ID A0A3B4GKU1_9CICH Unreviewed; 451 AA.
AC A0A3B4GKU1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Platelet glycoprotein 4 {ECO:0000256|ARBA:ARBA00020772};
DE AltName: Full=Glycoprotein IIIb {ECO:0000256|ARBA:ARBA00032780};
DE AltName: Full=PAS IV {ECO:0000256|ARBA:ARBA00031821};
DE AltName: Full=PAS-4 {ECO:0000256|ARBA:ARBA00032188};
DE AltName: Full=Platelet glycoprotein IV {ECO:0000256|ARBA:ARBA00029966};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000023667.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000023667.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000256|ARBA:ARBA00000626};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33656;
CC Evidence={ECO:0000256|ARBA:ARBA00000626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)-
CC octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245;
CC Evidence={ECO:0000256|ARBA:ARBA00000542};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45265;
CC Evidence={ECO:0000256|ARBA:ARBA00000542};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoate(out) = butanoate(in); Xref=Rhea:RHEA:45248,
CC ChEBI:CHEBI:17968; Evidence={ECO:0000256|ARBA:ARBA00001892};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45249;
CC Evidence={ECO:0000256|ARBA:ARBA00001892};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC ChEBI:CHEBI:7896; Evidence={ECO:0000256|ARBA:ARBA00000934};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45257;
CC Evidence={ECO:0000256|ARBA:ARBA00000934};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tetracosanoate(out) = tetracosanoate(in);
CC Xref=Rhea:RHEA:45260, ChEBI:CHEBI:31014;
CC Evidence={ECO:0000256|ARBA:ARBA00023949};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45261;
CC Evidence={ECO:0000256|ARBA:ARBA00023949};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tetradecanoate(out) = tetradecanoate(in);
CC Xref=Rhea:RHEA:45252, ChEBI:CHEBI:30807;
CC Evidence={ECO:0000256|ARBA:ARBA00000996};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45253;
CC Evidence={ECO:0000256|ARBA:ARBA00000996};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004221}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004236}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. Membrane raft
CC {ECO:0000256|ARBA:ARBA00004285}.
CC -!- SIMILARITY: Belongs to the CD36 family.
CC {ECO:0000256|ARBA:ARBA00010532}.
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DR AlphaFoldDB; A0A3B4GKU1; -.
DR Ensembl; ENSPNYT00000024250.1; ENSPNYP00000023667.1; ENSPNYG00000017687.1.
DR GeneTree; ENSGT00940000153372; -.
DR Proteomes; UP000261460; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR InterPro; IPR005428; CD36/SCARB1/SNMP1.
DR InterPro; IPR002159; CD36_fam.
DR PANTHER; PTHR11923:SF12; PLATELET GLYCOPROTEIN 4; 1.
DR PANTHER; PTHR11923; SCAVENGER RECEPTOR CLASS B TYPE-1 SR-B1; 1.
DR Pfam; PF01130; CD36; 1.
DR PRINTS; PR01610; CD36ANTIGEN.
DR PRINTS; PR01609; CD36FAMILY.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605428-52};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 9..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 423..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DISULFID 233..301
FT /evidence="ECO:0000256|PIRSR:PIRSR605428-52"
FT DISULFID 262..323
FT /evidence="ECO:0000256|PIRSR:PIRSR605428-52"
FT DISULFID 303..312
FT /evidence="ECO:0000256|PIRSR:PIRSR605428-52"
SQ SEQUENCE 451 AA; 50261 MW; FE921A8EA75CB619 CRC64;
MGCFSIKCGL LAGSVFGAVI AILGGILIPV GDMIIERTVK KEAVIEPGTT AYDNWAASEI
AIYRQFWFFD VKNPQQVVQE GAFPEVQEKG PYTYKTRYLP KANVTFNPNN TASFVLPLGA
IFEPSMSVGP EEDTVTSLNL AVAGAYSLLP PASHILLDMV INSTNSSLFQ HRTVKELLWG
YYDPILKDTI GLFSPYNGTT DGPYNVFTGK DDISKVSVID RWRGETFWND TYCDMINGTD
GSSFAPFVDK DVPLYFFSSD ICRSVSASYE ATMNLKGIEV YRYSLLPSTL ASPVDNPDNK
CFCRNYETTK NCTLAGALDM SSCSDGRPIF ISLPHFLQGS EYLRQVVLGL HPDEEHHKTF
LDVEPITGFT LNFAKRIQVN MMYGPLLNQE KMTWTATLDD KTADMFKREL LSRIDMLEIV
QQVLLIAGVI IFCVCLIAFF CVRRKSKANL G
//
