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O02840 (CADH5_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cadherin-5
Alternative name(s):
Vascular endothelial cadherin
Short name=VE-cadherin
CD_antigen=CD144
Gene names
Name:CDH5
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length782 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 a important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. It associates with alpha-catenin forming a link to the cytoskeleton. 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 By similarity.

Subunit structure

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

Subcellular location

Cell junction By similarity. Cell membrane; Single-pass type I membrane protein. Note: Found at cell-cell boundaries and probably at cell-matrix boundaries. KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions By similarity.

Domain

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.

Post-translational modification

Phosphorylated on tyrosine residues by KDR/VEGFR-2. Dephosphorylated by PTPRB By similarity.

O-glycosylated By similarity.

Sequence similarities

Contains 5 cadherin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 4422 Potential
PRO_0000003759
Chain45 – 782738Cadherin-5
PRO_0000003760

Regions

Topological domain45 – 598554Extracellular Potential
Transmembrane599 – 61921Helical; Potential
Topological domain620 – 782163Cytoplasmic Potential
Domain45 – 148104Cadherin 1
Domain149 – 255107Cadherin 2
Domain256 – 370115Cadherin 3
Domain371 – 475105Cadherin 4
Domain476 – 592117Cadherin 5
Compositional bias736 – 75116Ser-rich

Sites

Metal binding551Calcium 1 By similarity
Metal binding551Calcium 2 By similarity
Metal binding561Calcium 1 By similarity
Metal binding1061Calcium 1 By similarity
Metal binding1081Calcium 1 By similarity
Metal binding1081Calcium 2 By similarity
Metal binding1401Calcium 2 By similarity
Metal binding1411Calcium 2; via carbonyl oxygen By similarity
Metal binding1421Calcium 3 By similarity
Metal binding1431Calcium 1 By similarity
Metal binding1431Calcium 2 By similarity
Metal binding1441Calcium 3; via carbonyl oxygen By similarity
Metal binding1741Calcium 3 By similarity
Metal binding1761Calcium 2 By similarity
Metal binding1761Calcium 3 By similarity
Metal binding1831Calcium 3; via carbonyl oxygen By similarity
Metal binding2281Calcium 3 By similarity

Amino acid modifications

Glycosylation581N-linked (GlcNAc...) Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation3601N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Potential
Glycosylation5221N-linked (GlcNAc...) Potential
Glycosylation5341N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O02840 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 7403F974E2DF782F

FASTA78287,546
        10         20         30         40         50         60 
MQVLVMLLAA AGTYLGLLTA PTAASNPGRQ DTPSTLPLHR RQKRDWIWNQ MHIDEEKNGS 

        70         80         90        100        110        120 
LPHYVGKIKS SVNHKNTKYQ LKGESAGKVF RVDENTGDVY AFERLDREKI PEYQLVALVV 

       130        140        150        160        170        180 
DKNTEKNLES PSSFTIKVHD INDNWPVFTQ LVFNASVPEM SVIGTSVIQL TAVDADDPTV 

       190        200        210        220        230        240 
ADHASVIYRL KEGEEHFRIR GPGLIETASK NLDRETVPMY KIVVETQDAQ GLRGDSGTAT 

       250        260        270        280        290        300 
VFITLQDVND NFPVFTQTRY TFSVPEDIRV GSPLGSLFVK DPDEPQNRKT KYSIVQGEYR 

       310        320        330        340        350        360 
DTFTIEPDPT RNEGIIKPMK PLDYERIQQY SFTIEATDPT IDLRYLSGTS TKNIARVIIN 

       370        380        390        400        410        420 
VTDVDEPPNF KQPFYHFQLR ENEKKPWIGS VLAVDPDAAQ RSIGYSIRRT SDKGQFFGIN 

       430        440        450        460        470        480 
KHGNIYNVKE LDREVYPWYN LTVEAKELDS RGTPTGKESI VQVHIEVLDE NDNAPEFAKP 

       490        500        510        520        530        540 
YEAKVCEDAP QGKLVVQISA IDKDVTPRDV KFKFSLSTED SNFTLTDNHD NTANITVKHG 

       550        560        570        580        590        600 
YFDRERAKVH HLPILISDNG RPSLTGTSTL HVTVCKCNER GEFTLCEEMG AQVGVSIQAL 

       610        620        630        640        650        660 
VAIFLCILTI AVISLLVYLR RRLRKQARAH GKSVPEIHEQ LVTYDEEGGG EMDTTSYDVS 

       670        680        690        700        710        720 
VLNSVRHGGA KPPRPALDAR PSLYAQVQKP PRHAPGAHAP GEMAAMIEVK KDEADHDGGG 

       730        740        750        760        770        780 
PPYDTLHIFG YEGAESIAES LSSLGTDSSD SDIDYDFLND WGPRFKMLAE LYGSDPREEL 


LY 

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References

[1]Kilshaw P.J.
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13919 mRNA. Translation: CAA74225.1.
RefSeqNP_001001649.2. NM_001001649.2.
UniGeneSsc.75.

3D structure databases

ProteinModelPortalO02840.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID414737.
KEGGssc:414737.

Organism-specific databases

CTD1003.

Phylogenomic databases

HOVERGENHBG005217.
KOK06533.

Family and domain databases

Gene3D2.60.40.60. 5 hits.
4.10.900.10. 1 hit.
InterProIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR027397. Catenin_binding_dom.
[Graphical view]
PfamPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
[Graphical view]
PRINTSPR00205. CADHERIN.
SMARTSM00112. CA. 5 hits.
[Graphical view]
SUPFAMSSF49313. SSF49313. 5 hits.
PROSITEPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCADH5_PIG
AccessionPrimary (citable) accession number: O02840
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families