ID PIGR_HUMAN Reviewed; 764 AA. AC P01833; Q68D81; Q8IZY7; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 26-JUN-2007, sequence version 4. DT 13-FEB-2019, entry version 190. DE RecName: Full=Polymeric immunoglobulin receptor; DE Short=PIgR; DE Short=Poly-Ig receptor; DE AltName: Full=Hepatocellular carcinoma-associated protein TB6; DE Contains: DE RecName: Full=Secretory component; DE Flags: Precursor; GN Name=PIGR; 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], AND VARIANT SER-365. RX PubMed=1682231; DOI=10.1007/BF00201717; RA Krajci P., Grzeschik K.H., Geurts van Kessel A.H., Olaisen B., RA Brandtzaeg P.; RT "The human transmembrane secretory component (poly-Ig receptor): RT molecular cloning, restriction fragment length polymorphism and RT chromosomal sublocalization."; RL Hum. Genet. 87:642-648(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-365. RX PubMed=1355431; DOI=10.1002/eji.1830220920; RA Krajci P., Kvale D., Tasken K., Brandtzaeg P.; RT "Molecular cloning and exon-intron mapping of the gene encoding human RT transmembrane secretory component (the poly-Ig receptor)."; RL Eur. J. Immunol. 22:2309-2315(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Dong X., Pang X., Cheng W.; RT "Cloning and characterization of hepatocellular carcinoma associated- RT genes."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-365. RC TISSUE=Small intestine; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 72-764, AND VARIANT SER-365. RX PubMed=2920039; DOI=10.1016/0006-291X(89)92790-3; RA Krajci P., Solberg R., Sandberg M., Oyen O., Jahnsen T., RA Brandtzaeg P.; RT "Molecular cloning of the human transmembrane secretory component RT (poly-Ig receptor) and its mRNA expression in human tissues."; RL Biochem. Biophys. Res. Commun. 158:783-789(1989). RN [6] RP PROTEIN SEQUENCE OF 19-577, VARIANT SER-365, DISULFIDE BONDS, AND RP GLYCOSYLATION AT ASN-83; ASN-90; ASN-135; ASN-186; ASN-421; ASN-469 RP AND ASN-499. RX PubMed=6526384; RA Eiffert H., Quentin E., Decker J., Hillemeir S., Hufschmidt M., RA Klingmueller D., Weber M.H., Hilschmann N.; RT "The primary structure of human free secretory component and the RT arrangement of disulfide bonds."; RL Hoppe-Seyler's Z. Physiol. Chem. 365:1489-1495(1984). RN [7] RP PROTEIN SEQUENCE OF 19-577, AND VARIANT SER-365. RX PubMed=1859628; RA Eiffert H., Quentin E., Wiederhold M., Hillemeir S., Decker J., RA Weber M., Hilschmann N.; RT "Determination of the molecular structure of the human free secretory RT component."; RL Biol. Chem. Hoppe-Seyler 372:119-128(1991). RN [8] RP PROTEIN SEQUENCE OF 118-138; 212-230; 232-268; 273-288 AND 578-603. RX PubMed=9237679; DOI=10.1016/S0014-5793(97)00629-7; RA Hughes G.J., Frutiger S., Savoy L.-A., Reason A.J., Morris H.R., RA Jaton J.-C.; RT "Human free secretory component is composed of the first 585 amino RT acid residues of the polymeric immunoglobulin receptor."; RL FEBS Lett. 410:443-446(1997). RN [9] RP PROTEIN SEQUENCE OF 573-648, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Tear; RX PubMed=25946035; DOI=10.1021/acs.jproteome.5b00179; RA Azkargorta M., Soria J., Ojeda C., Guzman F., Acera A., Iloro I., RA Suarez T., Elortza F.; RT "Human basal tear peptidome characterization by CID, HCD, and ETD RT followed by in silico and in vitro analyses for antimicrobial peptide RT identification."; RL J. Proteome Res. 14:2649-2658(2015). