ID A0A2K5JK15_COLAP Unreviewed; 890 AA.
AC A0A2K5JK15;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Cadherin-2 {ECO:0000256|ARBA:ARBA00021703};
DE AltName: Full=Neural cadherin {ECO:0000256|ARBA:ARBA00031121};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000029166.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000029166.1}
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 junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004135}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU003318}. Cell surface
CC {ECO:0000256|ARBA:ARBA00004241}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A2K5JK15; -.
DR STRING; 336983.ENSCANP00000029166; -.
DR Ensembl; ENSCANT00000052295.1; ENSCANP00000029166.1; ENSCANG00000037720.1.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; 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:SF79; CADHERIN-2; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 5.
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:UP000233080};
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 708..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..251
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 252..366
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 367..481
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 482..589
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 588..694
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 847..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 890 AA; 98229 MW; 3999469EA9F82EE2 CRC64;
MCRIASVEAS GEIALCKTGF PEDVYSAVLS KDVHEGQPLL NVKFSNCNGK RKVQYESSEP
ADFKVDEDGM VYAVRSFPLS SEHAKFLIYA QDKETQEKWQ VAVKLSLKPT LTEDSVKEPP
EVEEIVFPRQ FSKHSGHLQR QKRDWVIPPI NLPENSRGPF PQELVRIRSD RDKNLSLRYS
VTGPGADQPP TGIFIINPIS GQLSVTKPLD REQIARFHLR AHAVDINGNQ VENPIDIVIN
VIDMNDNRPE FLHQVWNGTV PEGSKPGTYV MTVTAIDADD PNALNGMLRY RILSQAPSTP
SPNMFTINNE TGDIITVAAG LDREKVQQYT LIIQATDMEG NPTYGLSNTA TAIITVTDVN
DNPPEFTAMT FYGEVPENRV DVIVANLTVT DKDQPHTPAW NAVYRISGGD PTGRFAIQTD
PNSNDGLVTV VKPIDFETNR MFVLTVAAEN QVPLAKGIQH PPQSTATVSV TVIDVNENPY
FAPNPKIIRQ EEGLHAGTML TTFTAQDPDR YMQQNIRYTK LSDPANWLKI DPVNGQITTI
AVLDRESPNV KNNIYNATFL ASDNGIPPMS GTGTLQIYLL DINDNAPQVL PQEAETCETP
DPNSINITAL DYDIDPNAGP FAFDLPLSPV TIKRNWTITR LNGDFAQLNL KIKFLEAGIY
EVPIIITDSG NPPKSNISIL RVKVCQCDSN GDCTDVDRIV GAGLGTGAII AILLCIIILL
ILVLMFVVWM KRRDKERQAK QLLIDPEDDV RDNILKYDEE GGGEEDQDYD LSQLQQPDTV
EPDAIKPVGI RRMDERPIHA EPQYPVRSAA PHPGDIGDFI NEGLKAADND PTAPPYDSLL
VFDYEGSGST AGSLSSLNSS SSGGEQDYDY LNDWGPRFKK LADMYGGGDD
//
