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-JUN-2016, entry version 92. DE RecName: Full=Proton-associated sugar transporter A; 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; Synonyms=Dnb5; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RP BY 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 RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Mediates glucose uptake along the pH gradient. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glycoside-pentoside-hexuronide (GPH) CC cation symporter transporter (TC 2.A.2) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AK082651; Type=Frameshift; Positions=217; 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 UniGene; Mm.29280; -. DR ProteinModelPortal; Q8BIV7; -. DR STRING; 10090.ENSMUSP00000036774; -. DR iPTMnet; Q8BIV7; -. DR PhosphoSite; Q8BIV7; -. DR MaxQB; Q8BIV7; -. DR PaxDb; Q8BIV7; -. DR PRIDE; Q8BIV7; -. 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 eggNOG; KOG0637; Eukaryota. DR eggNOG; ENOG410Y28T; LUCA. DR GeneTree; ENSGT00390000018882; -. DR HOGENOM; HOG000231090; -. DR HOVERGEN; HBG053518; -. DR InParanoid; Q8BIV7; -. DR KO; K15378; -. DR OMA; PKYGSFI; -. DR OrthoDB; EOG7G4QDJ; -. DR PhylomeDB; Q8BIV7; -. DR TreeFam; TF325412; -. DR PRO; PR:Q8BIV7; -. DR Proteomes; UP000000589; Chromosome 4. DR Bgee; Q8BIV7; -. DR CleanEx; MM_SLC45A1; -. DR ExpressionAtlas; Q8BIV7; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005355; F:glucose transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 2. PE 1: Evidence at protein level; KW Complete proteome; Membrane; Phosphoprotein; Reference proteome; KW Sugar transport; Symport; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 751 Proton-associated sugar transporter A. FT /FTId=PRO_0000122515. FT TRANSMEM 93 113 Helical. {ECO:0000255}. FT TRANSMEM 123 143 Helical. {ECO:0000255}. FT TRANSMEM 155 175 Helical. {ECO:0000255}. FT TRANSMEM 191 211 Helical. {ECO:0000255}. FT TRANSMEM 233 253 Helical. {ECO:0000255}. FT TRANSMEM 268 288 Helical. {ECO:0000255}. FT TRANSMEM 536 556 Helical. {ECO:0000255}. FT TRANSMEM 576 596 Helical. {ECO:0000255}. FT TRANSMEM 606 626 Helical. {ECO:0000255}. FT TRANSMEM 630 650 Helical. {ECO:0000255}. FT TRANSMEM 688 708 Helical. {ECO:0000255}. FT TRANSMEM 710 730 Helical. {ECO:0000255}. FT MOD_RES 500 500 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT CONFLICT 287 287 S -> R (in Ref. 1; BAE34311). FT {ECO:0000305}. FT CONFLICT 433 433 S -> L (in Ref. 1; BAE34311). FT {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 //