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-421 AND RP ASN-469. RC TISSUE=Bile; RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200; RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; RT "A proteomic analysis of human bile."; RL Mol. Cell. Proteomics 3:715-728(2004). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90; ASN-421 AND ASN-469. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-186; RP ASN-421; ASN-469 AND ASN-499. RC TISSUE=Saliva; RX PubMed=16740002; DOI=10.1021/pr050492k; RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., RA Loo J.A.; RT "Identification of N-linked glycoproteins in human saliva by RT glycoprotein capture and mass spectrometry."; RL J. Proteome Res. 5:1493-1503(2006). RN [13] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-90; ASN-135; RP ASN-186; ASN-421; ASN-469 AND ASN-499. RC TISSUE=Milk; RX PubMed=18780401; DOI=10.1002/pmic.200701057; RA Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; RT "Identification of N-linked glycoproteins in human milk by hydrophilic RT interaction liquid chromatography and mass spectrometry."; RL Proteomics 8:3833-3847(2008). RN [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-421 AND ASN-469. 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 [15] RP GLYCOSYLATION AT ASN-469. RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core RT fucosylated glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [16] 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 [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [18] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 19-127. RX PubMed=15530357; DOI=10.1016/j.str.2004.09.006; RA Hamburger A.E., West A.P. Jr., Bjorkman P.J.; RT "Crystal structure of a polymeric immunoglobulin binding fragment of RT the human polymeric immunoglobulin receptor."; RL Structure 12:1925-1935(2004). CC -!- FUNCTION: This receptor binds polymeric IgA and IgM at the CC basolateral surface of epithelial cells. The complex is then CC transported across the cell to be secreted at the apical surface. CC During this process a cleavage occurs that separates the CC extracellular (known as the secretory component) from the CC transmembrane segment. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. CC -!- SUBCELLULAR LOCATION: Secretory component: Secreted. CC -!- PTM: N-glycosylation is not necessary for Ig binding. CC {ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, CC ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:18780401, CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:6526384}. 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; S62403; AAB20203.1; -; mRNA. DR EMBL; S43449; AAB23176.1; -; Genomic_DNA. DR EMBL; S43437; AAB23176.1; JOINED; Genomic_DNA. DR EMBL; S43441; AAB23176.1; JOINED; Genomic_DNA. DR EMBL; S43442; AAB23176.1; JOINED; Genomic_DNA. DR EMBL; S43443; AAB23176.1; JOINED; Genomic_DNA. DR EMBL; S43444; AAB23176.1; JOINED; Genomic_DNA. DR EMBL; S43445; AAB23176.1; JOINED; Genomic_DNA. DR EMBL; S43446; AAB23176.1; JOINED; Genomic_DNA. DR EMBL; S43447; AAB23176.1; JOINED; Genomic_DNA. DR EMBL; S43448; AAB23176.1; JOINED; Genomic_DNA. DR EMBL; AF272149; AAN65630.1; -; mRNA. DR EMBL; CR749533; CAH18339.1; -; mRNA. DR EMBL; M24559; AAA36102.1; -; mRNA. DR CCDS; CCDS1474.1; -. DR PIR; A46537; QRHUGS. DR RefSeq; NP_002635.2; NM_002644.3. DR RefSeq; XP_011507931.1; XM_011509629.1. DR UniGene; Hs.497589; -. DR PDB; 1XED; X-ray; 1.90 A; A/B/C/D/E/F=19-127. DR PDB; 2OCW; X-ray; -; A=19-603. DR PDB; 3CHN; Other; 1.00 