ID ITB5_HUMAN Reviewed; 799 AA. AC P18084; B0LPF8; B2RD70; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 27-MAR-2024, entry version 231. DE RecName: Full=Integrin beta-5; DE Flags: Precursor; GN Name=ITGB5; 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]. RC TISSUE=Thymic epithelium; RX PubMed=2328726; DOI=10.1002/j.1460-2075.1990.tb08275.x; RA Ramaswamy H., Hemler M.E.; RT "Cloning, primary structure and properties of a novel human integrin beta RT subunit."; RL EMBO J. 9:1561-1568(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2371275; DOI=10.1073/pnas.87.14.5354; RA Suzuki S., Huang Z.S., Tanihara H.; RT "Cloning of an integrin beta subunit exhibiting high homology with integrin RT beta 3 subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 87:5354-5358(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2211615; DOI=10.1016/s0021-9258(17)44878-2; RA McLean J.W., Vestal D.J., Cheresh D.A., Bodary S.C.; RT "cDNA sequence of the human integrin beta 5 subunit."; RL J. Biol. Chem. 265:17126-17131(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-431. 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG SeattleSNPs variation discovery resource; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP INTERACTION WITH MYO10. RX PubMed=15156152; DOI=10.1038/ncb1136; RA Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A., RA Cheney R.E., Stromblad S.; RT "Myosin-X provides a motor-based link between integrins and the RT cytoskeleton."; RL Nat. Cell Biol. 6:523-531(2004). RN [8] RP INTERACTION WITH CCN3. RX PubMed=15611078; DOI=10.1074/jbc.m404903200; RA Lin C.G., Chen C.C., Leu S.J., Grzeszkiewicz T.M., Lau L.F.; RT "Integrin-dependent functions of the angiogenic inducer NOV (CCN3): RT implication in wound healing."; RL J. Biol. Chem. 280:8229-8237(2005). RN [9] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ADENOVIRUS TYPE C RP PENTON PROTEIN. RX PubMed=20615244; DOI=10.1186/1743-422x-7-148; RA Lyle C., McCormick F.; RT "Integrin alphavbeta5 is a primary receptor for adenovirus in CAR-negative RT cells."; RL Virol. J. 7:148-148(2010). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP INTERACTION WITH TNS3. RX PubMed=35687021; DOI=10.1083/jcb.202108027; RA Zuidema A., Atherton P., Kreft M., Hoekman L., Bleijerveld O.B., RA Nagaraj N., Chen N., Faessler R., Sonnenberg A.; RT "PEAK1 Y635 phosphorylation regulates cell migration through association RT with Tensin3 and integrins."; RL J. Cell Biol. 221:0-0(2022). CC -!- FUNCTION: Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for CC fibronectin. It recognizes the sequence R-G-D in its ligand. CC -!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB5 acts as a receptor CC for adenovirus type C. {ECO:0000269|PubMed:20615244}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-5 (ITGB5) CC associates with alpha-V (ITGAV). Interacts with MYO10 CC (PubMed:15156152). Interacts with DAB2. Integrin ITGAV:ITGB5 interacts CC with FBLN5 (via N-terminus) (By similarity). ITGAV:ITGB5 interacts with CC CCN3 (PubMed:15611078). Interacts with tensin TNS3; TNS3 also interacts CC with PEAK1, thus acting as an adapter molecule to bridge the CC association of PEAK1 with ITGB5 (PubMed:35687021). CC {ECO:0000250|UniProtKB:O70309, ECO:0000269|PubMed:15156152, CC ECO:0000269|PubMed:15611078, ECO:0000269|PubMed:35687021}. CC -!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB5 interacts with CC adenovirus type C penton protein. {ECO:0000269|PubMed:20615244}. CC -!- INTERACTION: CC P18084; Q9BY76: ANGPTL4; NbExp=3; IntAct=EBI-1223434, EBI-2968146; CC P18084; Q92624: APPBP2; NbExp=3; IntAct=EBI-1223434, EBI-743771; CC P18084; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1223434, EBI-3867333; CC P18084; O95967: EFEMP2; NbExp=3; IntAct=EBI-1223434, EBI-743414; CC P18084; Q13643: FHL3; NbExp=5; IntAct=EBI-1223434, EBI-741101; CC P18084; Q7Z6J6: FRMD5; NbExp=3; IntAct=EBI-1223434, EBI-727282; CC P18084; Q08379: GOLGA2; NbExp=3; IntAct=EBI-1223434, EBI-618309; CC P18084; P06756: ITGAV; NbExp=2; IntAct=EBI-1223434, EBI-298282; CC P18084; Q15323: KRT31; NbExp=3; IntAct=EBI-1223434, EBI-948001; CC P18084; O76011: KRT34; NbExp=3; IntAct=EBI-1223434, EBI-1047093; CC P18084; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-1223434, EBI-11959885; CC