ID   MFS2B_XENTR             Reviewed;         511 AA.
AC   A4IH46;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Sphingosine-1-phosphate transporter MFSD2B {ECO:0000305};
DE   AltName: Full=Major facilitator superfamily domain-containing protein 2B {ECO:0000305};
GN   Name=mfsd2b {ECO:0000250|UniProtKB:A6NFX1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lipid transporter that specifically mediates export of
CC       sphingosine-1-phosphate in red blood cells and platelets. Sphingosine-
CC       1-phosphate is a signaling sphingolipid and its export from red blood
CC       cells into in the plasma is required for red blood cell morphology.
CC       Sphingosine-1-phosphate export from platelets is required for platelet
CC       aggregation and thrombus formation. In addition to export, also able to
CC       mediate S1P import. {ECO:0000250|UniProtKB:Q3T9M1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sphing-4-enine 1-phosphate(in) = sphing-4-enine 1-
CC         phosphate(out); Xref=Rhea:RHEA:38667, ChEBI:CHEBI:60119;
CC         Evidence={ECO:0000250|UniProtKB:Q3T9M1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sphinganine 1-phosphate(in) = sphinganine 1-phosphate(out);
CC         Xref=Rhea:RHEA:38671, ChEBI:CHEBI:57939;
CC         Evidence={ECO:0000250|UniProtKB:Q3T9M1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=sphinga-4E,14Z-dienine-1-phosphate(in) = sphinga-4E,14Z-
CC         dienine-1-phosphate(out); Xref=Rhea:RHEA:70207, ChEBI:CHEBI:149632;
CC         Evidence={ECO:0000250|UniProtKB:Q3T9M1};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q3T9M1};
CC       Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the cell
CC       membrane and intracellular membranes. {ECO:0000250|UniProtKB:Q3T9M1}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC135369; AAI35370.1; -; mRNA.
DR   RefSeq; NP_001096238.1; NM_001102768.1.
DR   AlphaFoldDB; A4IH46; -.
DR   SMR; A4IH46; -.
DR   STRING; 8364.ENSXETP00000055220; -.
DR   PaxDb; A4IH46; -.
DR   DNASU; 100124793; -.
DR   GeneID; 100124793; -.
DR   KEGG; xtr:100124793; -.
DR   CTD; 388931; -.
DR   Xenbase; XB-GENE-6044470; mfsd2b.
DR   eggNOG; KOG4830; Eukaryota.
DR   HOGENOM; CLU_027408_6_1_1; -.
DR   InParanoid; A4IH46; -.
DR   OMA; LPMAEWF; -.
DR   OrthoDB; 827101at2759; -.
DR   PhylomeDB; A4IH46; -.
DR   TreeFam; TF331194; -.
DR   Proteomes; UP000008143; Chromosome 5.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000018209; Expressed in skeletal muscle tissue and 6 other tissues.
DR   ExpressionAtlas; A4IH46; baseline.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0046624; F:sphingolipid transporter activity; ISS:UniProtKB.
DR   GO; GO:0015293; F:symporter activity; IEA:InterPro.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:InterPro.
DR   GO; GO:0006869; P:lipid transport; ISS:UniProtKB.
DR   GO; GO:0071702; P:organic substance transport; IBA:GO_Central.
DR   GO; GO:1901731; P:positive regulation of platelet aggregation; ISS:UniProtKB.
DR   GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; ISS:UniProtKB.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR039672; MFS_2.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR11328; PTHR11328; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Lipid transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..511
FT                   /note="Sphingosine-1-phosphate transporter MFSD2B"
FT                   /id="PRO_0000341262"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        462..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   511 AA;  56318 MW;  7B68528780D01B5B CRC64;
     MAETSRELPL STLTASTRRA LRIRARQARE AKLSVLSKVC YAIGGAPNQV SGSASAFFLQ
     IYLLDVALIS PYQASLVLSL GKTWGGITDP IVGYCISKSK WTRIGRLMPW MLGCTPFLVV
     SYFLLWFVPT FETGRVLWYL AFFSCFQALS TAYHVPYTTL TMFLSTDQME RDSATAYRMT
     VEVLGTLIGA AVQGQIVASA HTGSHCNVTN MTGNLTADFL YEPTEYITSA RQVYMIAAGI
     IGCLYLLCIS VLFLGVKERD DPYALVAGKV IPFFKGFRET MQFGPYLNLI SSFLLISAAV
     QIQQSNFVLF CTHAADLQDH FQNLVLTILI AAVLSIPFWQ WFLQKFGKKM AAFGISLMIP
     FSIMLVTISS LVVAYVVAVA SGLSIAASLL LPWSMLPDVV DNFRLTNPQG KGLEAIFYSS
     FVFFTKLSAG IALGISTLSL QFADYNTSLC KQSYSVVLTL KLLIGAAPAL MIIIGLTILA
     FYPITEDTRK ETELALDVIR MRTRRSTLIV I