ID   CADH5_PIG               Reviewed;         782 AA.
AC   O02840;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   24-JAN-2024, entry version 120.
DE   RecName: Full=Cadherin-5;
DE   AltName: Full=Vascular endothelial cadherin;
DE            Short=VE-cadherin;
DE   AltName: CD_antigen=CD144;
DE   Flags: Precursor;
GN   Name=CDH5;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kilshaw P.J.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). This cadherin
CC       may play a important role in endothelial cell biology through control
CC       of the cohesion and organization of the intercellular junctions (By
CC       similarity). It associates with alpha-catenin forming a link to the
CC       cytoskeleton (By similarity). 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 (By similarity).
CC       Required for activation of PRKCZ and for localization of phosphorylated
CC       PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction (By similarity).
CC       {ECO:0000250|UniProtKB:P33151, ECO:0000250|UniProtKB:P55284,
CC       ECO:0000250|UniProtKB:Q8AYD0}.
CC   -!- SUBUNIT: Interacts (via cadherin 5 domain) with PTPRB (By similarity).
CC       Interacts with TRPC4 (By similarity). Interacts with KRIT1 (By
CC       similarity). Interacts with PARD3 (By similarity). Interacts with RTN4
CC       (isoform B) (By similarity). Interacts with PALS1; the interaction
CC       promotes PALS1 localization to cell junctions and is required for CDH5-
CC       mediated vascular lumen formation and endothelial cell (By similarity).
CC       {ECO:0000250|UniProtKB:P33151, ECO:0000250|UniProtKB:P55284}.
CC   -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000250|UniProtKB:P33151}.
CC       Cell membrane {ECO:0000250|UniProtKB:P33151}; Single-pass type I
CC       membrane protein {ECO:0000255}. Note=Found at cell-cell boundaries and
CC       probably at cell-matrix boundaries. KRIT1 and CDH5 reciprocally
CC       regulate their localization to endothelial cell-cell junctions.
CC       {ECO:0000250|UniProtKB:P33151}.
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:0000250}.
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DR   EMBL; Y13919; CAA74225.1; -; mRNA.
DR   RefSeq; NP_001001649.2; NM_001001649.2.
DR   AlphaFoldDB; O02840; -.
DR   SMR; O02840; -.
DR   STRING; 9823.ENSSSCP00000047033; -.
DR   GlyCosmos; O02840; 6 sites, No reported glycans.
DR   PeptideAtlas; O02840; -.
DR   Ensembl; ENSSSCT00055044391.1; ENSSSCP00055035372.1; ENSSSCG00055022576.1.
DR   GeneID; 414737; -.
DR   KEGG; ssc:414737; -.
DR   CTD; 1003; -.
DR   InParanoid; O02840; -.
DR   OrthoDB; 3667774at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
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:0005911; C:cell-cell junction; ISS:UniProtKB.
DR   GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
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:0044331; P:cell-cell adhesion mediated by cadherin; IBA:GO_Central.
DR   GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:1903659; P:regulation of complement-dependent cytotoxicity; IMP:AgBase.
DR   GO; GO:2000114; P:regulation of establishment of cell polarity; ISS: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.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell junction; Cell membrane;
KW   Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..44
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003759"
FT   CHAIN           45..782
FT                   /note="Cadherin-5"
FT                   /id="PRO_0000003760"
FT   TOPO_DOM        45..598
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        599..619
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        620..782
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          45..148
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          149..255
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          256..370
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          371..475
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          476..592
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REGION          620..659
FT                   /note="Required for interaction with PALS1"
FT                   /evidence="ECO:0000250|UniProtKB:P55284"
FT   BINDING         55
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         108
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
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="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        154
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        534
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   782 AA;  87546 MW;  7403F974E2DF782F CRC64;
     MQVLVMLLAA AGTYLGLLTA PTAASNPGRQ DTPSTLPLHR RQKRDWIWNQ MHIDEEKNGS
     LPHYVGKIKS SVNHKNTKYQ LKGESAGKVF RVDENTGDVY AFERLDREKI PEYQLVALVV
     DKNTEKNLES PSSFTIKVHD INDNWPVFTQ LVFNASVPEM SVIGTSVIQL TAVDADDPTV
     ADHASVIYRL KEGEEHFRIR GPGLIETASK NLDRETVPMY KIVVETQDAQ GLRGDSGTAT
     VFITLQDVND NFPVFTQTRY TFSVPEDIRV GSPLGSLFVK DPDEPQNRKT KYSIVQGEYR
     DTFTIEPDPT RNEGIIKPMK PLDYERIQQY SFTIEATDPT IDLRYLSGTS TKNIARVIIN
     VTDVDEPPNF KQPFYHFQLR ENEKKPWIGS VLAVDPDAAQ RSIGYSIRRT SDKGQFFGIN
     KHGNIYNVKE LDREVYPWYN LTVEAKELDS RGTPTGKESI VQVHIEVLDE NDNAPEFAKP
     YEAKVCEDAP QGKLVVQISA IDKDVTPRDV KFKFSLSTED SNFTLTDNHD NTANITVKHG
     YFDRERAKVH HLPILISDNG RPSLTGTSTL HVTVCKCNER GEFTLCEEMG AQVGVSIQAL
     VAIFLCILTI AVISLLVYLR RRLRKQARAH GKSVPEIHEQ LVTYDEEGGG EMDTTSYDVS
     VLNSVRHGGA KPPRPALDAR PSLYAQVQKP PRHAPGAHAP GEMAAMIEVK KDEADHDGGG
     PPYDTLHIFG YEGAESIAES LSSLGTDSSD SDIDYDFLND WGPRFKMLAE LYGSDPREEL
     LY
//