CADH5_HUMAN
ID CADH5_HUMAN Reviewed; 784 AA.
AC P33151; Q4VAI5; Q4VAI6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 5.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Cadherin-5;
DE AltName: Full=7B4 antigen;
DE AltName: Full=Vascular endothelial cadherin;
DE Short=VE-cadherin;
DE AltName: CD_antigen=CD144;
DE Flags: Precursor;
GN Name=CDH5;
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), AND VARIANT THR-517.
RC TISSUE=Endothelial cell;
RX PubMed=7627717; DOI=10.1161/01.atv.15.8.1229;
RA Breviario F., Caveda L., Corada M., Martin-Padura I., Navarro P., Golay J.,
RA Introna M., Gulino D., Lampugnani M.G., Dejana E.;
RT "Functional properties of human vascular endothelial cadherin
RT (7B4/cadherin-5), an endothelium-specific cadherin.";
RL Arterioscler. Thromb. Vasc. Biol. 15:1229-1239(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=9219219; DOI=10.3109/10739689709146790;
RA Ali J., Liao F., Martens E., Muller W.A.;
RT "Vascular endothelial cadherin (VE-cadherin): cloning and role in
RT endothelial cell-cell adhesion.";
RL Microcirculation 4:267-277(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANT THR-517.
RX PubMed=10861224; DOI=10.1042/0264-6021:3490159;
RA Shimoyama Y., Tsujimoto G., Kitajima M., Natori M.;
RT "Identification of three human type-II classic cadherins and frequent
RT heterophilic interactions between different subclasses of type-II classic
RT cadherins.";
RL Biochem. J. 349:159-167(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-517.
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-784 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=2059658; DOI=10.1091/mbc.2.4.261;
RA Suzuki S., Sano K., Tanihara H.;
RT "Diversity of the cadherin family: evidence for eight new cadherins in
RT nervous tissue.";
RL Cell Regul. 2:261-270(1991).
RN [6]
RP PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Endothelial cell;
RX PubMed=1522121; DOI=10.1083/jcb.118.6.1511;
RA Lampugnani M.G., Resnati M., Raiteri M., Pigott R., Pisacane A., Houen G.,
RA Ruco L.P., Dejana E.;
RT "A novel endothelial-specific membrane protein is a marker of cell-cell
RT contacts.";
RL J. Cell Biol. 118:1511-1522(1992).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15980433; DOI=10.1074/jbc.m502844200;
RA Andreeva A.V., Kutuzov M.A., Vaiskunaite R., Profirovic J., Meigs T.E.,
RA Predescu S., Malik A.B., Voyno-Yasenetskaya T.;
RT "G alpha12 interaction with alphaSNAP induces VE-cadherin localization at
RT endothelial junctions and regulates barrier function.";
RL J. Biol. Chem. 280:30376-30383(2005).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112; ASN-442; ASN-523 AND
RP ASN-535.
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., Moore R.J.,
RA 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 [9]
RP GLYCOSYLATION AT ASN-61; ASN-112 AND ASN-442.
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., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [10]
RP INTERACTION WITH TRPC4.
RX PubMed=19996314; DOI=10.1074/jbc.m109.060301;
RA Graziani A., Poteser M., Heupel W.M., Schleifer H., Krenn M.,
RA Drenckhahn D., Romanin C., Baumgartner W., Groschner K.;
RT "Cell-cell contact formation governs Ca2+ signaling by TRPC4 in the
RT vascular endothelium: evidence for a regulatory TRPC4-beta-catenin
RT interaction.";
RL J. Biol. Chem. 285:4213-4223(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KRIT1.
RX PubMed=20332120; DOI=10.1242/jcs.059329;
RA Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G.,
RA Chapon F., Dejana E.;
RT "CCM1 regulates vascular-lumen organization by inducing endothelial
RT polarity.";
RL J. Cell Sci. 123:1073-1080(2010).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH RTN4.
RX PubMed=21183689; DOI=10.1182/blood-2010-04-281956;
RA Di Lorenzo A., Manes T.D., Davalos A., Wright P.L., Sessa W.C.;
RT "Endothelial reticulon-4B (Nogo-B) regulates ICAM-1-mediated leukocyte
RT transmigration and acute inflammation.";
RL Blood 117:2284-2295(2011).
