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O02840

- CADH5_PIG

UniProt

O02840 - CADH5_PIG

Protein

Cadherin-5

Gene

CDH5

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    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 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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi55 – 551Calcium 1By similarity
    Metal bindingi55 – 551Calcium 2By similarity
    Metal bindingi56 – 561Calcium 1By similarity
    Metal bindingi106 – 1061Calcium 1By similarity
    Metal bindingi108 – 1081Calcium 1By similarity
    Metal bindingi108 – 1081Calcium 2By similarity
    Metal bindingi140 – 1401Calcium 2By similarity
    Metal bindingi141 – 1411Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi142 – 1421Calcium 3By similarity
    Metal bindingi143 – 1431Calcium 1By similarity
    Metal bindingi143 – 1431Calcium 2By similarity
    Metal bindingi144 – 1441Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi174 – 1741Calcium 3By similarity
    Metal bindingi176 – 1761Calcium 2By similarity
    Metal bindingi176 – 1761Calcium 3By similarity
    Metal bindingi183 – 1831Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi228 – 2281Calcium 3By similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro

    GO - Biological processi

    1. homophilic cell adhesion Source: InterPro
    2. regulation of establishment of cell polarity Source: UniProtKB

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Metal-binding

    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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. cell-cell junction Source: UniProtKB
    2. cell junction Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 4422Sequence AnalysisPRO_0000003759Add
    BLAST
    Chaini45 – 782738Cadherin-5PRO_0000003760Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi58 – 581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi522 – 5221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi534 – 5341N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

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

    Keywords - PTMi

    Cleavage on pair of basic residues, Glycoprotein, Phosphoprotein

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliO02840.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini45 – 598554ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini620 – 782163CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei599 – 61921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 148104Cadherin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini149 – 255107Cadherin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini256 – 370115Cadherin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini371 – 475105Cadherin 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini476 – 592117Cadherin 5PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi736 – 75116Ser-richAdd
    BLAST

    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

    Sequence similaritiesi

    Contains 5 cadherin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG005217.
    KOiK06533.

    Family and domain databases

    Gene3Di2.60.40.60. 5 hits.
    4.10.900.10. 1 hit.
    InterProiIPR002126. Cadherin.
    IPR015919. Cadherin-like.
    IPR020894. Cadherin_CS.
    IPR000233. Cadherin_cytoplasmic-dom.
    IPR027397. Catenin_binding_dom.
    [Graphical view]
    PfamiPF00028. Cadherin. 5 hits.
    PF01049. Cadherin_C. 1 hit.
    [Graphical view]
    PRINTSiPR00205. CADHERIN.
    SMARTiSM00112. CA. 5 hits.
    [Graphical view]
    SUPFAMiSSF49313. SSF49313. 5 hits.
    PROSITEiPS00232. CADHERIN_1. 3 hits.
    PS50268. CADHERIN_2. 5 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O02840-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQVLVMLLAA AGTYLGLLTA PTAASNPGRQ DTPSTLPLHR RQKRDWIWNQ    50
    MHIDEEKNGS LPHYVGKIKS SVNHKNTKYQ LKGESAGKVF RVDENTGDVY 100
    AFERLDREKI PEYQLVALVV DKNTEKNLES PSSFTIKVHD INDNWPVFTQ 150
    LVFNASVPEM SVIGTSVIQL TAVDADDPTV ADHASVIYRL KEGEEHFRIR 200
    GPGLIETASK NLDRETVPMY KIVVETQDAQ GLRGDSGTAT VFITLQDVND 250
    NFPVFTQTRY TFSVPEDIRV GSPLGSLFVK DPDEPQNRKT KYSIVQGEYR 300
    DTFTIEPDPT RNEGIIKPMK PLDYERIQQY SFTIEATDPT IDLRYLSGTS 350
    TKNIARVIIN VTDVDEPPNF KQPFYHFQLR ENEKKPWIGS VLAVDPDAAQ 400
    RSIGYSIRRT SDKGQFFGIN KHGNIYNVKE LDREVYPWYN LTVEAKELDS 450
    RGTPTGKESI VQVHIEVLDE NDNAPEFAKP YEAKVCEDAP QGKLVVQISA 500
    IDKDVTPRDV KFKFSLSTED SNFTLTDNHD NTANITVKHG YFDRERAKVH 550
    HLPILISDNG RPSLTGTSTL HVTVCKCNER GEFTLCEEMG AQVGVSIQAL 600
    VAIFLCILTI AVISLLVYLR RRLRKQARAH GKSVPEIHEQ LVTYDEEGGG 650
    EMDTTSYDVS VLNSVRHGGA KPPRPALDAR PSLYAQVQKP PRHAPGAHAP 700
    GEMAAMIEVK KDEADHDGGG PPYDTLHIFG YEGAESIAES LSSLGTDSSD 750
    SDIDYDFLND WGPRFKMLAE LYGSDPREEL LY 782
    Length:782
    Mass (Da):87,546
    Last modified:July 1, 1997 - v1
    Checksum:i7403F974E2DF782F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13919 mRNA. Translation: CAA74225.1.
    RefSeqiNP_001001649.2. NM_001001649.2.
    UniGeneiSsc.75.

    Genome annotation databases

    GeneIDi414737.
    KEGGissc:414737.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13919 mRNA. Translation: CAA74225.1 .
    RefSeqi NP_001001649.2. NM_001001649.2.
    UniGenei Ssc.75.

    3D structure databases

    ProteinModelPortali O02840.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 414737.
    KEGGi ssc:414737.

    Organism-specific databases

    CTDi 1003.

    Phylogenomic databases

    HOVERGENi HBG005217.
    KOi K06533.

    Family and domain databases

    Gene3Di 2.60.40.60. 5 hits.
    4.10.900.10. 1 hit.
    InterProi IPR002126. Cadherin.
    IPR015919. Cadherin-like.
    IPR020894. Cadherin_CS.
    IPR000233. Cadherin_cytoplasmic-dom.
    IPR027397. Catenin_binding_dom.
    [Graphical view ]
    Pfami PF00028. Cadherin. 5 hits.
    PF01049. Cadherin_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00205. CADHERIN.
    SMARTi SM00112. CA. 5 hits.
    [Graphical view ]
    SUPFAMi SSF49313. SSF49313. 5 hits.
    PROSITEi PS00232. CADHERIN_1. 3 hits.
    PS50268. CADHERIN_2. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

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

    Entry informationi

    Entry nameiCADH5_PIG
    AccessioniPrimary (citable) accession number: O02840
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3