ID A0A1S3F8X0_DIPOR Unreviewed; 529 AA.
AC A0A1S3F8X0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Sodium-dependent lysophosphatidylcholine symporter 1 isoform X1 {ECO:0000313|RefSeq:XP_012872292.1};
GN Name=Mfsd2a {ECO:0000313|RefSeq:XP_012872292.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012872292.1};
RN [1] {ECO:0000313|RefSeq:XP_012872292.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012872292.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_012872292.1; XM_013016838.1.
DR AlphaFoldDB; A0A1S3F8X0; -.
DR STRING; 10020.ENSDORP00000012075; -.
DR GeneID; 105986088; -.
DR KEGG; dord:105986088; -.
DR CTD; 84879; -.
DR InParanoid; A0A1S3F8X0; -.
DR OMA; VPYVAMP; -.
DR OrthoDB; 6761at2759; -.
DR Proteomes; UP000081671; 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:0140348; F:lysophosphatidylcholine flippase activity; IEA:Ensembl.
DR GO; GO:0051978; F:lysophospholipid:sodium symporter activity; IEA:Ensembl.
DR GO; GO:1901480; F:oleate transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0008643; P:carbohydrate transport; IEA:InterPro.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0050890; P:cognition; IEA:Ensembl.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; IEA:Ensembl.
DR GO; GO:0140329; P:lysophospholipid translocation; IEA:Ensembl.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; IEA:Ensembl.
DR GO; GO:0061744; P:motor behavior; IEA:Ensembl.
DR GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; IEA:Ensembl.
DR GO; GO:0008594; P:photoreceptor cell morphogenesis; IEA:Ensembl.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IEA:Ensembl.
DR GO; GO:0050773; P:regulation of dendrite development; IEA:Ensembl.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0150011; P:regulation of neuron projection arborization; IEA:Ensembl.
DR GO; GO:0150172; P:regulation of phosphatidylcholine metabolic process; IEA:Ensembl.
DR GO; GO:0150175; P:regulation of phosphatidylethanolamine metabolic process; IEA:Ensembl.
DR GO; GO:0150178; P:regulation of phosphatidylserine metabolic process; IEA:Ensembl.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IEA:Ensembl.
DR GO; GO:0003406; P:retinal pigment epithelium development; IEA:Ensembl.
DR GO; GO:0045056; P:transcytosis; IEA:Ensembl.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IEA:Ensembl.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000081671};
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 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 467..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 529 AA; 58227 MW; 44146502576EDCB8 CRC64;
MAKGEGAESS SAAGLLPTGI LQPGERPAQV KKEPKKKQQL SICNKLCYAV GGAPYQVTGC
ALGFFLQIYL LDVALVTPFS ASIILFVGRA WDAVTDPLVG FCISKSPWTQ LGRLMPWIIF
STPLAVIAYF LIWFVPDFSQ GQTLWYLIFY CLFETLVTCF HVPYSALTMF ISTEQSERDS
ATAYRMTVEV LGTVLGTAIQ GQIVGQANAP CLHYPNESSL APESANRTHS TTSLKQTQNA
YLLAAGVIAS IYVICAIILT LGVREQREPY EAQKTEQISF VRGLRLVMSH GPYVKLIAGF
LFTSLAFMLV EGNFALFCTY TLGFPNEFQN LLLAIMLSAT FTIPIWQWFL TRFGKKTAVY
VGISSAVPFL ILVALMESNL FVTYVVAIAA GVSVAAAFLL PWSMLPDVVD DFHLKHPNCH
DSEPIFFSFY VFFTKFASGV SLGISTLSLD FAGYKPRGCS QPSLVKFTLK MLVTMAPIIF
ILLGLFLFKL YPINEEKRRQ NKKALQALQD EASSSACSDS DSTELASIL
//