RN [13]
RP FUNCTION, AND GLYCOSYLATION AT ASN-61; ASN-112; ASN-157; ASN-362 AND
RP ASN-442.
RX PubMed=21269602; DOI=10.1016/j.jmb.2011.01.031;
RA Brasch J., Harrison O.J., Ahlsen G., Carnally S.M., Henderson R.M.,
RA Honig B., Shapiro L.;
RT "Structure and binding mechanism of vascular endothelial cadherin: a
RT divergent classical cadherin.";
RL J. Mol. Biol. 408:57-73(2011).
RN [14]
RP INTERACTION WITH PALS1.
RX PubMed=27466317; DOI=10.1091/mbc.e16-02-0127;
RA Brinkmann B.F., Steinbacher T., Hartmann C., Kummer D., Pajonczyk D.,
RA Mirzapourshafiyi F., Nakayama M., Weide T., Gerke V., Ebnet K.;
RT "VE-cadherin interacts with cell polarity protein Pals1 to regulate
RT vascular lumen formation.";
RL Mol. Biol. Cell 27:2811-2821(2016).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins (By
CC similarity). They preferentially interact with themselves in a
CC homophilic manner in connecting cells; cadherins may thus contribute to
CC the sorting of heterogeneous cell types (PubMed:21269602). This
CC cadherin may play a important role in endothelial cell biology through
CC control of the cohesion and organization of the intercellular junctions
CC (By similarity). It associates with alpha-catenin forming a link to the
CC cytoskeleton (PubMed:10861224). Acts in concert with KRIT1 and PALS1 to
CC establish and maintain correct endothelial cell polarity and vascular
CC lumen (By similarity). These effects are mediated by recruitment and
CC activation of the Par polarity complex and RAP1B (PubMed:20332120).
CC Required for activation of PRKCZ and for the localization of
CC phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction
CC (PubMed:20332120). {ECO:0000250|UniProtKB:P55284,
CC ECO:0000250|UniProtKB:Q8AYD0, ECO:0000269|PubMed:10861224,
CC ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:21269602}.
CC -!- SUBUNIT: Interacts (via cadherin 5 domain) with PTPRB (By similarity).
CC Interacts with TRPC4 (PubMed:19996314). Interacts with KRIT1
CC (PubMed:20332120). Interacts with PARD3 (By similarity). Interacts with
CC RTN4 (isoform B) (PubMed:21183689). Interacts with PALS1; the
CC interaction promotes PALS1 localization to cell junctions and is
CC required for CDH5-mediated vascular lumen formation and endothelial
CC cell (PubMed:27466317). {ECO:0000250|UniProtKB:P55284,
CC ECO:0000269|PubMed:19996314, ECO:0000269|PubMed:20332120,
CC ECO:0000269|PubMed:21183689, ECO:0000269|PubMed:27466317}.
CC -!- INTERACTION:
CC P33151; P35222: CTNNB1; NbExp=7; IntAct=EBI-2903122, EBI-491549;
CC P33151; Q8TEW0: PARD3; NbExp=5; IntAct=EBI-2903122, EBI-81968;
CC P33151; Q9NPB6: PARD6A; NbExp=4; IntAct=EBI-2903122, EBI-81876;
CC P33151; P23381: WARS1; NbExp=4; IntAct=EBI-2903122, EBI-721244;
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:20332120,
CC ECO:0000269|PubMed:21183689}. Cell membrane
CC {ECO:0000269|PubMed:15980433, ECO:0000305|PubMed:20332120}; Single-pass
CC type I membrane protein {ECO:0000305|PubMed:20332120}. Note=Found at
CC cell-cell boundaries and probably at cell-matrix boundaries. KRIT1 and
CC CDH5 reciprocally regulate their localization to endothelial cell-cell
CC junctions. {ECO:0000269|PubMed:20332120}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P33151-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P33151-2; Sequence=VSP_053861;
CC -!- TISSUE SPECIFICITY: Endothelial tissues and brain.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues by KDR/VEGFR-2.