P18084; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-1223434, EBI-11749135; CC P18084; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-1223434, EBI-10172290; CC P18084; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1223434, EBI-10171774; CC P18084; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-1223434, EBI-10172052; CC P18084; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-1223434, EBI-751260; CC P18084; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-1223434, EBI-11987425; CC P18084; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-1223434, EBI-11522433; CC P18084; Q9HD67: MYO10; NbExp=2; IntAct=EBI-1223434, EBI-307061; CC P18084; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-1223434, EBI-22310682; CC P18084; Q8N720: ZNF655; NbExp=3; IntAct=EBI-1223434, EBI-625509; CC P18084; P97479: Myo7a; Xeno; NbExp=8; IntAct=EBI-1223434, EBI-1149557; CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. CC -!- DOMAIN: The VWFA domain (or beta I domain) contains three cation- CC binding sites: the ligand-associated metal ion-binding site (LIMBS or CC SyMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent CC MIDAS site (ADMIDAS). This domain is also part of the ligand-binding CC site. {ECO:0000250|UniProtKB:P05106}. 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; X53002; CAA37188.1; -; mRNA. DR EMBL; M35011; AAA52707.1; -; mRNA. DR EMBL; J05633; AAA59183.1; -; mRNA. DR EMBL; AK315429; BAG37817.1; -; mRNA. DR EMBL; EU332848; ABY87537.1; -; Genomic_DNA. DR EMBL; BC006541; AAH06541.1; -; mRNA. DR CCDS; CCDS3030.1; -. DR PIR; A38308; A38308. DR RefSeq; NP_002204.2; NM_002213.4. DR PDB; 7S46; X-ray; 2.10 A; B=760-770. DR PDB; 7S47; X-ray; 2.00 A; A/B=743-774. DR PDB; 7S48; X-ray; 1.90 A; B=760-770. DR PDBsum; 7S46; -. DR PDBsum; 7S47; -. DR PDBsum; 7S48; -. DR AlphaFoldDB; P18084; -. DR SMR; P18084; -. DR BioGRID; 109899; 162. DR ComplexPortal; CPX-1796; Integrin alphav-beta5 complex. DR CORUM; P18084; -. DR ELM; P18084; -. DR IntAct; P18084; 57. DR MINT; P18084; -. DR STRING; 9606.ENSP00000296181; -. DR BindingDB; P18084; -. DR ChEMBL; CHEMBL2096675; -. DR ChEMBL; CHEMBL4106150; -. DR GuidetoPHARMACOLOGY; 2459; -. DR GlyConnect; 1418; 6 N-Linked glycans (2 sites). DR GlyCosmos; P18084; 8 sites, 6 glycans. DR GlyGen; P18084; 10 sites, 6 N-linked glycans (2 sites), 1 O-linked glycan (2 sites). DR iPTMnet; P18084; -. DR PhosphoSitePlus; P18084; -. DR SwissPalm; P18084; -. DR BioMuta; ITGB5; -. DR DMDM; 124970; -. DR CPTAC; CPTAC-1284; -. DR EPD; P18084; -. DR jPOST; P18084; -. DR MassIVE; P18084; -. DR MaxQB; P18084; -. DR PaxDb; 9606-ENSP00000296181; -. DR PeptideAtlas; P18084; -. DR ProteomicsDB; 53546; -. DR Pumba; P18084; -. DR Antibodypedia; 963; 594 antibodies from 42 providers. DR DNASU; 3693; -. DR Ensembl; ENST00000296181.9; ENSP00000296181.4; ENSG00000082781.12. DR GeneID; 3693; -. DR KEGG; hsa:3693; -. DR MANE-Select; ENST00000296181.9; ENSP00000296181.4; NM_002213.5; NP_002204.2. DR UCSC; uc003eho.4; human. DR AGR; HGNC:6160; -. DR CTD; 3693; -. DR DisGeNET; 3693; -. DR GeneCards; ITGB5; -. DR HGNC; HGNC:6160; ITGB5. DR HPA; ENSG00000082781; Low tissue specificity. DR MIM; 147561; gene. DR neXtProt; NX_P18084; -. DR OpenTargets; ENSG00000082781; -. DR PharmGKB; PA29959; -. DR VEuPathDB; HostDB:ENSG00000082781; -. DR eggNOG; KOG1226; Eukaryota. DR GeneTree; ENSGT01090000259987; -. DR HOGENOM; CLU_011772_0_1_1; -. DR InParanoid; P18084; -. DR OMA; CVMLFTY; -. DR OrthoDB; 5475862at2759; -. DR PhylomeDB; P18084; -. DR TreeFam; TF105392; -. DR PathwayCommons; P18084; -. DR Reactome; R-HSA-1236973; Cross-presentation of particulate exogenous antigens (phagosomes). 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 Reactome; R-HSA-3000170; Syndecan interactions. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR Reactome; R-HSA-445355; Smooth Muscle Contraction. DR SignaLink; P18084; -. DR SIGNOR; P18084; -. DR BioGRID-ORCS; 3693; 202 hits in 1169 CRISPR screens. DR ChiTaRS; ITGB5; human. DR GeneWiki; Integrin,_beta_5; -. DR GenomeRNAi; 3693; -. DR Pharos; P18084; Tbio. DR PRO; PR:P18084; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P18084; Protein. DR Bgee; ENSG00000082781; Expressed in stromal cell of endometrium and 206 other cell types or tissues. DR ExpressionAtlas; P18084; baseline and differential. 