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 27-MAR-2024, entry version 214. 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). RN [7] {ECO:0007744|PDB:6OM1, ECO:0007744|PDB:6OM2} RP X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 43-498 IN COMPLEX WITH ITGAV; RP TGFB1 PEPTIDE; CALCIUM AND MAGNESIUM, DOMAIN, DISULFIDE BONDS, AND RP GLYCOSYLATION AT ASN-402; ASN-421 AND ASN-431. RX PubMed=31792290; DOI=10.1038/s41467-019-13248-5; RA Wang J., Su Y., Iacob R.E., Engen J.R., Springer T.A.; RT "General structural features that regulate integrin affinity revealed by RT atypical alphaVbeta8."; RL Nat. Commun. 10:5481-5481(2019). 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 -!- DOMAIN: The VWFA domain (or beta I domain) contains two cation-binding CC sites: the ligand-associated metal ion-binding site (LIMBS or SyMBS) CC and the metal ion-dependent adhesion site (MIDAS) (PubMed:31792290). CC Unlike in the other beta integrins, the cation-binding site adjacent CC MIDAS site (ADMIDAS) in ITGB8 is not functional due to the presence of CC two Asn residues instead of 2 Asp residues (PubMed:31792290). This CC domain is also part of the ligand-binding site (PubMed:31792290). CC {ECO:0000269|PubMed:31792290}. CC -!- SIMILARITY: Belongs to the integrin beta chain family. {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; 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. 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. 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 PDB; 7Y1T; EM; 3.24 A; B=43-498. DR PDB; 8TCF; EM; 2.90 A; B=104-467. DR PDBsum; 6DJP; -. DR PDBsum; 6OM1; -. DR PDBsum; 6OM2; -. DR PDBsum; 6UJA; -. DR PDBsum; 6UJB; -. DR PDBsum; 6UJC; -. DR PDBsum; 7Y1T; -. DR PDBsum; 8TCF; -. DR AlphaFoldDB; P26012; -. DR EMDB; EMD-20794; -. DR EMDB; EMD-20795; -. DR EMDB; EMD-20796; -. DR EMDB; EMD-33572; -. DR EMDB; EMD-33573; -. DR EMDB; EMD-41153; -. DR EMDB; EMD-7939; -. DR SMR; P26012; -. DR BioGRID; 109902; 35. DR ComplexPortal; CPX-1821; Integrin alphav-beta8 complex. DR CORUM; P26012; -. DR IntAct; P26012; 13. DR MINT; P26012; -. DR STRING; 9606.ENSP00000222573; -. DR BindingDB; P26012; -. DR ChEMBL; CHEMBL3430892; -. DR GuidetoPHARMACOLOGY; 2462; -. DR GlyCosmos; P26012; 7 sites, No reported glycans. 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; 9606-ENSP00000222573; -. DR PeptideAtlas; P26012; -. DR ProteomicsDB; 4212; -. DR ProteomicsDB; 54309; -. [P26012-1] DR Pumba; P26012; -. DR ABCD; P26012; 21 sequenced antibodies. DR Antibodypedia; 25377; 208 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 AGR; HGNC:6163; -. DR CTD; 3696; -. DR DisGeNET; 3696; -. DR GeneCards; ITGB8; -. DR HGNC; HGNC:6163; ITGB8. DR HPA; ENSG00000105855; Low tissue specificity. DR MIM; 604160; gene. DR neXtProt; NX_P26012; -. DR OpenTargets; ENSG00000105855; -. DR PharmGKB; PA29962; -. DR VEuPathDB; HostDB:ENSG00000105855; -. DR eggNOG; KOG1226; Eukaryota. DR GeneTree; ENSGT01090000259987; -. DR HOGENOM; CLU_011772_3_1_1; -. DR InParanoid; P26012; -. DR OMA; SKIDNPC; -. DR OrthoDB; 5475862at2759; -. 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; 13 hits in 1147 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 179 other cell types or tissues. 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; IBA:GO_Central. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051216; P:cartilage development; IMP:UniProtKB. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0007160; P:cell-matrix adhesion; NAS: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; ISS:UniProtKB. 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; 2.10.25.10; Laminin; 3. DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1. DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 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; IPR002369; Integrin_bsu_VWA. DR InterPro; IPR032695; Integrin_dom_sf. DR InterPro; IPR016201; PSI. