CADH5_CHICK
ID CADH5_CHICK Reviewed; 773 AA.
AC Q8AYD0; F1P1Y9;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cadherin-5 {ECO:0000250|UniProtKB:P33151};
DE AltName: Full=Vascular endothelial cadherin {ECO:0000303|PubMed:21269602};
DE Short=VE-cadherin {ECO:0000303|PubMed:21269602};
DE Flags: Precursor;
GN Name=CDH5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000312|EMBL:AAN33002.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Romero S., Jaffredo T., Dunon D.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [3] {ECO:0000305, ECO:0000312|PDB:3PPE}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 41-243 IN COMPLEX WITH CALCIUM,
RP FUNCTION, DOMAIN, AND GLYCOSYLATION.
RX PubMed=21269602; DOI=10.1016/j.jmb.2011.01.031;
RA Brasch J., Harrison O.J., Ahlsen G., Carnally S.M., Henderson R.M.,
RA Honig B., Shapiro L.;
RT "Structure and binding mechanism of vascular endothelial cadherin: a
RT divergent classical cadherin.";
RL J. Mol. Biol. 408:57-73(2011).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells; cadherins may thus contribute to the sorting of
CC heterogeneous cell types. This cadherin may play a important role in
CC endothelial cell biology through control of the cohesion and
CC organization of the intercellular junctions.
CC {ECO:0000269|PubMed:21269602}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000250|UniProtKB:P33151}.
CC Cell membrane {ECO:0000250|UniProtKB:P33151}; Single-pass type I
CC membrane protein {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:0000269|PubMed:21269602}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:21269602}.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:21269602}.
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DR EMBL; AF522067; AAN33002.1; -; mRNA.
DR EMBL; AADN03006318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_989558.1; NM_204227.1.
DR PDB; 3PPE; X-ray; 2.10 A; A/B=41-243.
DR PDBsum; 3PPE; -.
DR AlphaFoldDB; Q8AYD0; -.
DR SMR; Q8AYD0; -.
DR STRING; 9031.ENSGALP00000008445; -.
DR PaxDb; Q8AYD0; -.
DR Ensembl; ENSGALT00000063435; ENSGALP00000043893; ENSGALG00000032349.
DR GeneID; 374068; -.
DR KEGG; gga:374068; -.
DR CTD; 1003; -.
DR VEuPathDB; HostDB:geneid_374068; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000160587; -.
DR HOGENOM; CLU_005284_3_2_1; -.
DR OMA; NVKFKFA; -.
DR OrthoDB; 259069at2759; -.
DR PhylomeDB; Q8AYD0; -.
DR TreeFam; TF329887; -.
DR Reactome; R-GGA-418990; Adherens junctions interactions.
DR Reactome; R-GGA-5218920; VEGFR2 mediated vascular permeability.
DR PRO; PR:Q8AYD0; -.
DR Proteomes; UP000000539; Chromosome 11.
DR Bgee; ENSGALG00000032349; Expressed in lung and 12 other tissues.
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: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:0060317; P:cardiac epithelial to mesenchymal transition; IMP:AgBase.
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:2000114; P:regulation of establishment of cell polarity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..40
FT /evidence="ECO:0000250|UniProtKB:P33151, ECO:0000255"
FT /id="PRO_0000425446"
FT CHAIN 41..773
FT /note="Cadherin-5"
FT /evidence="ECO:0000250|UniProtKB:P33151"
FT /id="PRO_0000425447"
FT TOPO_DOM 41..595
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..617
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..773
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..144
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 145..251
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 252..366
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 367..474
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 474..582
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 104
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21269602"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21269602"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 202
FT /note="S -> F (in Ref. 1; AAN33002)"
FT /evidence="ECO:0000305"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:3PPE"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:3PPE"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:3PPE"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:3PPE"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:3PPE"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:3PPE"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:3PPE"
FT STRAND 231..242
FT /evidence="ECO:0007829|PDB:3PPE"
SQ SEQUENCE 773 AA; 86782 MW; 04B7BE173745B0D2 CRC64;
MKKLILLFSL FLAPAFSYKE NQKINQNFSS NNTSHKRLKR DWIWNRMHIR EEIDSPLPHH
VGKLTSSVGN KNAMYIIEGE SANTIFKVQG YDGDIYAFER LDREKKAEYE LTAHIIDRRN
NRSLEPPSKF IIKVSDINDN APIFVQKIFN GSVPEMSRLG TSVTKVTAED ADDPTVAGHA
TVTYQIIKGN EYFTVDDSGV ISTARADLDR ESQSAYEIIV KAKDALGLTG ESSTATVIIR
LTDINDNFPV FKHPSFHFRV PENISVGGEV GRVKVEDIDE PQHRNTKYSF VRGDYRDTFE
IIANPFTNEG IIRPKKPLDF EKVAEYRFDI EATDHNVNPA YYKPGGSRSI STITIEVTDV
DEPPVFTKLS YEFKVRENDP EIKTLGSVWA HDPDAAKRKI RFARRRASPN GDYVRVSDSG
IIQLPKPLDR EFSSLYNITV AAQEILEDGR LSDRESHAQV HVIVTDENDN APELVYPEEP
RVCENAAPGK VIIRISATDK DEISPGGFFT YSLTTEDSNF SLTENPDNTA NITVKDGQFN
RELAKIHYLP VIISDNGNPE LSSTNTLVIS VCKCNEKGDF TFCEERAKQV GVSVQALVAI
FICIFTIIAV IALLILLRKR HKKDLSGLRR NVAEIHEQLV TYDEEGGGEM DTTSYDVSVL
NSVRKNGIKP EVVPSAYAQV QKPPGNTTSG AGEMEMMIEV KKDEADNDRD LLPYDTLHIY
GYEGAESIAE SLSSLESGSS DSDIDYDFLN DWGPRFKMLA ELYGSEPNED FVY
