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 08-NOV-2023, entry version 131. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000036774; -. DR ProteomicsDB; 260905; -. DR Antibodypedia; 57179; 13 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 AGR; MGI:2653235; -. 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; CDYYQSR; -. DR OrthoDB; 5480802at2759; -. DR PhylomeDB; Q8BIV7; -. DR TreeFam; TF325412; -. DR BioGRID-ORCS; 242773; 0 hits in 76 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: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; MFS general substrate transporter like domains; 2. DR InterPro; IPR011701; MFS. DR InterPro; IPR036259; MFS_trans_sf. DR PANTHER; PTHR19432:SF6; PROTON-ASSOCIATED SUGAR TRANSPORTER A; 1. DR PANTHER; PTHR19432; SUGAR TRANSPORTER; 1. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 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 //