; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC006581; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471116; EAW88603.1; -; Genomic_DNA. DR EMBL; CH471116; EAW88606.1; -; Genomic_DNA. DR EMBL; BC093840; AAH93840.2; -; mRNA. DR EMBL; BC112131; AAI12132.1; -; mRNA. DR CCDS; CCDS73439.1; -. [A8K2U0-2] DR CCDS; CCDS8596.2; -. [A8K2U0-1] DR RefSeq; NP_001269353.1; NM_001282424.2. DR RefSeq; XP_016874359.1; XM_017018870.1. [A8K2U0-1] DR UniGene; Hs.620532; -. DR ProteinModelPortal; A8K2U0; -. DR IntAct; A8K2U0; 5. DR MINT; A8K2U0; -. DR STRING; 9606.ENSP00000299698; -. DR MEROPS; I39.007; -. DR GlyConnect; 1003; -. DR iPTMnet; A8K2U0; -. DR PhosphoSitePlus; A8K2U0; -. DR BioMuta; A2ML1; -. DR EPD; A8K2U0; -. DR jPOST; A8K2U0; -. DR MaxQB; A8K2U0; -. DR PaxDb; A8K2U0; -. DR PRIDE; A8K2U0; -. DR ProteomicsDB; 1852; -. DR Ensembl; ENST00000299698; ENSP00000299698; ENSG00000166535. [A8K2U0-1] DR Ensembl; ENST00000539547; ENSP00000438292; ENSG00000166535. [A8K2U0-2] DR GeneID; 144568; -. DR KEGG; hsa:144568; -. DR UCSC; uc001quz.6; human. [A8K2U0-1] DR CTD; 144568; -. DR DisGeNET; 144568; -. DR EuPathDB; HostDB:ENSG00000166535.19; -. DR GeneCards; A2ML1; -. DR HGNC; HGNC:23336; A2ML1. DR HPA; HPA038847; -. DR HPA; HPA038848; -. DR MalaCards; A2ML1; -. DR MIM; 166760; phenotype. DR MIM; 610627; gene. DR neXtProt; NX_A8K2U0; -. DR OpenTargets; ENSG00000166535; -. DR Orphanet; 648; Noonan syndrome. DR eggNOG; KOG1366; Eukaryota. DR eggNOG; ENOG410XRED; LUCA. DR GeneTree; ENSGT00940000163018; -. DR HOVERGEN; HBG000039; -. DR InParanoid; A8K2U0; -. DR OMA; VSVCQKA; -. DR OrthoDB; 354230at2759; -. DR PhylomeDB; A8K2U0; -. DR TreeFam; TF313285; -. DR ChiTaRS; A2ML1; human. DR GenomeRNAi; 144568; -. DR PRO; PR:A8K2U0; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; ENSG00000166535; Expressed in 112 organ(s), highest expression level in mouth mucosa. DR ExpressionAtlas; A8K2U0; baseline and differential. DR Genevisible; A8K2U0; HS. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0030414; F:peptidase inhibitor activity; IDA:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. DR GO; GO:0052548; P:regulation of endopeptidase activity; IDA:UniProtKB. DR Gene3D; 2.60.40.10; -; 2. DR Gene3D; 2.60.40.690; -; 1. DR InterPro; IPR009048; A-macroglobulin_rcpt-bd. DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf. DR InterPro; IPR011625; A2M_N_BRD. DR InterPro; IPR011626; Alpha-macroglobulin_TED. