ID A0A2K6TU78_SAIBB Unreviewed; 897 AA.
AC A0A2K6TU78;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Cadherin-4 {ECO:0000256|ARBA:ARBA00041040};
GN Name=CDH4 {ECO:0000313|Ensembl:ENSSBOP00000023217.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000023217.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000023217.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6TU78; -.
DR Ensembl; ENSSBOT00000040072.1; ENSSBOP00000023217.1; ENSSBOG00000028115.1.
DR GeneTree; ENSGT00940000158073; -.
DR Proteomes; UP000233220; 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; 3.
DR Gene3D; 2.60.40.60; Cadherins; 6.
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; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR000233; Cadherin_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF81; CADHERIN-4; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR01820; DESMOCOLLIN.
DR SMART; SM00112; CA; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; Cadherin-like; 6.
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 Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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:UP000233220};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 703..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 151..258
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 259..373
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 374..488
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 489..596
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 595..703
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 108..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 98568 MW; B5869000EC6FD854 CRC64;
AHNEDLTTRE TCKAGFSEDD YTALISQNIL EGEKLLQVKF SSCLETKGTQ YETNSVDFKV
GADGTVFATR ELQVPSEQVA FTVTAWDSQT AERWDAVVRL LVAQTSSSHS GHKAQKGKKT
VALDPSPPPK DTLLPWPQHQ NSNGLRRRKR DWVIPPINVP ENSRGPFPQQ LVRIRSDKDN
DIPIRYSITG VGADQPPMEV FSIDSMSGRM YVTRPMDREE HASYHLRAHA VDMNGNKVEN
PIDLYIYVID MNDNRPEFIN QVYNGSVDEG SKPGTYVMTV TANDADDSTT ANGMVRYRIL
TQTPQSPSQN MFTINSETGD IVTVAAGLDR EKVQQYTVIV QATDMEGNLN YGLSNTATAI
ITVTDVNDNP PEFTTSTFAG EVPENRVETV VANLTVMDRD QPHSPNWNAV YRIISGDPSG
HFSVRTDPVT NEGMVTVVKA VDYELNRAFM LTVMVSNQAP LASGIQMSFQ STAGVTISVM
DINEAPYFPS NHKLIRLEEG VPPGTVLTTF SAVDPDRFMQ QAVRYSKLSD PANWLQVNTT
NGQITTAAVL DRESLYTKNN VYEATFLAAD NGIPPASGTG TLQIYLIDIN DNAPELLPKE
AQICEKPNLN AINITAADAD VDPNIGPYVF ELPFVPAAVR KNWTITRLNG DYAQLSLRIL
YLEAGMYDVP IIVTDSGNPP LSNMSIIKVK VCPCDDNGDC TTIGAVAAAG LGTGAIVAIL
ICILILLTMV LLFVVWMKRR EKERHTKQLL IDPEDDVRDN ILKYDEEGGG EEDQDYDLSQ
LQQPEAMGHV PSKAPGVRRV DERPVGAEPQ YPVRPMVPHP GDIGEFINEG LRAADNDPTA
PPYDSLLVFD YEGSGSTAGS VSSLNSSSSG DQDYDYLNDW GPRFKKLADM YGGGEED
//
