ID A0A2K5HP38_COLAP Unreviewed; 944 AA.
AC A0A2K5HP38;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Cadherin domain-containing protein {ECO:0000259|PROSITE:PS50268};
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:ENSCANP00000006114.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000006114.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May be
CC involved in the establishment and maintenance of specific neuronal
CC connections in the brain. {ECO:0000256|ARBA:ARBA00003436}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A2K5HP38; -.
DR Ensembl; ENSCANT00000023083.1; ENSCANP00000006114.1; ENSCANG00000019834.1.
DR Proteomes; UP000233080; 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 GO; GO:0007399; P:nervous system development; IEA:UniProt.
DR CDD; cd11304; Cadherin_repeat; 6.
DR Gene3D; 2.60.40.60; Cadherins; 6.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR032455; Cadherin_C.
DR InterPro; IPR031904; Cadherin_CBD.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF312; PROTOCADHERIN GAMMA-C5; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF16492; Cadherin_C_2; 1.
DR Pfam; PF15974; Cadherin_tail; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..944
FT /note="Cadherin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014454687"
FT TRANSMEM 690..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..133
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 134..242
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 243..350
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 359..454
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 455..564
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 579..677
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 721..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 102019 MW; 2114A13E42E2C7B5 CRC64;
MGHKTPPQLA GKWQVLCMLS LCCWGWVSGQ LRYSVVEESE PGTLVGNVAQ DLGLKMTDLL
SRRLQLGSEE NGRYFSLSLM SGALAVNQKI DRESLCGAST SCLLPVQVVT EHPLELIRVE
VEILDLNDNS PSFATHEREM RISESAAPGA RFPLDSAQDP DVGTNTVSFY TLSPNSHFSL
NVKTLKDGKP FPELVLEQQL DREAQTRHQL VLTAVDGGTP ARSGTTLISV IVLDINDNAP
TFQSSVLRVG IPENAPIGTL LLRLNATDPD EGTNGQLDYS FGDHTSEAVR NLFGLDPSSG
AIHVLGPIDF EESSFYEIHA RARDQGQPAM EGHCVIQVDV GDVNDNAPEV LLASLANPVL
ESTPVGTVVG LFNVRDRDSG RNGEVSLGIS PDLPFQIKPS ENHYSLLTSQ PLDREATSHY
TIELLASDAG SPPLHKHLTI RLNISDVNDN APHFNQQLYT AYILENRPPG SLLCTVAASD
PDTGDNARLT YSIVGNQIQG APASSFVYVN PEDGRVFAQR TFDYELLQML QIVVGVRDSG
SPPLHANTSL HVFVLDENDN APAVLHPRPG WEHSAPQRLP RSAPPGSLVT KVTAVDADAG
HNAWLSYSLL PQSTAPGLFL VSTHTGEVRT ARALLEDDSD TQQVVVLVRD NGDPSLSSTA
TVLLVLEDED PEEMPKSSDF LKHPPERSEL TLYLIVALAT VSLLSLVTFT FLSAKCLQGN
ADRDGGGAQC CRRPDSPSRD FYKQSSPNLQ VSSDGTLKYM EVTLRPTDSQ SHCYRTCFSP
ASDGSDFTFL RPLSVQQPTA LALEPDAIRS RSNTLRERSQ QAPPNTDWRF SQAQRPGTSG
SQNGDDTGTW PNNQFDTEML QAMILASASE AADGSSTLGG GAGTMGLSAR YGPQFTLQHV
PDYRQNVYIP GSNATLTNAA GKRDGKTPAG GNGNKKKSGK KEKK
//