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; HDA:UniProtKB. DR GO; GO:0034684; C:integrin alphav-beta5 complex; IDA:UniProtKB. DR GO; GO:0008305; C:integrin complex; IBA:GO_Central. DR GO; GO:0045335; C:phagocytic vesicle; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0043235; C:receptor complex; IDA:MGI. DR GO; GO:0005178; F:integrin binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW. DR GO; GO:0016477; P:cell migration; IMP:BHF-UCL. DR GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB. DR GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB. DR GO; GO:0090136; P:epithelial cell-cell adhesion; IMP:UniProtKB. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; NAS:ComplexPortal. DR Gene3D; 4.10.1240.30; -; 1. DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1. DR Gene3D; 2.10.25.10; Laminin; 4. 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; IPR040622; I-EGF_1. DR InterPro; IPR033760; Integrin_beta_N. DR InterPro; IPR015812; Integrin_bsu. DR InterPro; IPR014836; Integrin_bsu_cyt_dom. DR InterPro; IPR012896; Integrin_bsu_tail. DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf. DR InterPro; IPR002369; Integrin_bsu_VWA. DR InterPro; IPR032695; Integrin_dom_sf. DR InterPro; IPR016201; PSI. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1. DR PANTHER; PTHR10082:SF26; INTEGRIN BETA-5; 1. DR Pfam; PF18372; I-EGF_1; 1. DR Pfam; PF08725; Integrin_b_cyt; 1. DR Pfam; PF07965; Integrin_B_tail; 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; SM01241; Integrin_b_cyt; 1. DR SMART; SM01242; Integrin_B_tail; 1. DR SMART; SM00423; PSI; 1. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF57196; EGF/Laminin; 2. DR SUPFAM; SSF69687; Integrin beta tail domain; 1. DR SUPFAM; SSF69179; Integrin domains; 1. DR SUPFAM; SSF103575; Plexin repeat; 1. DR SUPFAM; SSF53300; vWA-like; 1. DR PROSITE; PS00022; EGF_1; 2. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS00243; INTEGRIN_BETA; 2. DR Genevisible; P18084; HS. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Cell adhesion; Cell membrane; Disulfide bond; KW EGF-like domain; Glycoprotein; Host cell receptor for virus entry; KW Host-virus interaction; Integrin; Magnesium; Membrane; Metal-binding; KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..799 FT /note="Integrin beta-5" FT /id="PRO_0000016348" FT TOPO_DOM 24..719 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 720..742 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 743..799 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 27..76 FT /note="PSI" FT /evidence="ECO:0000255" FT DOMAIN 136..378 FT /note="VWFA" FT /evidence="ECO:0000250|UniProtKB:P05106" FT DOMAIN 465..512 FT /note="EGF-like 1" FT /evidence="ECO:0000250|UniProtKB:P05106" FT DOMAIN 513..554 FT /note="EGF-like 2" FT /evidence="ECO:0000250|UniProtKB:P05106" FT DOMAIN 555..593 FT /note="EGF-like 3" FT /evidence="ECO:0000250|UniProtKB:P05106" FT DOMAIN 594..630 FT /note="EGF-like 4" FT /evidence="ECO:0000250|UniProtKB:P05106" FT BINDING 147 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="in MIDAS binding site" FT /evidence="ECO:0000250|UniProtKB:P05106" FT BINDING 149 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /note="in ADMIDAS binding site" FT /evidence="ECO:0000250|UniProtKB:P05106" FT BINDING 149 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="in MIDAS binding site" FT /evidence="ECO:0000250|UniProtKB:P05106" FT BINDING 152 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /note="in ADMIDAS binding site" FT /evidence="ECO:0000250|UniProtKB:P05106" FT BINDING 153 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /note="in ADMIDAS binding site" FT /evidence="ECO:0000250|UniProtKB:P05106" FT BINDING 184 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="in LIMBS binding site" FT /evidence="ECO:0000250|UniProtKB:P05106" FT BINDING 242 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="in LIMBS binding site" FT /evidence="ECO:0000250|UniProtKB:P05106" FT BINDING 244 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="in LIMBS binding site" FT /evidence="ECO:0000250|UniProtKB:P05106" FT BINDING 246 