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Database: UniProt
Entry: A0A3B4U998_SERDU
LinkDB: A0A3B4U998_SERDU
Original site: A0A3B4U998_SERDU 
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
//
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