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Database: UniProt
Entry: E1BF53_BOVIN
LinkDB: E1BF53_BOVIN
Original site: E1BF53_BOVIN 
ID   E1BF53_BOVIN            Unreviewed;       785 AA.
AC   E1BF53;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 2.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Cadherin 7 {ECO:0000313|Ensembl:ENSBTAP00000031052.4};
GN   Name=CDH7 {ECO:0000313|Ensembl:ENSBTAP00000031052.4,
GN   ECO:0000313|VGNC:VGNC:27106};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000031052.4, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000031052.4, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000031052.4,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000031052.4}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000031052.4};
RG   Ensembl;
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; NP_001179833.1; NM_001192904.1.
DR   RefSeq; XP_005224056.1; XM_005223999.3.
DR   AlphaFoldDB; E1BF53; -.
DR   SMR; E1BF53; -.
DR   STRING; 9913.ENSBTAP00000031052; -.
DR   PaxDb; 9913-ENSBTAP00000031052; -.
DR   Ensembl; ENSBTAT00000031089.5; ENSBTAP00000031052.4; ENSBTAG00000014488.6.
DR   GeneID; 537324; -.
DR   KEGG; bta:537324; -.
DR   CTD; 1005; -.
DR   VEuPathDB; HostDB:ENSBTAG00000014488; -.
DR   VGNC; VGNC:27106; CDH7.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000157031; -.
DR   HOGENOM; CLU_005284_3_1_1; -.
DR   InParanoid; E1BF53; -.
DR   OMA; YETMVCE; -.
DR   OrthoDB; 3667774at2759; -.
DR   TreeFam; TF329887; -.
DR   Reactome; R-BTA-418990; Adherens junctions interactions.
DR   Proteomes; UP000009136; Chromosome 24.
DR   Bgee; ENSBTAG00000014488; Expressed in semen and 34 other cell types or tissues.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
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:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; 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   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:SF91; CADHERIN-7; 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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..785
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003143907"
FT   TRANSMEM        599..628
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          73..153
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          154..262
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          263..377
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          378..482
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          482..599
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
SQ   SEQUENCE   785 AA;  87020 MW;  3EF40EB8C30334F7 CRC64;
     MKLGKVEFCH FLQLISLFLC FSGMSQAELS RSGSKPYFQS GRSRTKRSWV WNQFFVLEEY
     MGSDPLYVGK LHSDVDKGDG SIKYILSGEG ASSIFIIDEN TGDIHATKRL DREEQAYYTL
     RAQALDRLTN KPVEPESEFV IKIQDINDNE PKFLDGPYTA GVPEMSPVGT SVVQVTATDA
     DDPTYGNSAR VVYSILQGQP YFSVEPKTGV IKTALPNMDR EAKDQYLLVI QAKDMVGQNG
     GLSGTTSVTV TLTDVNDNPP RFPRRSYQYN VPESLPVASV VARIKAADAD IGANAEMDYK
     IVDGDGLGIF KIAVDKDTQE GIITIQKDLD FEAKTSYTLR IEAANRDADP RFLSLGPFSD
     TTTVKIIVED VDEPPVFSAP LYPMEVSEAT QVGNIIGTVA AHDPDSSNSP VRYSIDRNTD
     LERYFNIDAN SGVITTAKSL DRETNAVHNI TVLAMESQNP SQVGRGYVAI TILDINDNAP
     EFAMDYETTV CENAQPGQVI QKVSAVDKDE PANGHQFYFS LTTDATNNHN FSLKDNKDNT
     ASILTRRNGF RRQEQSVYYL PIFIVDSGSP SLSSTNTLTI RVCDCDADGV AQTCNAEAYV
     LPAGLSTGAL IAILACVLTL LVLILLIVTM RRRKKEPLIF DEERDIRENI VRYDDEGGGE
     EDTEAFDMAA LRNLNVMRDT KTRRDVTPEI QFLSRPTFKS IPDNVIFREF IWERLKEADV
     DPCAPPYDSL QTYAFEGNGS VAESLSSLDS ISSNSDQNYD YLSDWGPRFK RLADMYGNGQ
     ESLYS
//
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