ID A0A2K5NWD8_CERAT Unreviewed; 962 AA.
AC A0A2K5NWD8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Protocadherin gamma subfamily A, 4 {ECO:0000313|Ensembl:ENSCATP00000041737.1};
GN Name=PCDHGA4 {ECO:0000313|Ensembl:ENSCATP00000041737.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000041737.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000041737.1}
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; A0A2K5NWD8; -.
DR Ensembl; ENSCATT00000066166.1; ENSCATP00000041737.1; ENSCATG00000043500.1.
DR GeneTree; ENSGT00940000163745; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000043500; Expressed in cerebellum and 12 other cell types or tissues.
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:SF94; PROTOCADHERIN GAMMA-A4; 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:UP000233060};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 720..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..164
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 165..273
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 274..378
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 379..483
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 484..598
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 610..713
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 104179 MW; 75645355F9C014B3 CRC64;
MHFTLDPEYP GAPQASTEGK PKHRRLRGGV VMAAPPASPD RTRLLQICLL LGVLGEIRAE
QIRYSVFEEQ EEGSVVGNIA KDLGLAPREL VERGVRIVSR GRTQLFALNP RSGSLVTAGR
IDREELCDRS PNCVTILEIL LEDTVKILRV EVEIIDVNDN PPSFGTEQRE IKVAENENPG
TRFPLPEAFD PDVGVNCLQG YQLNSNGYFS LDVQSGADGI KYPELVLERA LDREEEAVHH
LVLTAFDGGD PVRSGTARIL IILVDTNDNA PLFTQPKYHV SVREHVPVGT RLLTVKATDP
DEGANGDVTY SFRKVRDKIS QLFQLNSLSG DITILGDLDY EDSGFYDIDV EAHDGPGLRA
RSKVLVTVLD ENDNAPEVTV TSLTSSVQET SSPGTVIALF NVHDSDSGGN GLVTCSIPDN
LPFILEKTYE NYYRLLTHRT LDREEVSEYN ITVTATDQGI PPLSTETHIS LQVMDINDNP
PTFPHASYSA YIPENNPRGA SILSMTAQDA DSGDNALITY SLAEDTFQDA PLSSYVSINS
NTGILYALRS FDYEQLRDLQ LLVTASDSGD PPLSSNVSVS LFVLDQNDNV PEILYPTFPT
DGSTGVELAP RSADSGYLVT KVVAVDRDSG QNAWLSYRLL KASEPGLFAV GLHTGEVRTA
RALLDRDALK QSLVVVVQDH GQPPLSATVT LTVAVANSIP DVLADLGSLK PSADPDDSGL
TLYLVVAVAA VSCVFLAFVM VLLALKLRRW HKSRLLHGEG SRLAGVPASH FVGVDGVRAF
LQTYSHEVSL TADSRKSHLI FPQPNYADTL ISQESCEKSE PLLITQDLLE TKGDLNLQQA
PPNTDWRFSQ AQRPGTSGSQ NGDDTGTWPN NQFDTEMLQA MILASASEAA DGSSTLGGGA
GTMGLSARYG PQFTLQHVPD YRQNVYIPGS NATLTNAAGK RDGKAAAGGN GNKKKSGKKE
KK
//
