MFS10_HUMAN
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 03-AUG-2022, entry version 153.
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
RC Colon {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 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).
CC -!- FUNCTION: Confers cellular resistance to apoptosis induced by the non-
CC steroidal anti-inflammatory drugs indomethacin and diclofenac. May act
CC as an efflux pump. {ECO:0000269|PubMed:17362938}.
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}.
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; 32.
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; Q14728; -.
DR PeptideAtlas; Q14728; -.
DR PRIDE; Q14728; -.
DR ProteomicsDB; 60148; -.
DR Antibodypedia; 8956; 80 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 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; ACFSVAF; -.
DR OrthoDB; 787769at2759; -.
DR PhylomeDB; Q14728; -.
DR TreeFam; TF314512; -.
DR PathwayCommons; Q14728; -.
DR SignaLink; Q14728; -.
DR BioGRID-ORCS; 10227; 15 hits in 1076 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 185 other tissues.
DR ExpressionAtlas; Q14728; baseline and differential.
DR Genevisible; Q14728; HS.
DR GO; GO:0031526; C:brush border membrane; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of 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; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Membrane; Nucleus; Reference proteome;
KW 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
