ITB8_HUMAN
ID ITB8_HUMAN Reviewed; 769 AA.
AC P26012; A4D133; B4DHD4;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Integrin beta-8 {ECO:0000305};
DE Flags: Precursor;
GN Name=ITGB8 {ECO:0000312|HGNC:HGNC:6163};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ITGAV,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=1918072; DOI=10.1016/s0021-9258(18)55042-0;
RA Moyle M., Napier M.A., McLean J.W.;
RT "Cloning and expression of a divergent integrin subunit beta 8.";
RL J. Biol. Chem. 266:19650-19658(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND INTERACTION WITH TGFB1.
RX PubMed=22278742; DOI=10.1091/mbc.e11-12-1018;
RA Wang R., Zhu J., Dong X., Shi M., Lu C., Springer T.A.;
RT "GARP regulates the bioavailability and activation of TGFbeta.";
RL Mol. Biol. Cell 23:1129-1139(2012).
CC -!- FUNCTION: Integrin alpha-V:beta-8 (ITGAV:ITGB8) is a receptor for
CC fibronectin (PubMed:1918072). It recognizes the sequence R-G-D in its
CC ligands (PubMed:1918072). Integrin alpha-V:beta-6 (ITGAV:ITGB6)
CC mediates R-G-D-dependent release of transforming growth factor beta-1
CC (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby
CC playing a key role in TGF-beta-1 activation on the surface of activated
CC regulatory T-cells (Tregs) (Probable). Required during vasculogenesis
CC (By similarity). {ECO:0000250|UniProtKB:Q0VBD0,
CC ECO:0000269|PubMed:1918072, ECO:0000305|PubMed:22278742}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:1918072).
CC Beta-8 (ITGB8) associates with alpha-V (ITGAV) to form ITGAV:ITGB8
CC (PubMed:1918072, PubMed:22278742). ITGAV:ITGB8 interacts with TGFB1
CC (PubMed:22278742). {ECO:0000269|PubMed:1918072,
CC ECO:0000269|PubMed:22278742}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1918072};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P26012-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P26012-2; Sequence=VSP_056531;
CC -!- TISSUE SPECIFICITY: Placenta, kidney, brain, ovary, uterus and in
CC several transformed cells. Transiently expressed in 293 human embryonic
CC kidney cells. {ECO:0000269|PubMed:1918072}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; M73780; AAA36034.1; -; mRNA.
DR EMBL; AK295044; BAG58095.1; -; mRNA.
DR EMBL; AC004130; AAQ96845.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24275.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93725.1; -; Genomic_DNA.
DR CCDS; CCDS5370.1; -. [P26012-1]
DR PIR; A41029; A41029.
DR RefSeq; NP_002205.1; NM_002214.2. [P26012-1]
DR RefSeq; XP_011513698.1; XM_011515396.1. [P26012-2]
DR RefSeq; XP_016867667.1; XM_017012178.1. [P26012-1]
DR RefSeq; XP_016867668.1; XM_017012179.1. [P26012-1]
DR RefSeq; XP_016867669.1; XM_017012180.1. [P26012-2]
DR RefSeq; XP_016867670.1; XM_017012181.1. [P26012-2]
DR RefSeq; XP_016867671.1; XM_017012182.1. [P26012-2]
DR RefSeq; XP_016867672.1; XM_017012183.1. [P26012-2]
DR PDB; 6DJP; EM; 4.80 A; B=43-681.
DR PDB; 6OM1; X-ray; 2.66 A; B/D/F/H=43-498.
DR PDB; 6OM2; X-ray; 2.77 A; B/D=43-463.
DR PDB; 6UJA; EM; 3.30 A; B=43-769.
DR PDB; 6UJB; EM; 3.51 A; B=43-769.
DR PDB; 6UJC; EM; 3.56 A; B=43-769.
DR PDBsum; 6DJP; -.
DR PDBsum; 6OM1; -.
DR PDBsum; 6OM2; -.