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR001599; Macroglobln_a2. DR InterPro; IPR019742; MacrogloblnA2_CS. DR InterPro; IPR002890; MG2. DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase. DR Pfam; PF00207; A2M; 1. DR Pfam; PF07703; A2M_BRD; 1. DR Pfam; PF07677; A2M_recep; 1. DR Pfam; PF01835; MG2; 1. DR Pfam; PF07678; TED_complement; 1. DR SMART; SM01360; A2M; 1. DR SMART; SM01359; A2M_N_2; 1. DR SMART; SM01361; A2M_recep; 1. DR SUPFAM; SSF48239; SSF48239; 1. DR SUPFAM; SSF49410; SSF49410; 1. DR SUPFAM; SSF81296; SSF81296; 1. DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1. PE 1: Evidence at protein level; KW Alternative splicing; Bait region; Complete proteome; Disulfide bond; KW Glycoprotein; Polymorphism; Protease inhibitor; Reference proteome; KW Secreted; Serine protease inhibitor; Signal; Thioester bond. FT SIGNAL 1 17 {ECO:0000255}. FT CHAIN 18 1454 Alpha-2-macroglobulin-like protein 1. FT {ECO:0000255}. FT /FTId=PRO_0000318074. FT REGION 695 726 Bait region. {ECO:0000255}. FT CARBOHYD 120 120 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 281 281 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 409 409 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 857 857 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1020 1020 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 40 78 {ECO:0000250|UniProtKB:P01023}. FT DISULFID 241 291 {ECO:0000250|UniProtKB:P01023}. FT DISULFID 259 279 {ECO:0000250|UniProtKB:P01023}. FT DISULFID 464 557 {ECO:0000250|UniProtKB:P01023}. FT DISULFID 589 769 {ECO:0000250|UniProtKB:P01023}. FT DISULFID 819 847 {ECO:0000250|UniProtKB:P01023}. FT DISULFID 845 881 {ECO:0000250|UniProtKB:P01023}. FT DISULFID 919 1307 {ECO:0000250|UniProtKB:P01023}. FT DISULFID 1075 1123 {ECO:0000250|UniProtKB:P01023}. FT DISULFID 1338 1453 {ECO:0000250|UniProtKB:P01023}. FT CROSSLNK 970 973 Isoglutamyl cysteine thioester (Cys-Gln). FT {ECO:0000250|UniProtKB:P01023}. FT VAR_SEQ 2 492 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_057135. FT VARIANT 207 207 G -> R (in dbSNP:rs11047499). FT /FTId=VAR_055463. FT VARIANT 255 1454 Missing (risk factor for otitis media). FT {ECO:0000269|PubMed:26121085}. FT /FTId=VAR_081009. FT VARIANT 296 296 V -> A (in dbSNP:rs192888493). FT {ECO:0000269|PubMed:26121085}. FT /FTId=VAR_081010. FT VARIANT 356 356 P -> R (may be a risk factor for otitis FT media; dbSNP:rs863224953). FT {ECO:0000269|PubMed:26121085}. FT /FTId=VAR_081011. FT VARIANT 850 850 D -> E (in dbSNP:rs1860926). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17974005, FT ECO:0000269|Ref.4}. FT /FTId=VAR_059083. FT VARIANT 893 1454 Missing (risk factor for otitis media). FT {ECO:0000269|PubMed:26121085}. FT /FTId=VAR_081012. FT VARIANT 970 970 C -> Y (in dbSNP:rs1558526). FT /FTId=VAR_055464. FT VARIANT 972 1454 Missing (risk factor for otitis media). FT {ECO:0000269|PubMed:26121085}. FT /FTId=VAR_081013. FT VARIANT 1001 1001 R -> W (may be a risk factor for otitis FT media; dbSNP:rs201725377). FT {ECO:0000269|PubMed:26121085}. FT /FTId=VAR_081014. FT VARIANT 1122 1122 R -> W (in dbSNP:rs1860967). