ID A0A384D115_URSMA Unreviewed; 783 AA.
AC A0A384D115;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 2.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Cadherin-5 {ECO:0000256|ARBA:ARBA00021701};
DE AltName: Full=Vascular endothelial cadherin {ECO:0000256|ARBA:ARBA00030559};
GN Name=CDH5 {ECO:0000313|RefSeq:XP_008700743.2};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008700743.2};
RN [1] {ECO:0000313|RefSeq:XP_008700743.2}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008700743.2};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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DR RefSeq; XP_008700743.2; XM_008702521.2.
DR STRING; 29073.ENSUMAP00000029128; -.
DR KEGG; umr:103673688; -.
DR OrthoDB; 3667774at2759; -.
DR Proteomes; UP000261680; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 5.
DR Gene3D; 2.60.40.60; Cadherins; 5.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 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_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF89; CADHERIN-5; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 5.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; Cadherin-like; 5.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003318};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000261680};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..783
FT /note="Cadherin-5"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035476390"
FT TRANSMEM 599..619
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 78..148
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 149..255
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 256..370
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 371..477
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 477..584
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
SQ SEQUENCE 783 AA; 87781 MW; 6D242BE7CF253B67 CRC64;
MQVLVLLLAS VGTCLGLLVA AAAGTTPARP DPPSVLPIHR RQKRDWIWNQ MHIDEEKNTS
LPHYVGKIKS SVNRKNAKYV LKGESVGKVF RVREDTGDVY AFERLDREKI PEYHLTALVV
DKNTNKNLES PSSFTIKVHD VNDNWPVFTH RLFNASVPEM SAVGTSVIRV TAVDADDPTV
ADHASVMYQI LKGEEYFAID GSGLIFTTTK TLDREMQAKY EIVVEARDAQ GLRGESGTAT
VLVTLQDIND NFPIFTQPKY TFAVPEDIRV GSSLGSLFVE DPDEPQNRMT KYSIVQGEYR
DTFTIETDPN HNEGIIKPMK PLDYEYIQQY IFTIEATDPT INLHYLSSVS IRKTARVIIN
VTDVDEPPNF KQSFYHFQLR ENQKKPLIGS VLATDPDAAR RSIGYSIRKT SDKGQFFRIT
KQGNIYNEKE LDREIYPWYN LTVEAKELDS SGYPTGKESI VQVHIEIMDE NDNPPEFAQP
YEPRVCENAA QGKLVVQISA IDKDITPRDV KFKFSLTTED SNFTLTDNHD NTANITVKYG
QFDRERAKVH HLPVLISDNG RPSLTGTSTL VVTICKCNEH GEFTHCEEMA GQAGVSIQAL
VAIFLCILTI TVITLLIFLR RRLRKQARAH GKSVPEIHEQ LVTYDEEGGG EMDTTSYDVS
VLNSVRHGGS KPPRPALEAR PSVYAQVQKP PRHAPAVHGG PGEMAAMIEV KKDEADHDGG
GPPYDTLHIY GYEGAESIAE SLSSLGTDSS DSDIDYDFLN DWGPRFKMLA ELYRSDPQEE
LLY
//