DR PDBsum; 6UJA; -.
DR PDBsum; 6UJB; -.
DR PDBsum; 6UJC; -.
DR AlphaFoldDB; P26012; -.
DR SMR; P26012; -.
DR BioGRID; 109902; 32.
DR ComplexPortal; CPX-1821; Integrin alphav-beta8 complex.
DR CORUM; P26012; -.
DR IntAct; P26012; 12.
DR MINT; P26012; -.
DR STRING; 9606.ENSP00000222573; -.
DR BindingDB; P26012; -.
DR ChEMBL; CHEMBL3430892; -.
DR GuidetoPHARMACOLOGY; 2462; -.
DR GlyGen; P26012; 7 sites.
DR iPTMnet; P26012; -.
DR PhosphoSitePlus; P26012; -.
DR BioMuta; ITGB8; -.
DR DMDM; 124975; -.
DR CPTAC; CPTAC-1311; -.
DR EPD; P26012; -.
DR jPOST; P26012; -.
DR MassIVE; P26012; -.
DR MaxQB; P26012; -.
DR PaxDb; P26012; -.
DR PeptideAtlas; P26012; -.
DR PRIDE; P26012; -.
DR ProteomicsDB; 4212; -.
DR ProteomicsDB; 54309; -. [P26012-1]
DR ABCD; P26012; 21 sequenced antibodies.
DR Antibodypedia; 25377; 183 antibodies from 29 providers.
DR DNASU; 3696; -.
DR Ensembl; ENST00000222573.5; ENSP00000222573.3; ENSG00000105855.10. [P26012-1]
DR Ensembl; ENST00000537992.5; ENSP00000441561.1; ENSG00000105855.10. [P26012-2]
DR GeneID; 3696; -.
DR KEGG; hsa:3696; -.
DR MANE-Select; ENST00000222573.5; ENSP00000222573.3; NM_002214.3; NP_002205.1.
DR UCSC; uc003suu.4; human. [P26012-1]
DR CTD; 3696; -.
DR DisGeNET; 3696; -.
DR GeneCards; ITGB8; -.
DR HGNC; HGNC:6163; ITGB8.
DR HPA; ENSG00000105855; Tissue enhanced (brain).
DR MIM; 604160; gene.
DR neXtProt; NX_P26012; -.
DR OpenTargets; ENSG00000105855; -.
DR PharmGKB; PA29962; -.
DR VEuPathDB; HostDB:ENSG00000105855; -.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT00980000198528; -.
DR HOGENOM; CLU_011772_3_1_1; -.
DR InParanoid; P26012; -.
DR OMA; DFSCPYY; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; P26012; -.
DR TreeFam; TF105392; -.
DR PathwayCommons; P26012; -.
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
DR SignaLink; P26012; -.
DR SIGNOR; P26012; -.
DR BioGRID-ORCS; 3696; 11 hits in 1067 CRISPR screens.
DR ChiTaRS; ITGB8; human.
DR GeneWiki; ITGB8; -.
DR GenomeRNAi; 3696; -.
DR Pharos; P26012; Tbio.
DR PRO; PR:P26012; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P26012; protein.
DR Bgee; ENSG00000105855; Expressed in pigmented layer of retina and 177 other tissues.
DR Genevisible; P26012; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0034686; C:integrin alphav-beta8 complex; IDA:UniProtKB.
DR GO; GO:0008305; C:integrin complex; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:1990430; F:extracellular matrix protein binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0051216; P:cartilage development; IMP:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IC:ComplexPortal.
DR GO; GO:0001573; P:ganglioside metabolic process; IEA:Ensembl.
DR GO; GO:0060022; P:hard palate development; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:ComplexPortal.
DR GO; GO:0061520; P:Langerhans cell differentiation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0060674; P:placenta blood vessel development; TAS:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1901388; P:regulation of transforming growth factor beta activation; IDA:ComplexPortal.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001570; P:vasculogenesis; IMP:UniProtKB.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR015442; Integrin_bsu-8.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 1.
