ID H0YSL6_TAEGU Unreviewed; 720 AA.
AC H0YSL6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Major facilitator superfamily domain containing 2A {ECO:0000313|Ensembl:ENSTGUP00000001276.2};
GN Name=MFSD2A {ECO:0000313|Ensembl:ENSTGUP00000001276.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000001276.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000001276.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000001276.2}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; H0YSL6; -.
DR STRING; 59729.ENSTGUP00000001276; -.
DR Ensembl; ENSTGUT00000001288.2; ENSTGUP00000001276.2; ENSTGUG00000001225.2.
DR GeneTree; ENSGT00390000005318; -.
DR HOGENOM; CLU_027408_6_1_1; -.
DR InParanoid; H0YSL6; -.
DR OMA; VPYVAMP; -.
DR TreeFam; TF331194; -.
DR Proteomes; UP000007754; Chromosome 23.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000007754};
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 302..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 486..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 550..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 574..596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 617..640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 660..681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 720 AA; 81619 MW; 743CF0B4BF176AC7 CRC64;
MFSSSMATEE LWPHRGEVRK APGEGPGPKE EEEEKKKKEE EEEEKLEEEE KKKREKEKKE
EEEEEEEKKR EKEEKEEEKE KKEEEKKEEE EEKKKKEEED EEEKKEEEEE KKKKEEEEKL
EEEKKKKREK EKKEEEEEEK EEEKKEKKKK EEENEKEEEE KEEAEAGGGG PVQPSSGRVS
RYKGVRRRLG PFIAHGMAGG GGAERPGAGG LLPPALRQHR RRESRERLSV CSKLCYAVGG
APYQITGCAL GFFLQIYLLD VAQVDAFYAS IILFAGRAWD AITDPMVGFF ISKTSWTRFG
RLMPWIMFST PFAIISYFLI WFVPDISTGQ VMWYLVFYCA FQTLVTCFHV PYSALTMFIS
REQSERDSAT AYRMTVEVLG TVLGTAIQGQ IVGKVDTPCV GSPFFFGLTN SSVAMEELNM
THDPGSLTDT RNAYMIAAGV IGGLYILCAL ILLLGVRERR EASELQSDEP VSFFQGLKLV
MNHGPYIKLI AGFLFTSLAF MLLEGNFALF CTYTLGFRNE FQNILLAIML SATLTIPFWQ
WFLTRFGKKT AVYVGISSAI PFLIAVVVLD SNLFVTYVVA VAAGISVAAA FLLPWSMLPD
VIDDFKLQHP SSHGHEAIFF SFYVFFTKFT AGVSLGISTL SLDFAGYQTR GCSQPGQVNF
TLKMLVSAVP VGLILLSLLL FKLYPIDEEK RSKNKKALQD LREESNSSSE SDNTELASIV
//
