CADH5_PIG
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 03-AUG-2022, entry version 114.
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 PeptideAtlas; O02840; -.
DR PRIDE; O02840; -.
DR Ensembl; ENSSSCT00055044391; ENSSSCP00055035372; ENSSSCG00055022576.
DR GeneID; 414737; -.
DR KEGG; ssc:414737; -.
DR CTD; 1003; -.
DR InParanoid; O02840; -.
DR OrthoDB; 259069at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0001955; P:blood vessel maturation; IEA:InterPro.
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:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; 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 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 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