DR PANTHER; PTHR10082:SF9; PTHR10082:SF9; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM00423; PSI; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; Integrin; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..769
FT /note="Integrin beta-8"
FT /id="PRO_0000016354"
FT TOPO_DOM 43..684
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 685..704
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 705..769
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 146..384
FT /note="VWFA"
FT REPEAT 471..510
FT /note="I"
FT REPEAT 511..552
FT /note="II"
FT REPEAT 553..592
FT /note="III"
FT REPEAT 593..629
FT /note="IV"
FT REGION 471..629
FT /note="Cysteine-rich tandem repeats"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 648
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..469
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 55..65
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 58..94
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 68..83
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 211..218
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 266..307
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 407..419
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 467..471
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 481..494
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 491..520
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 526..531
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 528..561
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 533..546
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 567..572
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 574..583
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 607..612
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 609..657
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 614..624
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 627..630
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT DISULFID 634..643
FT /evidence="ECO:0000255|PIRSR:PIRSR002512-1"
FT VAR_SEQ 1..135
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056531"
FT VARIANT 552
FT /note="S -> F (in dbSNP:rs5002476)"
FT /id="VAR_034028"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6UJA"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:6OM1"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6OM1"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:6OM1"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:6OM1"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:6OM1"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:6OM2"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:6OM2"
FT STRAND 223..232
FT /evidence="ECO:0007829|PDB:6OM1"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:6OM1"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:6OM1"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 274..283
FT /evidence="ECO:0007829|PDB:6OM1"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:6OM1"
FT TURN 315..319
FT /evidence="ECO:0007829|PDB:6OM1"
FT HELIX 325..335
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:6OM1"
FT HELIX 348..353
FT /evidence="ECO:0007829|PDB:6OM1"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:6OM1"
FT HELIX 373..384
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:6OM2"
FT STRAND 400..406
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:6OM2"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 428..435
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:6OM1"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:6OM1"
SQ SEQUENCE 769 AA; 85632 MW; F7E3994F92B12A65 CRC64;
MCGSALAFFT AAFVCLQNDR RGPASFLWAA WVFSLVLGLG QGEDNRCASS NAASCARCLA
LGPECGWCVQ EDFISGGSRS ERCDIVSNLI SKGCSVDSIE YPSVHVIIPT ENEINTQVTP
GEVSIQLRPG AEANFMLKVH PLKKYPVDLY YLVDVSASMH NNIEKLNSVG NDLSRKMAFF
SRDFRLGFGS YVDKTVSPYI SIHPERIHNQ CSDYNLDCMP PHGYIHVLSL TENITEFEKA
VHRQKISGNI DTPEGGFDAM LQAAVCESHI GWRKEAKRLL LVMTDQTSHL ALDSKLAGIV
VPNDGNCHLK NNVYVKSTTM EHPSLGQLSE KLIDNNINVI FAVQGKQFHW YKDLLPLLPG
TIAGEIESKA ANLNNLVVEA YQKLISEVKV QVENQVQGIY FNITAICPDG SRKPGMEGCR
NVTSNDEVLF NVTVTMKKCD VTGGKNYAII KPIGFNETAK IHIHRNCSCQ CEDNRGPKGK
CVDETFLDSK CFQCDENKCH FDEDQFSSES CKSHKDQPVC SGRGVCVCGK CSCHKIKLGK
VYGKYCEKDD FSCPYHHGNL CAGHGECEAG RCQCFSGWEG DRCQCPSAAA QHCVNSKGQV
CSGRGTCVCG RCECTDPRSI GRFCEHCPTC YTACKENWNC MQCLHPHNLS QAILDQCKTS
CALMEQQHYV DQTSECFSSP SYLRIFFIIF IVTFLIGLLK VLIIRQVILQ WNSNKIKSSS
DYRVSASKKD KLILQSVCTR AVTYRREKPE EIKMDISKLN AHETFRCNF