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1. DR PANTHER; PTHR10082:SF9; INTEGRIN BETA-8; 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; SSF57196; EGF/Laminin; 2. DR SUPFAM; SSF69179; Integrin domains; 1. DR SUPFAM; SSF103575; Plexin repeat; 1. DR SUPFAM; SSF53300; vWA-like; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS00243; INTEGRIN_BETA; 2. DR Genevisible; P26012; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane; KW Disulfide bond; EGF-like domain; Glycoprotein; Integrin; Magnesium; KW Membrane; Metal-binding; Receptor; Reference proteome; Repeat; Signal; KW 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 46..95 FT /note="PSI" FT /evidence="ECO:0000255" FT DOMAIN 146..384 FT /note="VWFA" FT /evidence="ECO:0000305|PubMed:31792290" FT DOMAIN 471..510 FT /note="EGF-like 1" FT /evidence="ECO:0000250|UniProtKB:P05106" FT DOMAIN 511..552 FT /note="EGF-like 2" FT /evidence="ECO:0000250|UniProtKB:P05106" FT DOMAIN 553..592 FT /note="EGF-like 3" FT /evidence="ECO:0000250|UniProtKB:P05106" FT DOMAIN 593..629 FT /note="EGF-like 4" FT /evidence="ECO:0000250|UniProtKB:P05106" FT BINDING 154 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="in MIDAS binding site" FT /evidence="ECO:0000269|PubMed:31792290, FT ECO:0007744|PDB:6OM1, ECO:0007744|PDB:6OM2" FT BINDING 156 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="in MIDAS binding site" FT /evidence="ECO:0000269|PubMed:31792290, FT ECO:0007744|PDB:6OM2" FT BINDING 193 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /note="in LIMBS binding site" FT /evidence="ECO:0000269|PubMed:31792290, FT ECO:0007744|PDB:6OM1, ECO:0007744|PDB:6OM2" FT BINDING 249 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /note="in LIMBS binding site" FT /evidence="ECO:0000269|PubMed:31792290, FT ECO:0007744|PDB:6OM1, ECO:0007744|PDB:6OM2" FT BINDING 251 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /note="in LIMBS binding site" FT /evidence="ECO:0000269|PubMed:31792290, FT ECO:0007744|PDB:6OM1, ECO:0007744|PDB:6OM2" FT BINDING 253 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /note="in LIMBS binding site" FT /evidence="ECO:0000269|PubMed:31792290, FT ECO:0007744|PDB:6OM1, ECO:0007744|PDB:6OM2" FT BINDING 254 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /note="in LIMBS binding site" FT /evidence="ECO:0000269|PubMed:31792290, FT ECO:0007744|PDB:6OM1, ECO:0007744|PDB:6OM2" FT BINDING 254 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="in MIDAS binding site" FT /evidence="ECO:0000269|PubMed:31792290, FT ECO:0007744|PDB:6OM1, ECO:0007744|PDB:6OM2" 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:0000269|PubMed:31792290, FT ECO:0007744|PDB:6OM1" FT CARBOHYD 421 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:31792290, FT ECO:0007744|PDB:6OM1" FT CARBOHYD 431 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:31792290, FT ECO:0007744|PDB:6OM1, ECO:0007744|PDB:6OM2" 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..65 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 55..469 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 58..83 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 68..94 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 211..218 FT /evidence="ECO:0007744|PDB:6OM1, ECO:0007744|PDB:6OM2, FT ECO:0007744|PDB:6UJA, ECO:0007744|PDB:6UJB, FT ECO:0007744|PDB:6UJC, ECO:0007744|PDB:7Y1T" FT DISULFID 266..307 FT /evidence="ECO:0007744|PDB:6OM1, ECO:0007744|PDB:6OM2, FT ECO:0007744|PDB:6UJA, ECO:0007744|PDB:6UJB, FT ECO:0007744|PDB:6UJC, ECO:0007744|PDB:7Y1T" FT DISULFID 407..419 FT /evidence="ECO:0007744|PDB:6OM1, ECO:0007744|PDB:6OM2, FT ECO:0007744|PDB:6UJA, ECO:0007744|PDB:6UJB, FT ECO:0007744|PDB:6UJC, ECO:0007744|PDB:7Y1T" FT DISULFID 439..467 FT /evidence="ECO:0007744|PDB:6OM1, ECO:0007744|PDB:6UJA, FT ECO:0007744|PDB:6UJB, ECO:0007744|PDB:6UJC" FT DISULFID 471..494 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 511..526 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 520..531 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 533..546 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 553..567 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 561..572 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 574..583 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 585..609 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 593..607 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 601..612 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 614..624 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 627..630 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 634..661 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 640..657 FT /evidence="ECO:0000250|UniProtKB:P05106" 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:8TCF" 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 166..168 FT /evidence="ECO:0007829|PDB:7Y1T" 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 415..417 FT /evidence="ECO:0007829|PDB:7Y1T" 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 //