CC Dephosphorylated by PTPRB (By similarity). {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:21269602}.
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DR EMBL; X79981; CAA56306.1; -; mRNA.
DR EMBL; U84722; AAB41796.1; -; mRNA.
DR EMBL; AB035304; BAA87418.1; -; mRNA.
DR EMBL; BC096363; AAH96363.1; -; mRNA.
DR EMBL; BC096364; AAH96364.3; -; mRNA.
DR EMBL; BC117520; AAI17521.1; -; mRNA.
DR EMBL; X59796; CAA42468.1; -; mRNA.
DR CCDS; CCDS10804.1; -. [P33151-1]
DR PIR; S49893; IJHUC5.
DR RefSeq; NP_001786.2; NM_001795.4. [P33151-1]
DR AlphaFoldDB; P33151; -.
DR SMR; P33151; -.
DR BioGRID; 107438; 107.
DR CORUM; P33151; -.
DR DIP; DIP-41172N; -.
DR IntAct; P33151; 78.
DR MINT; P33151; -.
DR STRING; 9606.ENSP00000344115; -.
DR DrugBank; DB05685; FX06.
DR DrugBank; DB00480; Lenalidomide.
DR GlyConnect; 617; 30 N-Linked glycans (4 sites).
DR GlyGen; P33151; 8 sites, 42 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P33151; -.
DR PhosphoSitePlus; P33151; -.
DR BioMuta; CDH5; -.
DR DMDM; 322510142; -.
DR jPOST; P33151; -.
DR MassIVE; P33151; -.
DR MaxQB; P33151; -.
DR PaxDb; P33151; -.
DR PeptideAtlas; P33151; -.
DR PRIDE; P33151; -.
DR ProteomicsDB; 54900; -. [P33151-1]
DR TopDownProteomics; P33151-1; -. [P33151-1]
DR Antibodypedia; 3717; 1245 antibodies from 43 providers.
DR DNASU; 1003; -.
DR Ensembl; ENST00000341529.8; ENSP00000344115.3; ENSG00000179776.19. [P33151-1]
DR Ensembl; ENST00000614547.4; ENSP00000479381.1; ENSG00000179776.19. [P33151-2]
DR Ensembl; ENST00000649567.1; ENSP00000497290.1; ENSG00000179776.19. [P33151-1]
DR GeneID; 1003; -.
DR KEGG; hsa:1003; -.
DR MANE-Select; ENST00000341529.8; ENSP00000344115.3; NM_001795.5; NP_001786.2.
DR UCSC; uc002eom.5; human. [P33151-1]
DR CTD; 1003; -.
DR DisGeNET; 1003; -.
DR GeneCards; CDH5; -.
DR HGNC; HGNC:1764; CDH5.
DR HPA; ENSG00000179776; Tissue enhanced (placenta).
DR MIM; 601120; gene.
DR neXtProt; NX_P33151; -.
DR OpenTargets; ENSG00000179776; -.
DR PharmGKB; PA26301; -.
DR VEuPathDB; HostDB:ENSG00000179776; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000160587; -.
DR HOGENOM; CLU_005284_3_2_1; -.
DR InParanoid; P33151; -.
DR OMA; NVKFKFA; -.
DR OrthoDB; 259069at2759; -.
DR PhylomeDB; P33151; -.
DR TreeFam; TF329887; -.
DR PathwayCommons; P33151; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR SignaLink; P33151; -.
DR SIGNOR; P33151; -.
DR BioGRID-ORCS; 1003; 35 hits in 1068 CRISPR screens.
DR ChiTaRS; CDH5; human.
DR GeneWiki; VE-cadherin; -.
DR GenomeRNAi; 1003; -.
DR Pharos; P33151; Tbio.
DR PRO; PR:P33151; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P33151; protein.
DR Bgee; ENSG00000179776; Expressed in right lung and 178 other tissues.
DR ExpressionAtlas; P33151; baseline and differential.
DR Genevisible; P33151; HS.
DR GO; GO:0005912; C:adherens junction; IDA:CAFA.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
DR GO; GO:0070700; F:BMP receptor binding; IPI:ARUK-UCL.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0070051; F:fibrinogen binding; IMP:ARUK-UCL.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:ARUK-UCL.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IPI:UniProtKB.
