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Database: UniProt
Entry: A0A2R9BJP3_PANPA
LinkDB: A0A2R9BJP3_PANPA
Original site: A0A2R9BJP3_PANPA 
ID   A0A2R9BJP3_PANPA        Unreviewed;       530 AA.
AC   A0A2R9BJP3;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=MFSD2 lysolipid transporter A, lysophospholipid {ECO:0000313|Ensembl:ENSPPAP00000029904.1};
GN   Name=MFSD2A {ECO:0000313|Ensembl:ENSPPAP00000029904.1};
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000029904.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000029904.1, ECO:0000313|Proteomes:UP000240080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
RN   [2] {ECO:0000313|Ensembl:ENSPPAP00000029904.1}
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   EMBL; AJFE02051330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003815463.1; XM_003815415.2.
DR   AlphaFoldDB; A0A2R9BJP3; -.
DR   STRING; 9597.ENSPPAP00000029904; -.
DR   Ensembl; ENSPPAT00000052758.1; ENSPPAP00000029904.1; ENSPPAG00000037970.1.
DR   GeneID; 100967551; -.
DR   KEGG; pps:100967551; -.
DR   CTD; 84879; -.
DR   GeneTree; ENSGT00390000005318; -.
DR   OMA; VPYVAMP; -.
DR   OrthoDB; 6761at2759; -.
DR   Proteomes; UP000240080; Chromosome 1.
DR   Bgee; ENSPPAG00000037970; Expressed in liver and 5 other cell types or tissues.
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   CDD; cd17451; MFS_NLS1_MFSD2A; 1.
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:UP000240080};
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        47..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        241..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        293..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        331..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        358..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        382..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        426..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        468..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   530 AA;  58549 MW;  3B6A152EE9F1A3B9 CRC64;
     MAKGEGAESG SAAGLLPTSI LQSTERPAQV KKEPKKKKQQ LSVCNKLCYA LGGAPYQVTG
     CALGFFLQIY LLDVAQVGPF SASIILFVGR AWDAITDPLV GLCISKSPWT CLGRLMPWII
     FSTPLAVIAY FLIWFVPDFP HGQTYWYLLF YCLFETMVTC FHVPYSALTM FISTEQTERD
     SATAYRMTVE VLGTVLGTAI QGQIVGQADT PCFQDLNSST VASQSANHTH GTTSHRETQK
     AYLLAAGVIV CIYIICAVIL ILGVREQREP YEAQQAEPIA YFRGLRLVMS HGPYIKLITG
     FLFTSLAFML VEGNFVLFCT YTLGFRNEFQ NLLLAIMLSA TLTIPIWQWF LTRFGKKTAV
     YVGISSAVPF LILVALMESN LIITYAVAVA AGISVAAAFL LPWSMLPDVI DDFHLKQPHF
     HGTEPIFFSF YVFFTKFASG VSLGISTLSL DFAGYQTRGC SQPEPVKFTL NMLVTMAPIV
     LILLGLLLFK MYPIDEERRR QNKKALQALR DEASSSGCSE TDSTELASIL
//
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