MFSD8_MOUSE
ID MFSD8_MOUSE Reviewed; 519 AA.
AC Q8BH31; Q91VS1; Q9CZ06;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Major facilitator superfamily domain-containing protein 8;
GN Name=Mfsd8;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Testis;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-519.
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).
CC -!- FUNCTION: May be a carrier that transport small solutes by using
CC chemiosmotic ion gradients. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Sorting to lysosomes involves
CC tyrosine- and/or dileucine-based motifs. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AK013144; BAB28676.1; -; mRNA.
DR EMBL; AK032080; BAC27687.1; -; mRNA.
DR EMBL; AK077957; BAC37083.1; -; mRNA.
DR EMBL; BC010483; AAH10483.1; -; mRNA.
DR EMBL; BC113183; AAI13184.1; -; mRNA.
DR EMBL; BC113790; AAI13791.1; -; mRNA.
DR CCDS; CCDS17329.1; -.
DR RefSeq; NP_082416.2; NM_028140.4.
DR AlphaFoldDB; Q8BH31; -.
DR SMR; Q8BH31; -.
DR STRING; 10090.ENSMUSP00000026859; -.
DR GlyGen; Q8BH31; 2 sites.
DR iPTMnet; Q8BH31; -.
DR PhosphoSitePlus; Q8BH31; -.
DR EPD; Q8BH31; -.
DR MaxQB; Q8BH31; -.
DR PaxDb; Q8BH31; -.
DR PRIDE; Q8BH31; -.
DR ProteomicsDB; 292315; -.
DR Antibodypedia; 45354; 67 antibodies from 21 providers.
DR DNASU; 72175; -.
DR Ensembl; ENSMUST00000026859; ENSMUSP00000026859; ENSMUSG00000025759.
DR GeneID; 72175; -.
DR KEGG; mmu:72175; -.
DR UCSC; uc008pbp.1; mouse.
DR CTD; 256471; -.
DR MGI; MGI:1919425; Mfsd8.
DR VEuPathDB; HostDB:ENSMUSG00000025759; -.
DR eggNOG; KOG2325; Eukaryota.
DR GeneTree; ENSGT00530000063854; -.
DR HOGENOM; CLU_027024_2_0_1; -.
DR InParanoid; Q8BH31; -.
DR OMA; AWSNDEA; -.
DR OrthoDB; 685352at2759; -.
DR PhylomeDB; Q8BH31; -.
DR TreeFam; TF316590; -.
DR BioGRID-ORCS; 72175; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Mfsd8; mouse.
DR PRO; PR:Q8BH31; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BH31; protein.
DR Bgee; ENSMUSG00000025759; Expressed in white adipose tissue and 63 other tissues.
DR ExpressionAtlas; Q8BH31; baseline and differential.
DR Genevisible; Q8BH31; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0097352; P:autophagosome maturation; IMP:MGI.
DR GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR GO; GO:0048666; P:neuron development; IMP:MGI.
DR GO; GO:0010506; P:regulation of autophagy; IMP:MGI.
DR GO; GO:1905165; P:regulation of lysosomal protein catabolic process; IMP:MGI.
DR GO; GO:0038202; P:TORC1 signaling; IMP: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 2: Evidence at transcript level;
KW Glycoprotein; Lysosome; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..519
FT /note="Major facilitator superfamily domain-containing
FT protein 8"
FT /id="PRO_0000311233"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..75
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..416
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 440..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..483
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..519
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 13..14
FT /note="Dileucine internalization motif"
FT /evidence="ECO:0000250"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 25
FT /note="S -> G (in Ref. 2; AAH10483)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="S -> F (in Ref. 1; BAB28676)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="S -> N (in Ref. 1; BAB28676)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="V -> G (in Ref. 1; BAB28676)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="A -> T (in Ref. 1; BAB28676)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="L -> F (in Ref. 2; AAH10483)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="S -> P (in Ref. 2; AAH10483)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 57569 MW; 552FF574371BE4FE CRC64;
MANLGSEAER EPLLGPGSPG SREWSEIETQ EHYKSRWKSV RILYLTMFLS SVGFSIVIMS
IWPYLQKIDQ TADASFLGWV IASYSLGQMV ASPLFGLWSN YRPRKEPLIV SISISVAANC
LYAYVHVPAA HNKYYMLIAR GLVGFGAGNV AVVRSYIAGA TSLQERTNAM ANTSTCQALG
FILGPVFQTC FALIGEKGVT WDIIKLQVNM YTAPVLLAAF LGILNIILIL FILREHRVDD
LGRQCKSVNF QEENTDEPQI PEGSIDQVAV VATNIVFFVV LFIFAVYETI LTPLTLDMYA
WTQEQAVLYD GILLVAFGVE AVLVFMGVKL LSKKIGERAI LLGGFVVVWV GFFILLPWGN
QFPKIQWEDL HNSSTPNTTF GEIIIGLWNS SREDHSEQPT GCPIEQTWCL YTPVIHLAQF
LTAAVLIGTG YPACSVMSYT LYSKVLGPKP QGIYMGWLTT SGSAARILGP VFISHVYTYL
GPRWAFSLVC GIVVLTILLI GAVYKRLVAF SVRYMRIQE
