CADH5_BOVIN
ID CADH5_BOVIN Reviewed; 783 AA.
AC Q6URK6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=14672921; DOI=10.1152/ajplung.00305.2003;
RA Iyer S., Ferreri D.M., DeCocco N.C., Minnear F.L., Vincent P.A.;
RT "VE-cadherin-p120 interaction is required for maintenance of endothelial
RT barrier function.";
RL Am. J. Physiol. 286:L1143-L1153(2004).
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:0000269|PubMed:14672921}. Cell
CC membrane {ECO:0000269|PubMed:14672921}; Single-pass type I membrane
CC protein {ECO:0000255}. Note=Found at cell-cell boundaries and probably
CC at cell-matrix boundaries. KRIT1 and CDH5 reciprocally regulate their
CC 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; AY363224; AAQ63484.1; -; mRNA.
DR RefSeq; NP_001001601.1; NM_001001601.1.
DR AlphaFoldDB; Q6URK6; -.
DR SMR; Q6URK6; -.
DR DIP; DIP-48767N; -.
DR IntAct; Q6URK6; 1.
DR STRING; 9913.ENSBTAP00000009760; -.
DR PaxDb; Q6URK6; -.
DR PRIDE; Q6URK6; -.
DR GeneID; 414735; -.
DR KEGG; bta:414735; -.
DR CTD; 1003; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q6URK6; -.
DR OrthoDB; 259069at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0001955; P:blood vessel maturation; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
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..25
FT /evidence="ECO:0000255"
FT PROPEP 26..45
FT /evidence="ECO:0000255"
FT /id="PRO_0000247562"
FT CHAIN 46..783
FT /note="Cadherin-5"
FT /id="PRO_0000247563"
FT TOPO_DOM 46..599
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..783
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 44..149
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 150..256
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 257..371
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 372..478
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 478..585
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 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
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 109
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="2"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 175
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="2"
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 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 783 AA; 87467 MW; 9193F3BAA3298D3D CRC64;
MQALVMLLAT GATYYLGLLA AAAAAVNPGR PNTPGSLPAH RRQKRDWIWN QMHIDEERND
SLPHYVGKIK SSVDPKKTEY QLRGESAGKV FRVDKNTGDV YALERLDREK ISEYHLTALV
VDKDSKKNLE SPSSFTIKVH DVNDNWPVFT HRVFNASVPE MSGIGTSVIQ VTAMDADDPT
VADHASVVYQ LTKGKENFDI RGSGLIVTMN KHLDRETQDK YEVVVKAEDA QGRRGESGTA
TVFITLQDVN DNFPIFTQNR YTFSVPEDIR VGSPLGSLFV EDPDEPQNRK TKYSFVQGEY
RDTFTIDTDP SHNEGIIKPI KPLDYERIRQ YSFTIEATDP TIDLRYLGST SPKNIARVII
NVTDVDEPPI FQQPFYHFQL QENQKKPLIG SVLAKDPDAA QRDIRYSIRR TSDKGQFFGI
TKKGGIYNDK ELDREVYPWY NLTVEAKEVD LSGTPTGKES IVQVHIEVMD ENDNAPEFAK
PYEPKVCENA PQGKLVVQIS ATDKDITPRD VKFKFSLSTE DSNFTLIDNH DNTANIIVKY
GYFDRERAKV HHLPVLISDN GRPSLTGTST LHVTVCKCNE HGEFTLCEEA AAQVGISIQA
LVAIFLCILT FTVITLLIIL RRRLRKQARA HGKSVPEIHE QLVTYDEEGG GEMDTTSYDV
SVLNSARHGG AKPPRPALDA RPSLYAQVQK PPRQAPGAHA PGEMAAMIGV KKDEADHDGG
GPPYDTLHIY GYEGAESIAE SLSSLGTDSS DSDIDYDFLN DWGTRFKMLA ELYGSDPQEE
LVY
