ID   MFS10_HUMAN             Reviewed;         455 AA.
AC   Q14728; Q07706;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Major facilitator superfamily domain-containing protein 10;
DE   AltName: Full=Tetracycline transporter-like protein;
GN   Name=MFSD10; Synonyms=TETRAN;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1] {ECO:0000312|EMBL:AAA36729.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Frontal cortex {ECO:0000312|EMBL:AAA36729.1};
RX   PubMed=8353488; DOI=10.1093/hmg/2.6.673;
RA   Duyao M.P., Taylor S.A.M., Buckler A.J., Ambrose C.M., Lin C., Groot N.,
RA   Church D., Barnes G., Wasmuth J.J., Housman D.E., MacDonald M.E.,
RA   Gusella J.F.;
RT   "A gene from chromosome 4p16.3 with similarity to a superfamily of
RT   transporter proteins.";
RL   Hum. Mol. Genet. 2:673-676(1993).
RN   [2] {ECO:0000312|EMBL:AL390065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3] {ECO:0000312|EMBL:EAW82496.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000312|EMBL:AAH01502.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=B-cell {ECO:0000312|EMBL:AAH14979.1}, and Colon
RC   {ECO:0000312|EMBL:AAH01502.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=17362938; DOI=10.1016/j.febslet.2007.03.001;
RA   Mima S., Ushijima H., Hwang H.-J., Tsutsumi S., Makise M., Yamaguchi Y.,
RA   Tsuchiya T., Mizushima H., Mizushima T.;
RT   "Identification of the TPO1 gene in yeast, and its human orthologue TETRAN,
RT   which cause resistance to NSAIDs.";
RL   FEBS Lett. 581:1457-1463(2007).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=18638446; DOI=10.1016/j.bbrc.2008.07.034;
RA   Ushijima H., Hiasa M., Namba T., Hwang H.J., Hoshino T., Mima S.,
RA   Tsuchiya T., Moriyama Y., Mizushima T.;
RT   "Expression and function of TETRAN, a new type of membrane transporter.";
RL   Biochem. Biophys. Res. Commun. 374:325-330(2008).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [8] {ECO:0007744|PDB:6S4M}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-444.
RA   Pascoa T.C., Pike A.C.W., Bushell S.R., Quigley A., Chu A.,
RA   Mukhopadhyay S.M.M., Shrestha L., Venkaya S., Chalk R., Burgess-Brown N.A.,
RA   Edwards A.M., Arrowsmith C.H., Bountra C., Carpenter E.P.;
RT   "Crystal structure of the human organic anion transporter TETRAN
RT   (MFSD10).";
RL   Submitted (JUN-2019) to the PDB data bank.
CC   -!- FUNCTION: Probable organic anion transporter which may serve as a
CC       transporter for some non-steroidal anti-inflammatory drugs (NSAIDs) as
CC       well as other organic anions across the luminal membranes of renal
CC       proximal tubules at the final excretion step into the urine.
CC       {ECO:0000269|PubMed:17362938, ECO:0000269|PubMed:18638446}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=13 uM for fluorescein {ECO:0000269|PubMed:18638446};
CC         Vmax=75 pmol/min/mg enzyme {ECO:0000269|PubMed:18638446};
CC   -!- INTERACTION:
CC       Q14728; P45973: CBX5; NbExp=3; IntAct=EBI-11337904, EBI-78219;
CC       Q14728; Q92876: KLK6; NbExp=3; IntAct=EBI-11337904, EBI-2432309;
CC       Q14728; P16284: PECAM1; NbExp=3; IntAct=EBI-11337904, EBI-716404;
CC       Q14728; P37173: TGFBR2; NbExp=3; IntAct=EBI-11337904, EBI-296151;
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC       {ECO:0000250|UniProtKB:Q9D2V8}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000305|PubMed:18638446}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in luminal membrane of renal tubules (at
CC       protein level) (PubMed:18638446). Detected in all tissues tested with
CC       higher expression in heart, splee, kidney, leukocytes and prostate
CC       (PubMed:18638446). {ECO:0000269|PubMed:18638446}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       {ECO:0000255}.
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DR   EMBL; L11669; AAA36729.1; -; mRNA.
DR   EMBL; AL390065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471131; EAW82496.1; -; Genomic_DNA.
DR   EMBL; BC001502; AAH01502.1; -; mRNA.
DR   EMBL; BC014979; AAH14979.1; -; mRNA.
DR   CCDS; CCDS3365.1; -.
DR   PIR; I54353; I54353.
DR   RefSeq; NP_001111.3; NM_001120.4.
DR   RefSeq; NP_001139541.1; NM_001146069.1.
DR   PDB; 6S4M; X-ray; 2.40 A; A=1-444.
DR   PDBsum; 6S4M; -.
DR   AlphaFoldDB; Q14728; -.
DR   SMR; Q14728; -.
DR   BioGRID; 115521; 36.
DR   IntAct; Q14728; 14.
DR   MINT; Q14728; -.
DR   STRING; 9606.ENSP00000332646; -.
DR   iPTMnet; Q14728; -.
