MFS10_MOUSE
ID MFS10_MOUSE Reviewed; 456 AA.
AC Q9D2V8; Q3U800; Q3UN73; Q9D1A7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Major facilitator superfamily domain-containing protein 10;
DE AltName: Full=Tetracycline transporter-like protein;
GN Name=Mfsd10; Synonyms=Tetran;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:BAB31378.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB31378.1}, and
RC NOD {ECO:0000312|EMBL:BAC40724.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:BAE31219.1},
RC Cerebellum {ECO:0000312|EMBL:BAE25874.1},
RC Embryo {ECO:0000312|EMBL:BAB22982.1}, Kidney {ECO:0000312|EMBL:BAB31378.1},
RC and Thymus {ECO:0000312|EMBL:BAC40724.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2] {ECO:0000312|EMBL:AAH23012.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3 {ECO:0000312|EMBL:AAH23012.1}, and
RC ICR {ECO:0000312|EMBL:AAH64775.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH23012.1}, and
RC Trophoblast stem cell {ECO:0000312|EMBL:AAH64775.1};
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=31142202; DOI=10.1080/19491034.2019.1618175;
RA Cheng L.C., Baboo S., Lindsay C., Brusman L., Martinez-Bartolome S.,
RA Tapia O., Zhang X., Yates J.R. III, Gerace L.;
RT "Identification of new transmembrane proteins concentrated at the nuclear
RT envelope using organellar proteomics of mesenchymal cells.";
RL Nucleus 10:126-143(2019).
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 (By similarity). {ECO:0000250|UniProtKB:Q14728}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:31142202}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB22982.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK003763; BAB22982.1; ALT_INIT; mRNA.
DR EMBL; AK018736; BAB31378.1; -; mRNA.
DR EMBL; AK089055; BAC40724.1; -; mRNA.
DR EMBL; AK144407; BAE25874.1; -; mRNA.
DR EMBL; AK152438; BAE31219.1; -; mRNA.
DR EMBL; BC023012; AAH23012.1; -; mRNA.
DR EMBL; BC064775; AAH64775.1; -; mRNA.
DR CCDS; CCDS19217.1; -.
DR RefSeq; NP_080936.1; NM_026660.2.
DR RefSeq; XP_006504140.1; XM_006504077.3.
DR RefSeq; XP_006504141.1; XM_006504078.3.
DR RefSeq; XP_011239069.1; XM_011240767.2.
DR RefSeq; XP_011239070.1; XM_011240768.2.
DR RefSeq; XP_017176573.1; XM_017321084.1.
DR AlphaFoldDB; Q9D2V8; -.
DR SMR; Q9D2V8; -.
DR BioGRID; 212789; 3.
DR STRING; 10090.ENSMUSP00000001109; -.
DR TCDB; 2.A.1.2.73; the major facilitator superfamily (mfs).
DR GlyGen; Q9D2V8; 1 site.
DR PhosphoSitePlus; Q9D2V8; -.
DR SwissPalm; Q9D2V8; -.
DR EPD; Q9D2V8; -.
DR MaxQB; Q9D2V8; -.
DR PaxDb; Q9D2V8; -.
DR PRIDE; Q9D2V8; -.
DR ProteomicsDB; 295600; -.
DR Antibodypedia; 8956; 80 antibodies from 21 providers.
DR DNASU; 68294; -.
DR Ensembl; ENSMUST00000001109; ENSMUSP00000001109; ENSMUSG00000001082.
DR Ensembl; ENSMUST00000114329; ENSMUSP00000109968; ENSMUSG00000001082.
DR Ensembl; ENSMUST00000114331; ENSMUSP00000109970; ENSMUSG00000001082.
DR GeneID; 68294; -.
DR KEGG; mmu:68294; -.
DR UCSC; uc008xct.1; mouse.
DR CTD; 10227; -.
DR MGI; MGI:1915544; Mfsd10.
DR VEuPathDB; HostDB:ENSMUSG00000001082; -.
DR eggNOG; KOG2615; Eukaryota.
DR GeneTree; ENSGT00940000164295; -.
DR InParanoid; Q9D2V8; -.
DR OMA; ACFSVAF; -.
DR OrthoDB; 787769at2759; -.
DR PhylomeDB; Q9D2V8; -.
DR TreeFam; TF314512; -.
DR BioGRID-ORCS; 68294; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Mfsd10; mouse.
DR PRO; PR:Q9D2V8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D2V8; protein.
DR Bgee; ENSMUSG00000001082; Expressed in yolk sac and 223 other tissues.
DR ExpressionAtlas; Q9D2V8; baseline and differential.
DR Genevisible; Q9D2V8; MM.
DR GO; GO:0031526; C:brush border membrane; IDA:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043252; P:sodium-independent organic anion transport; ISO:MGI.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Glycoprotein; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..456
FT /note="Major facilitator superfamily domain-containing
FT protein 10"
FT /id="PRO_0000324659"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 177
FT /note="G -> R (in Ref. 1; BAB22982)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="V -> M (in Ref. 1; BAE31219)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="M -> L (in Ref. 1; BAE31219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 49369 MW; 242AD79516B266F6 CRC64;
MGWAGDAGCT PRPPIRPRPA SERRVIIVLF LGLLLDLLAF TLLLPLLPGL LERHGREQDP
LYGSWQRGVD WFASAIGMPA EKRYNSVLFG GLIGSAFSLL QFFSAPLTGA ASDYLGRRPV
MMLSLTGLAI SYAVWATSRS FKAFLASRVI GGISKGNVNL STAIVADLGS PPTRSQGMAV
IGVAFSLAFT LGPMLGAFLS VEMVPWISLL FAISDMLFIF CFLPETLPQE KRASSVTLGF
HTAAHLLSPL ALLRFAAVTH SQDPPAEHRL RNLRRLGLVY FLYLFLFSGL EYTLSFLAHQ
RFQFSSLQQG KMFFFIGLTM ATIQGTYARR ISPGKEAAAV TRAMLLLVPA FLLIGWAHSL
PTLGLGLMLY SFAAAVVVPG LSTMVSSYGS PGQKGTIMGI LRSLGALGRA LGPVVAASVY
WLTGAQVCFT VCSALFLLPF LLLWKLKHPA ETSKEE