A; J=353-458, S=19-603. DR PDB; 3CM9; Other; 1.00 A; J=353-458, S=19-603. DR PDB; 5D4K; X-ray; 2.60 A; A/B=19-565. DR PDBsum; 1XED; -. DR PDBsum; 2OCW; -. DR PDBsum; 3CHN; -. DR PDBsum; 3CM9; -. DR PDBsum; 5D4K; -. DR ProteinModelPortal; P01833; -. DR SMR; P01833; -. DR BioGrid; 111302; 34. DR IntAct; P01833; 7. DR STRING; 9606.ENSP00000348888; -. DR GlyConnect; 550; -. DR iPTMnet; P01833; -. DR PhosphoSitePlus; P01833; -. DR UniCarbKB; P01833; -. DR BioMuta; PIGR; -. DR DMDM; 150421625; -. DR jPOST; P01833; -. DR PaxDb; P01833; -. DR PeptideAtlas; P01833; -. DR PRIDE; P01833; -. DR ProteomicsDB; 51489; -. DR Ensembl; ENST00000356495; ENSP00000348888; ENSG00000162896. DR GeneID; 5284; -. DR KEGG; hsa:5284; -. DR UCSC; uc001hez.4; human. DR CTD; 5284; -. DR DisGeNET; 5284; -. DR EuPathDB; HostDB:ENSG00000162896.5; -. DR GeneCards; PIGR; -. DR H-InvDB; HIX0028583; -. DR HGNC; HGNC:8968; PIGR. DR HPA; CAB009454; -. DR HPA; HPA006154; -. DR HPA; HPA012012; -. DR MIM; 173880; gene. DR neXtProt; NX_P01833; -. DR OpenTargets; ENSG00000162896; -. DR PharmGKB; PA33300; -. DR eggNOG; ENOG410IHXB; Eukaryota. DR eggNOG; ENOG41128ZA; LUCA. DR GeneTree; ENSGT00940000161667; -. DR HOGENOM; HOG000115545; -. DR HOVERGEN; HBG008199; -. DR InParanoid; P01833; -. DR KO; K13073; -. DR OMA; YWCGVKQ; -. DR OrthoDB; 1319689at2759; -. DR PhylomeDB; P01833; -. DR TreeFam; TF334441; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR ChiTaRS; PIGR; human. DR EvolutionaryTrace; P01833; -. DR GeneWiki; Polymeric_immunoglobulin_receptor; -. DR GenomeRNAi; 5284; -. DR PRO; PR:P01833; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000162896; Expressed in 148 organ(s), highest expression level in parotid gland. DR Genevisible; P01833; HS. DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0043235; C:receptor complex; IDA:MGI. DR GO; GO:0001792; F:polymeric immunoglobulin receptor activity; IDA:UniProtKB. DR GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IDA:UniProtKB. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0038093; P:Fc receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0002415; P:immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor; IDA:UniProtKB. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0043113; P:receptor clustering; IDA:UniProtKB. DR GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB. DR Gene3D; 2.60.40.10; -; 5. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR Pfam; PF07686; V-set; 5. DR SMART; SM00409; IG; 5. DR SMART; SM00406; IGv; 4. DR SUPFAM; SSF48726; SSF48726; 5. DR PROSITE; PS50835; IG_LIKE; 2. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism; KW Reference proteome; Repeat; Secreted; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 18 {ECO:0000269|PubMed:1859628, FT ECO:0000269|PubMed:6526384}. FT CHAIN 19 764 Polymeric immunoglobulin receptor. FT /FTId=PRO_0000014900. FT CHAIN 19 603 Secretory component. FT /FTId=PRO_0000014901. FT TOPO_DOM 19 638 Extracellular. {ECO:0000255}. FT TRANSMEM 639 661 Helical. {ECO:0000255}. FT TOPO_DOM 662 764 Cytoplasmic. {ECO:0000255}. FT DOMAIN 19 120 Ig-like V-type 1. FT DOMAIN 145 237 Ig-like V-type 2. FT DOMAIN 250 352 Ig-like V-type 3. FT DOMAIN 364 458 Ig-like V-type 4. FT DOMAIN 462 561 Ig-like V-type 5. FT MOD_RES 673 673 Phosphoserine. FT {ECO:0000250|UniProtKB:P15083}. FT MOD_RES 682 682 Phosphoserine. FT {ECO:0000250|UniProtKB:O70570}. FT MOD_RES 689 689 Phosphoserine. FT {ECO:0000250|UniProtKB:P15083}. FT MOD_RES 735 