ID A0A2K6BF41_MACNE Unreviewed; 932 AA.
AC A0A2K6BF41;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Protocadherin gamma subfamily A, 4 {ECO:0000313|Ensembl:ENSMNEP00000010002.1};
GN Name=PCDHGA4 {ECO:0000313|Ensembl:ENSMNEP00000010002.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000010002.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000010002.1}
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; A0A2K6BF41; -.
DR Ensembl; ENSMNET00000034179.1; ENSMNEP00000010002.1; ENSMNEG00000029363.1.
DR GeneTree; ENSGT00940000163745; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000029363; 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:SF56; PROTOCADHERIN GAMMA-A7; 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:UP000233120};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..932
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014427038"
FT TRANSMEM 689..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..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 348..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; 101518 MW; D3D847713BD542AC CRC64;
MAAQPRGGDY RGFLLLSILL GTLWEAWAGR ILYSVSEETD KGSFVGDIAK DLGLEPQELA
ERGVRIVSRG RTQLFALNPR SGSLVTAGRI DREEICAQSA RCLVNFNILM EDKMNLYPID
VEIIDINDNV PRFLTEEINV KIMENTAPGV RFPLSEAGDP DVGTNSLHSY QLSPNRHFSL
AVQSGNDGTK YPELVLERVL DREEERVHHL VLTASDGGDP PRSSTARIQV TVVDVNDHAP
VFFLPQYQVT VPENVPVGTK LLTVHAIDLD EGVNGEVTYS FRKITPKLLQ MFHLNSLTGE
LSTLEGLDYE ETGFYEMEVQ AQDVPGSLTK AKVLITVLDV NDNAPEVIMT SLSSSIPEDT
PLGTVIALFY LQDRDSGKNG EVTCTIPENL PFKLEKSIDN YYRLVTTKNL DRETLSLYNI
TLKATDGGIP PLSRETHISM QVADTNDNPP TFPHSSYSVY IPENNPRGAS IFLVTAQDHD
SEENAQVTYS LAEDTIQGRP VSSYVSINSD TGVLYALQSF DYEQLRELQL TVTARDSGDP
PLSSNMSLSL FVLDQNDNPP EILYPALPTD GSTGLELAPR SAEPGYLVTK VVAVDKDSGQ
NAWLSYLLLK ASETGLFTVG LHTGEVRTAR ALLDRDALKQ SLLVAVQDHG QPPLSATVTL
TVAVADSIPE VLADLGSLEP SNGPYNSDLM LYLVVAVAAV SCIFLAFVLV LLALRLQRWL
KSGRLQASES GLASVPTSHY VGMDGVRAFL QTYSHEVSLT SDSRKSHLIF PQPNYADTLI
SQESCEKNDS LLTSVDFHEC KDKVPTIQQA PPNTDWRFSQ AQRPGTSGSQ NGDDTGTWPN
NQFDTEMLQA MILASASEAA DGSSTLGGGA GTMGLSARYG PQFTLQHVPD YRQNVYIPGS
NATLTNAAGK RDGKAPAGGN GNKKKSGKKE KK
//
