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Database: UniProt
Entry: A0A2K5JK17_COLAP
LinkDB: A0A2K5JK17_COLAP
Original site: A0A2K5JK17_COLAP 
ID   A0A2K5JK17_COLAP        Unreviewed;       872 AA.
AC   A0A2K5JK17;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
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:ENSCANP00000029184.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000029184.1}
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; A0A2K5JK17; -.
DR   Ensembl; ENSCANT00000052315.1; ENSCANP00000029184.1; 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        690..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          126..233
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          234..348
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          349..463
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          464..571
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          570..676
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          829..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        830..849
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   872 AA;  96370 MW;  9CE60E380B101337 CRC64;
     KAGAPEDPVS RKYEKKGKAL EEGMKFSNCN GKRKVQYESS EPADFKVDED GMVYAVRSFP
     LSSEHAKFLI YAQDKETQEK WQVAVKLSLK PTLTEDSVKE PPEVEEIVFP RQFSKHSGHL
     QRQKRDWVIP PINLPENSRG PFPQELVRIR SDRDKNLSLR YSVTGPGADQ PPTGIFIINP
     ISGQLSVTKP LDREQIARFH LRAHAVDING NQVENPIDIV INVIDMNDNR PEFLHQVWNG
     TVPEGSKPGT YVMTVTAIDA DDPNALNGML RYRILSQAPS TPSPNMFTIN NETGDIITVA
     AGLDREKVQQ YTLIIQATDM EGNPTYGLSN TATAIITVTD VNDNPPEFTA MTFYGEVPEN
     RVDVIVANLT VTDKDQPHTP AWNAVYRISG GDPTGRFAIQ TDPNSNDGLV TVVKPIDFET
     NRMFVLTVAA ENQVPLAKGI QHPPQSTATV SVTVIDVNEN PYFAPNPKII RQEEGLHAGT
     MLTTFTAQDP DRYMQQNIRY TKLSDPANWL KIDPVNGQIT TIAVLDRESP NVKNNIYNAT
     FLASDNGIPP MSGTGTLQIY LLDINDNAPQ VLPQEAETCE TPDPNSINIT ALDYDIDPNA
     GPFAFDLPLS PVTIKRNWTI TRLNGDFAQL NLKIKFLEAG IYEVPIIITD SGNPPKSNIS
     ILRVKVCQCD SNGDCTDVDR IVGAGLGTGA IIAILLCIII LLILVLMFVV WMKRRDKERQ
     AKQLLIDPED DVRDNILKYD EEGGGEEDQD YDLSQLQQPD TVEPDAIKPV GIRRMDERPI
     HAEPQYPVRS AAPHPGDIGD FINEGLKAAD NDPTAPPYDS LLVFDYEGSG STAGSLSSLN
     SSSSGGEQDY DYLNDWGPRF KKLADMYGGG DD
//
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