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17974005, FT ECO:0000269|Ref.4}. FT /FTId=VAR_071854. FT VARIANT 1131 1131 T -> M (in dbSNP:rs7959680). FT /FTId=VAR_055465. FT VARIANT 1229 1229 H -> R (in dbSNP:rs10219561). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17974005, FT ECO:0000269|Ref.4}. FT /FTId=VAR_059084. FT VARIANT 1257 1257 M -> V (in dbSNP:rs7308811). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:17974005, FT ECO:0000269|Ref.4}. FT /FTId=VAR_071855. FT VARIANT 1312 1312 T -> M (in dbSNP:rs201083574). FT {ECO:0000269|PubMed:14702039}. FT /FTId=VAR_071856. FT VARIANT 1412 1412 T -> A (in dbSNP:rs7315591). FT /FTId=VAR_055466. FT VARIANT 1431 1431 A -> V (in dbSNP:rs863224955). FT {ECO:0000269|PubMed:26121085}. FT /FTId=VAR_081015. FT CONFLICT 733 733 F -> L (in Ref. 1; BAC85654/BAF83044). FT {ECO:0000305}. FT CONFLICT 748 748 G -> E (in Ref. 2; AL832139). FT {ECO:0000305}. FT CONFLICT 1150 1150 M -> I (in Ref. 1; BAF83044). FT {ECO:0000305}. FT CONFLICT 1248 1248 L -> P (in Ref. 1; BAC85654). FT {ECO:0000305}. FT CONFLICT 1452 1452 P -> L (in Ref. 2; AL832139). FT {ECO:0000305}. SQ SEQUENCE 1454 AA; 161107 MW; 15ED65D000834E33 CRC64; MWAQLLLGML ALSPAIAEEL PNYLVTLPAR LNFPSVQKVC LDLSPGYSDV KFTVTLETKD KTQKLLEYSG LKKRHLHCIS FLVPPPAGGT EEVATIRVSG VGNNISFEEK KKVLIQRQGN GTFVQTDKPL YTPGQQVYFR IVTMDSNFVP VNDKYSMVEL QDPNSNRIAQ WLEVVPEQGI VDLSFQLAPE AMLGTYTVAV AEGKTFGTFS VEEYVLPKFK VEVVEPKELS TVQESFLVKI CCRYTYGKPM LGAVQVSVCQ KANTYWYREV EREQLPDKCR NLSGQTDKTG CFSAPVDMAT FDLIGYAYSH QINIVATVVE EGTGVEANAT QNIYISPQMG SMTFEDTSNF YHPNFPFSGK IRVRGHDDSF LKNHLVFLVI YGTNGTFNQT LVTDNNGLAP FTLETSGWNG TDVSLEGKFQ MEDLVYNPEQ VPRYYQNAYL HLRPFYSTTR SFLGIHRLNG PLKCGQPQEV LVDYYIDPAD ASPDQEISFS YYLIGKGSLV MEGQKHLNSK KKGLKASFSL SLTFTSRLAP DPSLVIYAIF PSGGVVADKI QFSVEMCFDN QVSLGFSPSQ QLPGAEVELQ LQAAPGSLCA LRAVDESVLL LRPDRELSNR SVYGMFPFWY GHYPYQVAEY DQCPVSGPWD FPQPLIDPMP QGHSSQRSII WRPSFSEGTD LFSFFRDVGL KILSNAKIKK PVDCSHRSPE YSTAMGAGGG HPEAFESSTP LHQAEDSQVR QYFPETWLWD LFPIGNSGKE AVHVTVPDAI TEWKAMSFCT SQSRGFGLSP TVGLTAFKPF FVDLTLPYSV VRGESFRLTA TIFNYLKDCI RVQTDLAKSH EYQLESWADS QTSSCLCADD AKTHHWNITA VKLGHINFTI STKILDSNEP CGGQKGFVPQ KGRSDTLIKP VLVKPEGVLV EKTHSSLLCP KGKVASESVS LELPVDIVPD STKAYVTVLG DIMGTALQNL DGLVQMPSGC GEQNMVLFAP IIYVLQYLEK AGLLTEEIRS RAVGFLEIGY QKELMYKHSN GSYSAFGERD GNGNTWLTAF VTKCFGQAQK FIFIDPKNIQ DALKWMAGNQ LPSGCYANVG NLLHTAMKGG VDDEVSLTAY VTAALLEMGK DVDDPMVSQG LRCLKNSATS TTNLYTQALL AYIFSLAGEM DIRNILLKQL DQQAIISGES IYWSQKPTPS SNASPWSEPA AVDVELTAYA LLAQLTKPSL TQKEIAKATS IVAWLAKQHN AYGGFSSTQD TVVALQALAK YATTAYMPSE EINLVVKSTE NFQRTFNIQS VNRLVFQQDT LPNVPGMYTL EASGQGCVYV QTVLRYNILP PTNMKTFSLS VEIGKARCEQ PTSPRSLTLT IHTSYVGSRS SSNMAIVEVK MLSGFSPMEG TNQLLLQQPL VKKVEFGTDT LNIYLDELIK NTQTYTFTIS QSVLVTNLKP ATIKVYDYYL PDEQATIQYS DPCE //