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Protein

Cadherin-5

Gene

Cdh5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. This cadherin may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. Acts in concert with KRIT1 to establish and maintain correct endothelial cell polarity and vascular lumen. These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for activation of PRKCZ and for localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi56Calcium 1By similarity1
Metal bindingi56Calcium 2By similarity1
Metal bindingi57Calcium 1By similarity1
Metal bindingi107Calcium 1By similarity1
Metal bindingi109Calcium 1By similarity1
Metal bindingi109Calcium 2By similarity1
Metal bindingi141Calcium 2By similarity1
Metal bindingi142Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi143Calcium 3By similarity1
Metal bindingi144Calcium 1By similarity1
Metal bindingi144Calcium 2By similarity1
Metal bindingi145Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi175Calcium 3By similarity1
Metal bindingi177Calcium 2By similarity1
Metal bindingi177Calcium 3By similarity1
Metal bindingi184Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi229Calcium 3By similarity1

GO - Molecular functioni

GO - Biological processi

  • blood vessel maturation Source: MGI
  • cell-cell adhesion Source: MGI
  • cell-cell junction assembly Source: MGI
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: InterPro
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of inflammatory response Source: MGI
  • positive regulation of angiogenesis Source: MGI
  • positive regulation of establishment of endothelial barrier Source: MGI
  • regulation of establishment of cell polarity Source: UniProtKB
  • transforming growth factor beta receptor signaling pathway Source: MGI

Keywordsi

Biological processCell adhesion
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-418990 Adherens junctions interactions
R-MMU-5218920 VEGFR2 mediated vascular permeability

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-5
Alternative name(s):
Vascular endothelial cadherin
Short name:
VE-cadherin
CD_antigen: CD144
Gene namesi
Name:Cdh5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:105057 Cdh5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini46 – 599ExtracellularSequence analysisAdd BLAST554
Transmembranei600 – 620HelicalSequence analysisAdd BLAST21
Topological domaini621 – 784CytoplasmicSequence analysisAdd BLAST164

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi774Y → A: No effect on PARD3 binding. 1 Publication1
Mutagenesisi777D → A: Impairs PARD3 binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000000375725 – 45Sequence analysisAdd BLAST21
ChainiPRO_000000375846 – 784Cadherin-5Add BLAST739

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi59N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi155N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi441N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi523N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi535N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Phosphorylated on tyrosine residues by KDR/VEGFR-2. Dephosphorylated by PTPRB.1 Publication
O-glycosylated.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP55284
PaxDbiP55284
PeptideAtlasiP55284
PRIDEiP55284

PTM databases

iPTMnetiP55284
PhosphoSitePlusiP55284

Expressioni

Developmental stagei

Expressed in endothelial cells of allantois/umbilical vessels at 8.5 dpc (at protein level). During hemangioblast differentiation, expressed in hemogenic endothelium cells and down-regulated in nascent blood precursors.2 Publications

Inductioni

Up-regulated by SOX7.1 Publication

Gene expression databases

BgeeiENSMUSG00000031871
CleanExiMM_CDH5
ExpressionAtlasiP55284 baseline and differential
GenevisibleiP55284 MM

Interactioni

Subunit structurei

Interacts (via cadherin 5 domain) with PTPRB. Interacts with TRPC4. Interacts with KRIT1 (By similarity). Interacts with PARD3.By similarity2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198640, 4 interactors
CORUMiP55284
ELMiP55284
IntActiP55284, 10 interactors
MINTiP55284
STRINGi10090.ENSMUSP00000034339

Structurei

Secondary structure

1784
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi773 – 776Combined sources4
Beta strandi781 – 783Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KOHNMR-B769-784[»]
ProteinModelPortaliP55284
SMRiP55284
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55284

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 149Cadherin 1PROSITE-ProRule annotationAdd BLAST104
Domaini150 – 256Cadherin 2PROSITE-ProRule annotationAdd BLAST107
Domaini257 – 371Cadherin 3PROSITE-ProRule annotationAdd BLAST115
Domaini372 – 476Cadherin 4PROSITE-ProRule annotationAdd BLAST105
Domaini477 – 593Cadherin 5PROSITE-ProRule annotationAdd BLAST117

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi738 – 753Ser-richAdd BLAST16

