MFSD3_MOUSE
ID MFSD3_MOUSE Reviewed; 412 AA.
AC Q5U419; Q8VED1; Q9D7F8;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Major facilitator superfamily domain-containing protein 3;
GN Name=Mfsd3;
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=Tongue;
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].
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Colon, and Mammary tumor;
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 TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=27981419; DOI=10.1007/s12031-016-0867-8;
RA Perland E., Hellsten S.V., Lekholm E., Eriksson M.M., Arapi V.,
RA Fredriksson R.;
RT "The Novel Membrane-Bound Proteins MFSD1 and MFSD3 are Putative SLC
RT Transporters Affected by Altered Nutrient Intake.";
RL J. Mol. Neurosci. 61:199-214(2017).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In brain, expressed in the cortex, striatum,
CC hippocampus, hypothalamus, thalamus and cerebellum (at protein level)
CC (PubMed:27981419). Widely expressed with highest levels in kidney and
CC liver (PubMed:27981419). {ECO:0000269|PubMed:27981419}.
CC -!- INDUCTION: After 24 hours of starvation, up-regulated in the brainstem
CC and cerebellum and down-regulated in the hypothalamus
CC (PubMed:27981419). Following 8 weeks of high-fat diet, down-regulated
CC in the brainstem (PubMed:27981419). {ECO:0000269|PubMed:27981419}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AK009269; BAB26184.1; -; mRNA.
DR EMBL; AK089539; BAC40919.1; -; mRNA.
DR EMBL; BC019171; AAH19171.1; -; mRNA.
DR EMBL; BC085305; AAH85305.1; -; mRNA.
DR CCDS; CCDS27587.1; -.
DR RefSeq; NP_081398.2; NM_027122.3.
DR AlphaFoldDB; Q5U419; -.
DR SMR; Q5U419; -.
DR STRING; 10090.ENSMUSP00000019224; -.
DR PhosphoSitePlus; Q5U419; -.
DR MaxQB; Q5U419; -.
DR PaxDb; Q5U419; -.
DR PRIDE; Q5U419; -.
DR ProteomicsDB; 293465; -.
DR DNASU; 69572; -.
DR GeneID; 69572; -.
DR KEGG; mmu:69572; -.
DR UCSC; uc007wlt.1; mouse.
DR CTD; 113655; -.
DR MGI; MGI:1916822; Mfsd3.
DR eggNOG; KOG3574; Eukaryota.
DR InParanoid; Q5U419; -.
DR OrthoDB; 716614at2759; -.
DR PhylomeDB; Q5U419; -.
DR TreeFam; TF330933; -.
DR BioGRID-ORCS; 69572; 2 hits in 75 CRISPR screens.
DR PRO; PR:Q5U419; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q5U419; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015295; F:solute:proton symporter activity; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR004752; AmpG_permease/AT-1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR12778; PTHR12778; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..412
FT /note="Major facilitator superfamily domain-containing
FT protein 3"
FT /id="PRO_0000273393"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 189
FT /note="R -> K (in Ref. 1; BAB26184)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="E -> K (in Ref. 1; BAB26184)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="G -> A (in Ref. 1; BAB26184)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="L -> W (in Ref. 1; BAB26184)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="A -> V (in Ref. 1; BAB26184)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="L -> I (in Ref. 1; BAB26184)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="L -> P (in Ref. 1; BAB26184/BAC40919 and 2;
FT AAH19171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 43165 MW; 5BC7A67452921693 CRC64;
MHGKLLPLAG LYLVQGLPYG LQSSLLPILL RARGLSLTRV GLTKGLYAPW LLKLAWAPLV
DRRGTPRVWL TLSTLSLGLV CGLLAVLPPP QAGQTGLPTT VMGLLLLLNL GAAVQDVALD
TLAVQLLEPK ELGPGNTVQV VAYKLGSALA GGGLLVLFPT LSWPLLFLLL AATYWLAAAL
AWAAPALGRL PWPQASEHTP HSSYLLQDLL AVPGTLWTAG FVLTYKLGEQ GAGSLFPLLL
LDHGASASDL GLWSGLGAVT CSIAGSSLGG ALLARHWQPL KLLKTVLQLR LGSLACQTAL
LFHLNSPGAS VDPGTVMRGA VLLSLCLQQF FGGVVTTATF TVMMHCSQLA PRALQATHYS
FLATLELLGK LLLGTLAGVL ADSLGPHLCF AVFLVLSALP VLDLRLAPSN LT
