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Database: UniProt
Entry: A0A3Q3BHT7_KRYMA
LinkDB: A0A3Q3BHT7_KRYMA
Original site: A0A3Q3BHT7_KRYMA 
ID   A0A3Q3BHT7_KRYMA        Unreviewed;       487 AA.
AC   A0A3Q3BHT7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Major facilitator superfamily domain containing 2A {ECO:0000313|Ensembl:ENSKMAP00000029395.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000029395.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000029395.1}
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}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000256|ARBA:ARBA00008335}.
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DR   AlphaFoldDB; A0A3Q3BHT7; -.
DR   Ensembl; ENSKMAT00000029761.1; ENSKMAP00000029395.1; ENSKMAG00000021771.1.
DR   GeneTree; ENSGT00390000005318; -.
DR   Proteomes; UP000264800; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        39..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        226..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        281..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        318..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        385..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        428..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          468..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  54414 MW;  2C57653BEFF5BCC2 CRC64;
     MAKGEGAEQY SNASLLNKSD SSDGIKLARK HRLSVWNKIC YAIGGAPYQI TGCALGFFLQ
     LYLLDVAQLD PFYASIILFV GRAWDAVTDP TVGFLVSRSP WTRFGRMLPW IVFSTPLAVL
     SYFLIWYVPP FANGKVFWYI IFYCLFQTLQ TCFHVPYSAL TMFISSDQKE RDSATAYRMT
     VEVLGTVLGT AIQGQIVGMA NAPCLPGPDL KVFFFFFFFA SSQKNAYMIA SGVICLIYIL
     CAVVLFFGVR EQKELSQMRT QPLPFFQGIK LVMGHGPYAK LVMAFLFTSL AFMVGIDLSA
     TIAIPFWQWF LTRFGKKMAV YVGSMSVIPF LILVVCIKSN LYVTYIVSFI AGVGVASAFL
     LPWSMLPDVL DDFKVKNPDS TGHEALFYSF YVFFTKFASG VSLGVSTLSL DFAGYISRGC
     SQPEEVALTL KLLVSAAPVA LIFVGLAILY FYPIDEKRRQ YNHKMLQEMR DSESDSESET
     TDISNVI
//
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