Domaini

Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.By similarity

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3594 Eukaryota
ENOG410XQHI LUCA
GeneTreeiENSGT00900000140970
HOGENOMiHOG000231252
HOVERGENiHBG005217
InParanoidiP55284
KOiK06533
OMAiHGKSVPE
OrthoDBiEOG091G03WQ
PhylomeDBiP55284
TreeFamiTF329887

Family and domain databases

Gene3Di4.10.900.10, 1 hit
InterProiView protein in InterPro
IPR002126 Cadherin
IPR015919 Cadherin-like
IPR020894 Cadherin_CS
IPR000233 Cadherin_cytoplasmic-dom
IPR027397 Catenin_binding_dom_sf
IPR030052 CDH5
PANTHERiPTHR24027:SF89 PTHR24027:SF89, 1 hit
PfamiView protein in Pfam
PF00028 Cadherin, 5 hits
PF01049 Cadherin_C, 1 hit
PRINTSiPR00205 CADHERIN
SMARTiView protein in SMART
SM00112 CA, 5 hits
SUPFAMiSSF49313 SSF49313, 5 hits
PROSITEiView protein in PROSITE
PS00232 CADHERIN_1, 3 hits
PS50268 CADHERIN_2, 5 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P55284-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRLTELATA LGAFLGLLAV AAMAGPNFPQ IDTPNMLPAH HRQKRDWIWN
60 70 80 90 100
QMHIDEEKNE SLPHYVGKIK SNVNRQNAKY VLQGEFAGKI FGVDANTGNV
110 120 130 140 150
LAYERLDREK VSEYFLTALI VDKNTNKNLE QPSSFTVKVH DINDNWPVFS
160 170 180 190 200
HQVFNASVPE MSAIGTSVIR VTAVDADDPT VAGHATVLYQ IVKGNEYFSI
210 220 230 240 250
DNSGLIFTKI KNLDREKQAE YKIVVETQDA LGLRGESGTA TVMIRLEDIN
260 270 280 290 300
DNFPVFTQST YTFSVPEDIR VGKPLGFLTV VDPDEPQNRM TKYSIMQGEY
310 320 330 340 350
RDTFTIETDP KRNEGIIKPT KSLDYEVIQQ YTFYIEATDP TIRYEYLSST
360 370 380 390 400
SGKNKAMVTI NVLDVDEPPV FQRHFYHFKL PENQKKPLIG TVVAKDPDKA
410 420 430 440 450
QRSIGYSIRK TSDRGQFFRI TKQGNIYNEK ELDRETYAWY NLTVEANELD
460 470 480 490 500
SRGNPVGKES IVQVYIEVLD ENDNPPEFAQ PYEPKVCENA AQGKLVVQIS
510 520 530 540 550
ATDKDVVPVN PKFKFALKNE DSNFTLINNH DNTANITVKY GQFNREHAKF
560 570 580 590 600
HYLPVLISDN GVPSLTGTST LTVGVCKCNE QGEFTFCEEM AAQAGVSIQA
610 620 630 640 650
LVAIFLCILT ITVITLLIIL RRRIRKQAHA HSKSALEIHE QLVTYDEEGG
660 670 680 690 700
GEMDTTSYDV SVLNSVRGGS TKPLRSTMDA RPAVYTQVQK PPRLAPGLHG
710 720 730 740 750
GPREMATMID VKKEEADNDG GGPPYDTLHI YGYEGAESIA ESLSSLSTNS
760 770 780
SDSDIDYDFL NDWGPRFKML AELYGSDPQE ELII
Length:784
Mass (Da):87,903
Last modified:September 9, 2003 - v2
Checksum:i7B75698DE2F7E160
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83930 mRNA Translation: CAA58782.2
D63942 mRNA Translation: BAA22617.1
BC054790 mRNA Translation: AAH54790.1
CCDSiCCDS22572.1
RefSeqiNP_033998.2, NM_009868.4
XP_006530693.1, XM_006530630.1
UniGeneiMm.21767

Genome annotation databases

EnsembliENSMUST00000034339; ENSMUSP00000034339; ENSMUSG00000031871
GeneIDi12562
KEGGimmu:12562
UCSCiuc009mzx.2 mouse

Similar proteinsi

Entry informationi

Entry nameiCADH5_MOUSE
AccessioniPrimary (citable) accession number: P55284
Secondary accession number(s): O35542
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 9, 2003
Last modified: May 23, 2018
This is version 148 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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