735 Phosphoserine. FT {ECO:0000250|UniProtKB:O70570}. FT CARBOHYD 83 83 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:15084671, FT ECO:0000269|PubMed:16740002, FT ECO:0000269|PubMed:18780401, FT ECO:0000269|PubMed:6526384}. FT CARBOHYD 90 90 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:15084671, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:16740002, FT ECO:0000269|PubMed:18780401, FT ECO:0000269|PubMed:6526384}. FT CARBOHYD 135 135 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:18780401, FT ECO:0000269|PubMed:6526384}. FT CARBOHYD 186 186 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16740002, FT ECO:0000269|PubMed:18780401, FT ECO:0000269|PubMed:6526384}. FT CARBOHYD 421 421 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:15084671, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:16740002, FT ECO:0000269|PubMed:18780401, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:6526384}. FT CARBOHYD 469 469 N-linked (GlcNAc...) (complex) FT asparagine. {ECO:0000269|PubMed:15084671, FT ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:16740002, FT ECO:0000269|PubMed:18780401, FT ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:6526384}. FT CARBOHYD 499 499 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16740002, FT ECO:0000269|PubMed:18780401, FT ECO:0000269|PubMed:6526384}. FT DISULFID 40 110 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:6526384}. FT DISULFID 56 64 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:6526384}. FT DISULFID 152 220 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:6526384}. FT DISULFID 257 325 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:6526384}. FT DISULFID 271 279 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:6526384}. FT DISULFID 371 441 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:6526384}. FT DISULFID 385 395 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:6526384}. FT DISULFID 482 544 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:6526384}. FT DISULFID 486 520 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:6526384}. FT DISULFID 496 503 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:6526384}. FT VARIANT 365 365 G -> S (in dbSNP:rs2275531). FT {ECO:0000269|PubMed:1355431, FT ECO:0000269|PubMed:1682231, FT ECO:0000269|PubMed:17974005, FT ECO:0000269|PubMed:1859628, FT ECO:0000269|PubMed:2920039, FT ECO:0000269|PubMed:6526384}. FT /FTId=VAR_025283. FT VARIANT 555 555 T -> I (in dbSNP:rs7542760). FT /FTId=VAR_032822. FT VARIANT 580 580 A -> V (in dbSNP:rs291102). FT /FTId=VAR_003920. FT CONFLICT 136 136 D -> Q (in Ref. 6; AA sequence and 7; AA FT sequence). {ECO:0000305}. FT CONFLICT 158 158 N -> D (in Ref. 6; AA sequence and 7; AA FT sequence). {ECO:0000305}. FT CONFLICT 208 209 NQ -> DE (in Ref. 6; AA sequence and 7; FT AA sequence). {ECO:0000305}. FT CONFLICT 229 229 Missing (in Ref. 6; AA sequence and 7; AA FT sequence). {ECO:0000305}. FT CONFLICT 234 234 D -> N (in Ref. 6; AA sequence and 7; AA FT sequence). {ECO:0000305}. FT CONFLICT 241 241 E -> Q (in Ref. 6; AA sequence and 7; AA FT sequence). {ECO:0000305}. FT CONFLICT 262 262 E -> Q (in Ref. 6; AA sequence and 7; AA FT sequence). {ECO:0000305}. FT CONFLICT 280 280 D -> N (in Ref. 6; AA sequence and 7; AA FT sequence). {ECO:0000305}. FT CONFLICT 392 392 N -> D (in Ref. 6; AA sequence and 7; AA FT sequence). {ECO:0000305}. FT CONFLICT 500 500 N -> D (in Ref. 6; AA sequence and 7; AA FT