DR GO; GO:0034332; P:adherens junction organization; IDA:ARUK-UCL.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:ARUK-UCL.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:ARUK-UCL.
DR GO; GO:0001955; P:blood vessel maturation; IEA:Ensembl.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:ARUK-UCL.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IDA:ARUK-UCL.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IMP:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:ARUK-UCL.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; TAS:ProtInc.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; NAS:ARUK-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IMP:ARUK-UCL.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IGI:BHF-UCL.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:ARUK-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IGI:BHF-UCL.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:ARUK-UCL.
DR GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IMP:ARUK-UCL.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IMP:ARUK-UCL.
DR GO; GO:1902396; P:protein localization to bicellular tight junction; IMP:ARUK-UCL.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IDA:ARUK-UCL.
DR GO; GO:0043114; P:regulation of vascular permeability; IDA:ARUK-UCL.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0001944; P:vasculature development; IBA:GO_Central.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR030052; CDH5.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR PANTHER; PTHR24027:SF89; PTHR24027:SF89; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..47
FT /evidence="ECO:0000255"
FT /id="PRO_0000003755"
FT CHAIN 48..784
FT /note="Cadherin-5"
FT /id="PRO_0000003756"
FT TOPO_DOM 48..599
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..784
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..151
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 152..258
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 259..372
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 373..477
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 478..593
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 621..660
FT /note="Required for interaction with PALS1"
FT /evidence="ECO:0000250|UniProtKB:P55284"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490,
FT ECO:0000269|PubMed:21269602"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:21269602"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21269602"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21269602"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:21269602"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT VAR_SEQ 380..494
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_053861"
FT VARIANT 503
FT /note="I -> T (in dbSNP:rs16956504)"
FT /id="VAR_028003"
FT VARIANT 517
FT /note="I -> T (in dbSNP:rs1049970)"
FT /evidence="ECO:0000269|PubMed:10861224,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7627717"
FT /id="VAR_028004"
FT CONFLICT 602
FT /note="V -> A (in Ref. 4; AAH96363/AAI17521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 784 AA; 87528 MW; 6DBEBFC4DA6899D1 CRC64;
MQRLMMLLAT SGACLGLLAV AAVAAAGANP AQRDTHSLLP THRRQKRDWI WNQMHIDEEK
NTSLPHHVGK IKSSVSRKNA KYLLKGEYVG KVFRVDAETG DVFAIERLDR ENISEYHLTA
VIVDKDTGEN LETPSSFTIK VHDVNDNWPV FTHRLFNASV PESSAVGTSV ISVTAVDADD
PTVGDHASVM YQILKGKEYF AIDNSGRIIT ITKSLDREKQ ARYEIVVEAR DAQGLRGDSG
TATVLVTLQD INDNFPFFTQ TKYTFVVPED TRVGTSVGSL FVEDPDEPQN RMTKYSILRG
DYQDAFTIET NPAHNEGIIK PMKPLDYEYI QQYSFIVEAT DPTIDLRYMS PPAGNRAQVI
INITDVDEPP IFQQPFYHFQ LKENQKKPLI GTVLAMDPDA ARHSIGYSIR RTSDKGQFFR
VTKKGDIYNE KELDREVYPW YNLTVEAKEL DSTGTPTGKE SIVQVHIEVL DENDNAPEFA
KPYQPKVCEN AVHGQLVLQI SAIDKDITPR NVKFKFILNT ENNFTLTDNH DNTANITVKY
GQFDREHTKV HFLPVVISDN GMPSRTGTST LTVAVCKCNE QGEFTFCEDM AAQVGVSIQA
VVAILLCILT ITVITLLIFL RRRLRKQARA HGKSVPEIHE QLVTYDEEGG GEMDTTSYDV
SVLNSVRRGG AKPPRPALDA RPSLYAQVQK PPRHAPGAHG GPGEMAAMIE VKKDEADHDG
DGPPYDTLHI YGYEGSESIA ESLSSLGTDS SDSDVDYDFL NDWGPRFKML AELYGSDPRE
ELLY
