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   24-JAN-2024, entry version 206.
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; 108.
DR   CORUM; P33151; -.
DR   DIP; DIP-41172N; -.
DR   IntAct; P33151; 78.
DR   MINT; P33151; -.
DR   STRING; 9606.ENSP00000497290; -.
DR   DrugBank; DB05685; FX06.
DR   DrugBank; DB00480; Lenalidomide.
DR   GlyConnect; 617; 30 N-Linked glycans (4 sites).
DR   GlyCosmos; P33151; 7 sites, 42 glycans.
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; 9606-ENSP00000344115; -.
DR   PeptideAtlas; P33151; -.
DR   ProteomicsDB; 54900; -. [P33151-1]
DR   TopDownProteomics; P33151-1; -. [P33151-1]
DR   Antibodypedia; 3717; 1443 antibodies from 43 providers.
DR   DNASU; 1003; -.
DR   Ensembl; ENST00000341529.8; ENSP00000344115.3; ENSG00000179776.20. [P33151-1]
DR   Ensembl; ENST00000649567.1; ENSP00000497290.1; ENSG00000179776.20. [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   AGR; HGNC:1764; -.
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; DCPIGIN; -.
DR   OrthoDB; 3667774at2759; -.
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; 38 hits in 1150 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 180 other cell types or tissues.
DR   ExpressionAtlas; P33151; baseline and differential.
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: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:0007043; P:cell-cell junction assembly; IMP:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; TAS:ProtInc.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IDA:ARUK-UCL.
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   CDD; cd11304; Cadherin_repeat; 5.
DR   Gene3D; 2.60.40.60; Cadherins; 5.
DR   Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 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_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   PANTHER; PTHR24027:SF89; CADHERIN-5; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 5.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin-like; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
DR   Genevisible; P33151; HS.
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
//