ID A0A3B4U998_SERDU Unreviewed; 519 AA.
AC A0A3B4U998;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Sodium-dependent lysophosphatidylcholine symporter 1-B-like {ECO:0000313|Ensembl:ENSSDUP00000014942.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000014942.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000014942.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-
CC phosphocholine(in) + Na(+)(in) = 1-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycero-3-phosphocholine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:43860, ChEBI:CHEBI:29101, ChEBI:CHEBI:73873;
CC Evidence={ECO:0000256|ARBA:ARBA00036185};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine(in) +
CC Na(+)(in) = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine(out) +
CC Na(+)(out); Xref=Rhea:RHEA:43856, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000256|ARBA:ARBA00035930};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine(in) + Na(+)(in) =
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:43864, ChEBI:CHEBI:29101, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000256|ARBA:ARBA00035893};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine(in) + Na(+)(in) = a 1-
CC acyl-sn-glycero-3-phosphocholine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:44376, ChEBI:CHEBI:29101, ChEBI:CHEBI:58168;
CC Evidence={ECO:0000256|ARBA:ARBA00036686};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine(in) + Na(+)(in) = a
CC 1-acyl-sn-glycero-3-phosphoethanolamine(out) + Na(+)(out);
CC Xref=Rhea:RHEA:43868, ChEBI:CHEBI:29101, ChEBI:CHEBI:64381;
CC Evidence={ECO:0000256|ARBA:ARBA00036741};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
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DR AlphaFoldDB; A0A3B4U998; -.
DR STRING; 41447.ENSSDUP00000014942; -.
DR Ensembl; ENSSDUT00000015226.1; ENSSDUP00000014942.1; ENSSDUG00000010903.1.
DR GeneTree; ENSGT00390000005318; -.
DR OMA; NSVGIYY; -.
DR OrthoDB; 6761at2759; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015293; F:symporter activity; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:InterPro.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR039672; MFS_2.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11328; MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11328:SF29; SODIUM-DEPENDENT LYSOPHOSPHATIDYLCHOLINE SYMPORTER 1; 1.
DR Pfam; PF13347; MFS_2; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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}.
FT TRANSMEM 42..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 519 AA; 57576 MW; 18A386BB2ED1D4FF CRC64;
MARGEGAEQY AASLLSVKPI NTEVKTAKPR EQRNRLSVCS KLCYAIGGAP YQITGSALGF
FLQIYLLDVA QLDPFYASII LFVGRAWDAV TDPTVGFLVS RSRWTRIGRM MPWILSSTPF
AVVTYFLIWY VPPFEQGKVI WYLIFYCLFQ SMQTCFHVPY SALTMFISSD HKERDSATAY
RMMVEVMGTV LGTAIQGQIV GGGSDCSTKP DVSDSRNSLA YNASGVSLEE TKQAYLLASG
VISIIYVLCA GVLFFGVKEQ KESSHKKSVP LTFRQGLWLV VSHTPYVKLV IGFLFTSLAF
MLLEGNFALF ITYALGHRND FQNILLVIML SGSLTIPLWQ WFLTRFGKKT ATYFGISWAI
PFMILIVCIE SNLIMSYLVS VAAGVSVAAA FLLPWSMLPD VVDDFKVKNP DIHGHEALFY
SFYVFFIKFA SGISLGISTL SLKFADYKTG SCSQPEAVSL TLKVLVSPVP VCLIIVGLLI
LRTYPIDEER RHGNQKLLQK ILDSETDSES EASALGSNV
//