ID A0A2K6TGY8_SAIBB Unreviewed; 932 AA.
AC A0A2K6TGY8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Protocadherin gamma subfamily C, 5 {ECO:0000313|Ensembl:ENSSBOP00000018923.1};
GN Name=PCDHGC5 {ECO:0000313|Ensembl:ENSSBOP00000018923.1};
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:ENSSBOP00000018923.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000018923.1}
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; A0A2K6TGY8; -.
DR Ensembl; ENSSBOT00000035740.1; ENSSBOP00000018923.1; ENSSBOG00000026061.1.
DR GeneTree; ENSGT00940000162232; -.
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 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:SF72; PROTOCADHERIN GAMMA-A8; 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; 2.
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:UP000233220};
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..932
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014465361"
FT TRANSMEM 689..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..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..347
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 356..452
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 453..562
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 579..682
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 804..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 101862 MW; 78087978B4A104F7 CRC64;
MATSRNRPRR GELILLCALL GTLWEVGRGQ IRYSVPEETD KGSFVGNISK DLRLEPRELA
KHGVRIVSRG RTQLFALNPR SGSLVTSGRI DREELCAQSP RCLININILV EDKGKLFGIE
VEIIDINDNN PKFQVEDLEV KINEIAVPGT RYPLPEAVDP DVGVNSLQSY QLSPNHHFSL
DVQTGDDGAI NPELVLERTL DREEEAAHHL VLTASDGGEP RRSSTVRIHM TVLDTNDNAP
VFAQPIYRVK VLENVPPGTR LLTVTASDPD EGTNGKVAYK FRKINEKQSL LFQLNENTGE
ISIAKSLDYE ECSFYEMEIQ AEDVGALLGR TKLLISVEDV NDNRPEVIIT SLFSPVLENS
LPGTVVAFLS VHDRDSGKNG HIVCYTRDNL PFKLEKSIDN YYRLVTWKYL DRENVSIYNI
TVMASDLGTP PLSTETHITL HVADINDNPP TFPHASYSAY ILENNLRGAS IFSLTAHDPD
SQENAQVTYS VMENTLQGAP LSSYISINSD TGVLYALQSF DYEQIRDLQL LVTASDSGDP
PLSSNVSLSL FVLDQNDNTP EILYPALPTD DSTGVELAPR SAEPGYLVTK VVAVDRDSGQ
NAWLSYRLLK ASEPGLFTVG LHTGEVRTAR ALLDRDALKQ SLVVAVQDHG QPPLSATVTL
TVAVADSIPE VLAELGNLKP SVDPDDSGLT LYLVVAVAAV SCVFLAFVVV LLGLRLRRWH
KSRLLQDSGG RLAGVPASHL VGVEEVQAFL QTYSHEVSLT TDSRKSHLIF PQPNYADTLI
SQESCEKNDS LLTSIDFHEC KNEADHGQQA PPNTDWRFSQ AQRPGTSGSQ NGDDTGTWPN
NQFDTEMLQA MILASASEAA DGSSTLGGGA GTMGLSARYG PQFTLQHVPD YRQNVYIPGS
NATLTNAAGK RDGKAPAGGN GNKKKSGKKE KK
//
