S45A1_MOUSE
ID S45A1_MOUSE Reviewed; 751 AA.
AC Q8BIV7; Q3TZ98;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Proton-associated sugar transporter A {ECO:0000305};
DE Short=PAST-A;
DE AltName: Full=Deleted in neuroblastoma 5 protein homolog;
DE Short=DNb-5 homolog;
DE AltName: Full=Solute carrier family 45 member 1;
GN Name=Slc45a1 {ECO:0000312|MGI:MGI:2653235}; Synonyms=Dnb5;
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=Cerebellum, and Inner ear;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-500, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Proton-associated glucose transporter in the brain.
CC {ECO:0000250|UniProtKB:Q8K4S3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-galactose(in) + H(+)(in) = D-galactose(out) + H(+)(out);
CC Xref=Rhea:RHEA:29019, ChEBI:CHEBI:4139, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000250|UniProtKB:Q8K4S3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) + H(+)(out) = D-glucose(in) + H(+)(in);
CC Xref=Rhea:RHEA:69556, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000250|UniProtKB:Q8K4S3};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8K4S3}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glycoside-pentoside-hexuronide (GPH) cation
CC symporter transporter (TC 2.A.2) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK082651; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK082651; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK158002; BAE34311.1; -; mRNA.
DR CCDS; CCDS18973.1; -.
DR RefSeq; NP_776135.2; NM_173774.3.
DR AlphaFoldDB; Q8BIV7; -.
DR STRING; 10090.ENSMUSP00000036774; -.
DR iPTMnet; Q8BIV7; -.
DR PhosphoSitePlus; Q8BIV7; -.
DR SwissPalm; Q8BIV7; -.
DR PaxDb; Q8BIV7; -.
DR PRIDE; Q8BIV7; -.
DR ProteomicsDB; 260905; -.
DR Antibodypedia; 57179; 10 antibodies from 4 providers.
DR DNASU; 242773; -.
DR Ensembl; ENSMUST00000037827; ENSMUSP00000036774; ENSMUSG00000039838.
DR GeneID; 242773; -.
DR KEGG; mmu:242773; -.
DR UCSC; uc008vxt.1; mouse.
DR CTD; 50651; -.
DR MGI; MGI:2653235; Slc45a1.
DR VEuPathDB; HostDB:ENSMUSG00000039838; -.
DR eggNOG; KOG0637; Eukaryota.
DR GeneTree; ENSGT00950000182914; -.
DR HOGENOM; CLU_015081_1_0_1; -.
DR InParanoid; Q8BIV7; -.
DR OMA; GIHWDRT; -.
DR OrthoDB; 1230185at2759; -.
DR PhylomeDB; Q8BIV7; -.
DR TreeFam; TF325412; -.
DR BioGRID-ORCS; 242773; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q8BIV7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BIV7; protein.
DR Bgee; ENSMUSG00000039838; Expressed in primary visual cortex and 57 other tissues.
DR ExpressionAtlas; Q8BIV7; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015517; F:galactose:proton symporter activity; ISS:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005356; F:glucose:proton symporter activity; IMP:UniProtKB.
DR GO; GO:0008506; F:sucrose:proton symporter activity; IBA:GO_Central.
DR GO; GO:0015757; P:galactose transmembrane transport; ISS:UniProtKB.
DR GO; GO:1904659; P:glucose transmembrane transport; IMP:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Membrane; Phosphoprotein; Reference proteome; Sugar transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..751
FT /note="Proton-associated sugar transporter A"
FT /id="PRO_0000122515"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 630..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 500
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 287
FT /note="S -> R (in Ref. 1; BAE34311)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="S -> L (in Ref. 1; BAE34311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 751 AA; 81474 MW; 129F390E154F6BBD CRC64;
MIPPASSTPP GEAVIPSVAP QDFWRSPISS YSGSVTGHIS HRANNFKRHP KRRKYIRPSP
PPPPNTPCPI ELVDFGDLHP QRSFWELLFN GCILFGIEFS YAMETAYVTP VLLQMGLPDQ
LYSLVWFISP ILGFLLQPLL GAWSDRCTSR FGRRRPFILV LAIGALLGLS LLLNGRDIGM
ALADTATNHK WGILLTVCGV VLMDFSADSA DNPSHAYMMD VCGPVDQDRG LNIHALMAGL
GGGFGYVVGG IHWDKTSFGR ALGGQLRVIY VFTAITLSVT TVLTLISIPE RPLRPLGEKR
TAMKSPSLPL PPSPPVLLEE GAGDALPSTT ATSLYASFSS PISPPSPLTP KYGSFISRDS
SLTGINEFAS SFGTSNIDSV LIDCFTAGHD NYLALPSSVP RQAISVSFPR APDGFYCQER
GLERREGPLT LGSDGDVLRV GSLDTSKPRA SGILKRPQTL ALPDVAGGNG PETSRRRNVT
FSQQVANILL NGVKYESELT GSSEQSEQPL SLRHLCSTIY NMPKALRNLC VNHFLGWLSF
EGMLLFYTDF MGEVVFQGDP KAPHTSEAYQ KYNSGVTMGC WGMCIYAFSA AFYSAILEKL
EECLSVRTLY FIAYLAFGLG TGLATLSRNL YVVLSLCTTY GILFSTLCTL PYSLLCDYYQ
SKKFAGSSAD GTRRGMGVDI SLLSCQYFLA QILVSLVLGP LTSAVGSANG VMYFSSLVSF
LGCLYSSLCV TYEIPSVDAA DEERQPLLLN V