DR   PhosphoSitePlus; Q14728; -.
DR   SwissPalm; Q14728; -.
DR   BioMuta; MFSD10; -.
DR   DMDM; 74735668; -.
DR   EPD; Q14728; -.
DR   jPOST; Q14728; -.
DR   MassIVE; Q14728; -.
DR   MaxQB; Q14728; -.
DR   PaxDb; 9606-ENSP00000332646; -.
DR   PeptideAtlas; Q14728; -.
DR   ProteomicsDB; 60148; -.
DR   Pumba; Q14728; -.
DR   Antibodypedia; 8956; 92 antibodies from 21 providers.
DR   DNASU; 10227; -.
DR   Ensembl; ENST00000329687.8; ENSP00000332646.4; ENSG00000109736.15.
DR   Ensembl; ENST00000355443.9; ENSP00000347619.4; ENSG00000109736.15.
DR   GeneID; 10227; -.
DR   KEGG; hsa:10227; -.
DR   MANE-Select; ENST00000355443.9; ENSP00000347619.4; NM_001146069.2; NP_001139541.1.
DR   UCSC; uc003gfw.4; human.
DR   AGR; HGNC:16894; -.
DR   CTD; 10227; -.
DR   GeneCards; MFSD10; -.
DR   HGNC; HGNC:16894; MFSD10.
DR   HPA; ENSG00000109736; Low tissue specificity.
DR   MIM; 610977; gene.
DR   neXtProt; NX_Q14728; -.
DR   OpenTargets; ENSG00000109736; -.
DR   PharmGKB; PA162395840; -.
DR   VEuPathDB; HostDB:ENSG00000109736; -.
DR   eggNOG; KOG2615; Eukaryota.
DR   GeneTree; ENSGT00940000164295; -.
DR   InParanoid; Q14728; -.
DR   OMA; EWYVNIS; -.
DR   OrthoDB; 1058006at2759; -.
DR   PhylomeDB; Q14728; -.
DR   TreeFam; TF314512; -.
DR   PathwayCommons; Q14728; -.
DR   SignaLink; Q14728; -.
DR   BioGRID-ORCS; 10227; 15 hits in 1154 CRISPR screens.
DR   ChiTaRS; MFSD10; human.
DR   GenomeRNAi; 10227; -.
DR   Pharos; Q14728; Tbio.
DR   PRO; PR:Q14728; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q14728; Protein.
DR   Bgee; ENSG00000109736; Expressed in right uterine tube and 187 other cell types or tissues.
DR   ExpressionAtlas; Q14728; baseline and differential.
DR   GO; GO:0031526; C:brush border membrane; IBA:GO_Central.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:MGI.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005637; C:nuclear inner membrane; ISS:UniProtKB.
DR   GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0008493; F:tetracycline transmembrane transporter activity; TAS:ProtInc.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0043252; P:sodium-independent organic anion transport; IDA:MGI.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR23504; MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 10; 1.
DR   PANTHER; PTHR23504:SF31; MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 10; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   Genevisible; Q14728; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Cell membrane; Membrane; Nucleus;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..455
FT                   /note="Major facilitator superfamily domain-containing
FT                   protein 10"
FT                   /id="PRO_0000324658"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        359..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        26
FT                   /note="T -> I (in Ref. 1; AAA36729)"
FT                   /evidence="ECO:0000305"
FT   HELIX           20..40
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           41..45
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           46..55
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           59..75
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           81..114
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           116..136
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           140..152
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           155..165
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           170..197
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           200..202
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           203..221
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           228..230
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           239..244
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           248..252
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           255..258
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   STRAND          260..262
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           266..301
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           305..325
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           327..329
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           335..355
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           359..385
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           390..392
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           393..422
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           424..434
FT                   /evidence="ECO:0007829|PDB:6S4M"
FT   HELIX           436..442
FT                   /evidence="ECO:0007829|PDB:6S4M"
SQ   SEQUENCE   455 AA;  48339 MW;  A449A8C479EAC889 CRC64;
     MGWGGGGGCT PRPPIHQQPP ERRVVTVVFL GLLLDLLAFT LLLPLLPGLL ESHGRAHDPL
     YGSWQGGVDW FATAIGMPVE KRYNSVLFGG LIGSAFSVLQ FLCAPLTGAT SDCLGRRPVM
     LLCLMGVATS YAVWATSRSF AAFLASRLIG GISKGNVSLS TAIVADLGSP LARSQGMAVI
     GVAFSLGFTL GPMLGASLPL EMAPWFALLF AASDLLFIFC FLPETLPLEK RAPSIALGFR
     DAADLLSPLA LLRFSAVARG QDPPSGDRLS SLRRLGLVYF LYLFLFSGLE YTLSFLTHQR
     FQFSSLQQGK MFFLIGLTMA TIQGAYARRI HPGGEVAAVK RALLLLVPAF LLIGWGRSLP
     VLGLGLLLYS FAAAVVVPCL SSVVAGYGSP GQKGTVMGTL RSLGALARAA GPLVAASVYW
     LAGAQACFTT WSGLFLLPFF LLQKLSYPAQ TLKAE
//