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="in LIMBS binding site" FT /evidence="ECO:0000250|UniProtKB:P05106" FT BINDING 247 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /note="in LIMBS binding site" FT /evidence="ECO:0000250|UniProtKB:P05106" FT BINDING 247 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /note="in MIDAS binding site" FT /evidence="ECO:0000250|UniProtKB:P05106" FT BINDING 362 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /note="in ADMIDAS binding site" FT /evidence="ECO:0000250|UniProtKB:P05106" FT MOD_RES 770 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CARBOHYD 347 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 460 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 477 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 505 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 552 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 586 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 654 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 705 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 28..46 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 36..463 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 39..64 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 49..75 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 202..211 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 259..300 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 401..413 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 433..461 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 465..484 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 476..487 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 489..498 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 500..530 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 513..528 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 522..533 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 535..548 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 550..571 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 555..569 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 563..574 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 576..585 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 587..610 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 594..608 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 602..613 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 615..625 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 628..631 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 635..682 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 641..661 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 644..657 FT /evidence="ECO:0000250|UniProtKB:P05106" FT DISULFID 690..714 FT /evidence="ECO:0000250|UniProtKB:P05106" FT VARIANT 428 FT /note="L -> V (in dbSNP:rs2291090)" FT /id="VAR_024290" FT VARIANT 431 FT /note="R -> Q (in dbSNP:rs2291089)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_049634" FT VARIANT 477 FT /note="N -> S (in dbSNP:rs2291087)" FT /id="VAR_049635" FT CONFLICT 193 FT /note="T -> A (in Ref. 2; AAA52707)" FT /evidence="ECO:0000305" FT CONFLICT 645 FT /note="L -> P (in Ref. 3; AAA59183)" FT /evidence="ECO:0000305" FT CONFLICT 790..792 FT /note="Missing (in Ref. 2; AAA52707)" FT /evidence="ECO:0000305" SQ SEQUENCE 799 AA; 88054 MW; D7E4727CA310512B CRC64; MPRAPAPLYA CLLGLCALLP RLAGLNICTS GSATSCEECL LIHPKCAWCS KEDFGSPRSI TSRCDLRANL VKNGCGGEIE SPASSFHVLR SLPLSSKGSG SAGWDVIQMT PQEIAVNLRP GDKTTFQLQV RQVEDYPVDL YYLMDLSLSM KDDLDNIRSL GTKLAEEMRK LTSNFRLGFG SFVDKDISPF SYTAPRYQTN PCIGYKLFPN CVPSFGFRHL LPLTDRVDSF NEEVRKQRVS RNRDAPEGGF DAVLQAAVCK EKIGWRKDAL HLLVFTTDDV PHIALDGKLG GLVQPHDGQC HLNEANEYTA SNQMDYPSLA LLGEKLAENN INLIFAVTKN HYMLYKNFTA LIPGTTVEIL DGDSKNIIQL IINAYNSIRS KVELSVWDQP EDLNLFFTAT CQDGVSYPGQ RKCEGLKIGD TASFEVSLEA RSCPSRHTEH VFALRPVGFR DSLEVGVTYN CTCGCSVGLE PNSARCNGSG TYVCGLCECS PGYLGTRCEC QDGENQSVYQ NLCREAEGKP LCSGRGDCSC NQCSCFESEF GKIYGPFCEC DNFSCARNKG VLCSGHGECH CGECKCHAGY IGDNCNCSTD ISTCRGRDGQ ICSERGHCLC GQCQCTEPGA FGEMCEKCPT CPDACSTKRD CVECLLLHSG KPDNQTCHSL CRDEVITWVD TIVKDDQEAV LCFYKTAKDC VMMFTYVELP SGKSNLTVLR EPECGNTPNA MTILLAVVGS ILLVGLALLA IWKLLVTIHD RREFAKFQSE RSRARYEMAS NPLYRKPIST HTVDFTFNKF NKSYNGTVD //