sequence). {ECO:0000305}. FT STRAND 26 31 {ECO:0000244|PDB:1XED}. FT STRAND 36 41 {ECO:0000244|PDB:1XED}. FT HELIX 46 50 {ECO:0000244|PDB:1XED}. FT STRAND 53 57 {ECO:0000244|PDB:1XED}. FT STRAND 60 62 {ECO:0000244|PDB:1XED}. FT STRAND 65 72 {ECO:0000244|PDB:1XED}. FT TURN 76 81 {ECO:0000244|PDB:1XED}. FT STRAND 82 87 {ECO:0000244|PDB:1XED}. FT TURN 88 91 {ECO:0000244|PDB:1XED}. FT STRAND 92 97 {ECO:0000244|PDB:1XED}. FT HELIX 102 104 {ECO:0000244|PDB:1XED}. FT STRAND 106 113 {ECO:0000244|PDB:1XED}. FT HELIX 115 117 {ECO:0000244|PDB:1XED}. FT STRAND 120 127 {ECO:0000244|PDB:1XED}. FT STRAND 136 143 {ECO:0000244|PDB:5D4K}. FT STRAND 148 153 {ECO:0000244|PDB:5D4K}. FT HELIX 156 158 {ECO:0000244|PDB:5D4K}. FT STRAND 163 178 {ECO:0000244|PDB:5D4K}. FT TURN 185 189 {ECO:0000244|PDB:5D4K}. FT STRAND 190 195 {ECO:0000244|PDB:5D4K}. FT STRAND 201 207 {ECO:0000244|PDB:5D4K}. FT HELIX 212 214 {ECO:0000244|PDB:5D4K}. FT STRAND 216 222 {ECO:0000244|PDB:5D4K}. FT STRAND 224 227 {ECO:0000244|PDB:5D4K}. FT STRAND 229 238 {ECO:0000244|PDB:5D4K}. FT STRAND 243 248 {ECO:0000244|PDB:5D4K}. FT STRAND 253 257 {ECO:0000244|PDB:5D4K}. FT TURN 262 265 {ECO:0000244|PDB:5D4K}. FT STRAND 268 273 {ECO:0000244|PDB:5D4K}. FT STRAND 275 277 {ECO:0000244|PDB:5D4K}. FT STRAND 279 287 {ECO:0000244|PDB:5D4K}. FT HELIX 291 293 {ECO:0000244|PDB:5D4K}. FT STRAND 296 299 {ECO:0000244|PDB:5D4K}. FT STRAND 308 312 {ECO:0000244|PDB:5D4K}. FT HELIX 317 319 {ECO:0000244|PDB:5D4K}. FT STRAND 321 327 {ECO:0000244|PDB:5D4K}. FT STRAND 339 347 {ECO:0000244|PDB:5D4K}. FT STRAND 357 361 {ECO:0000244|PDB:5D4K}. FT STRAND 365 372 {ECO:0000244|PDB:5D4K}. FT HELIX 375 377 {ECO:0000244|PDB:5D4K}. FT STRAND 383 386 {ECO:0000244|PDB:5D4K}. FT TURN 390 392 {ECO:0000244|PDB:5D4K}. FT STRAND 397 400 {ECO:0000244|PDB:5D4K}. FT HELIX 407 409 {ECO:0000244|PDB:5D4K}. FT TURN 410 412 {ECO:0000244|PDB:5D4K}. FT STRAND 413 419 {ECO:0000244|PDB:5D4K}. FT STRAND 421 430 {ECO:0000244|PDB:5D4K}. FT HELIX 433 435 {ECO:0000244|PDB:5D4K}. FT STRAND 437 442 {ECO:0000244|PDB:5D4K}. FT STRAND 451 457 {ECO:0000244|PDB:5D4K}. FT STRAND 463 465 {ECO:0000244|PDB:5D4K}. FT STRAND 468 473 {ECO:0000244|PDB:5D4K}. FT STRAND 478 484 {ECO:0000244|PDB:5D4K}. FT TURN 487 490 {ECO:0000244|PDB:5D4K}. FT STRAND 491 497 {ECO:0000244|PDB:5D4K}. FT STRAND 508 510 {ECO:0000244|PDB:5D4K}. FT STRAND 516 519 {ECO:0000244|PDB:5D4K}. FT STRAND 521 523 {ECO:0000244|PDB:5D4K}. FT STRAND 525 533 {ECO:0000244|PDB:5D4K}. FT HELIX 536 538 {ECO:0000244|PDB:5D4K}. FT STRAND 540 548 {ECO:0000244|PDB:5D4K}. FT STRAND 551 565 {ECO:0000244|PDB:5D4K}. SQ SEQUENCE 764 AA; 83284 MW; 927461F4EB3B05C7 CRC64; MLLFVLTCLL AVFPAISTKS PIFGPEEVNS VEGNSVSITC YYPPTSVNRH TRKYWCRQGA RGGCITLISS EGYVSSKYAG RANLTNFPEN GTFVVNIAQL SQDDSGRYKC GLGINSRGLS FDVSLEVSQG PGLLNDTKVY TVDLGRTVTI NCPFKTENAQ KRKSLYKQIG LYPVLVIDSS GYVNPNYTGR IRLDIQGTGQ LLFSVVINQL RLSDAGQYLC QAGDDSNSNK KNADLQVLKP EPELVYEDLR GSVTFHCALG PEVANVAKFL CRQSSGENCD VVVNTLGKRA PAFEGRILLN PQDKDGSFSV VITGLRKEDA GRYLCGAHSD GQLQEGSPIQ AWQLFVNEES TIPRSPTVVK GVAGGSVAVL CPYNRKESKS IKYWCLWEGA QNGRCPLLVD SEGWVKAQYE GRLSLLEEPG NGTFTVILNQ LTSRDAGFYW CLTNGDTLWR TTVEIKIIEG EPNLKVPGNV TAVLGETLKV PCHFPCKFSS YEKYWCKWNN TGCQALPSQD EGPSKAFVNC DENSRLVSLT LNLVTRADEG WYWCGVKQGH FYGETAAVYV AVEERKAAGS RDVSLAKADA APDEKVLDSG FREIENKAIQ DPRLFAEEKA VADTRDQADG SRASVDSGSS EEQGGSSRAL VSTLVPLGLV LAVGAVAVGV ARARHRKNVD RVSIRSYRTD ISMSDFENSR EFGANDNMGA SSITQETSLG GKEEFVATTE STTETKEPKK AKRSSKEEAE MAYKDFLLQS STVAAEAQDG PQEA //