RSCA1_MOUSE
ID RSCA1_MOUSE Reviewed; 582 AA.
AC Q9ER99; B1AUM1; B2RWX9; Q78HA0; Q9CVU8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Regulatory solute carrier protein family 1 member 1;
DE AltName: Full=Regulatory subunit of SGLT1;
DE AltName: Full=Transporter regulator RS1;
DE Short=mRS1;
GN Name=Rsc1a1;
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 [GENOMIC DNA].
RA Baumgarten K., Gorboulev V., Koepsell H.;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 358-582.
RC STRAIN=C57BL/6J; TISSUE=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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15601832; DOI=10.1128/mcb.25.1.78-87.2005;
RA Osswald C., Baumgarten K., Stuempel F., Gorboulev V., Akimjanova M.,
RA Knobeloch K.-P., Horak I., Kluge R., Joost H.G., Koepsell H.;
RT "Mice without the regulator gene Rsc1A1 exhibit increased Na+-D-glucose
RT cotransport in small intestine and develop obesity.";
RL Mol. Cell. Biol. 25:78-87(2005).
RN [7]
RP INTERACTION WITH YRDC.
RX PubMed=16024787; DOI=10.1128/mcb.25.15.6496-6508.2005;
RA Jiang W., Prokopenko O., Wong L., Inouye M., Mirochnitchenko O.;
RT "IRIP, a new ischemia/reperfusion-inducible protein that participates in
RT the regulation of transporter activity.";
RL Mol. Cell. Biol. 25:6496-6508(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Testis;
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: Mediates transcriptional and post-transcriptional regulation
CC of SLC5A1. Inhibits a dynamin and PKC-dependent exocytotic pathway of
CC SLC5A1. Also involved in transcriptional regulation of SLC22A2.
CC Exhibits glucose-dependent, short-term inhibition of SLC5A1 and SLC22A2
CC by inhibiting the release of vesicles from the trans-Golgi network (By
CC similarity). Regulates the expression of SLC5A1 in a tissue-specific
CC manner and is specifically involved in its regulation in the small
CC intestine. {ECO:0000250, ECO:0000269|PubMed:15601832}.
CC -!- SUBUNIT: Interacts with YRDC. {ECO:0000269|PubMed:16024787}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15601832}.
CC Nucleus {ECO:0000269|PubMed:15601832}. Golgi apparatus, trans-Golgi
CC network {ECO:0000250}. Note=Localizes at the inner side of the plasma
CC membrane.
CC -!- TISSUE SPECIFICITY: Expressed in epithelial and subepithelial cells of
CC small intestine. {ECO:0000269|PubMed:15601832}.
CC -!- DISRUPTION PHENOTYPE: Mice show a specific phenotype: first, a post-
CC transcriptional up-regulation of SLC5A1 in the small intestine, with an
CC increased d-glucose absorption rate and capacity; second, an increased
CC food intake that results in a visceral type of obesity.
CC {ECO:0000269|PubMed:15601832}.
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DR EMBL; Y11917; CAA72676.2; -; Genomic_DNA.
DR EMBL; AL671733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466615; EDL13393.1; -; Genomic_DNA.
DR EMBL; BC031491; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC150752; AAI50753.1; -; mRNA.
DR EMBL; AK006435; BAB24588.1; -; mRNA.
DR CCDS; CCDS18879.1; -.
DR RefSeq; NP_076033.4; NM_023544.5.
DR AlphaFoldDB; Q9ER99; -.
DR SMR; Q9ER99; -.
DR BioGRID; 213804; 1.
DR STRING; 10090.ENSMUSP00000101408; -.
DR PhosphoSitePlus; Q9ER99; -.
DR PaxDb; Q9ER99; -.
DR PRIDE; Q9ER99; -.
DR ProteomicsDB; 260738; -.
DR DNASU; 69994; -.
DR Ensembl; ENSMUST00000105782; ENSMUSP00000101408; ENSMUSG00000040715.
DR Ensembl; ENSMUST00000177592; ENSMUSP00000136018; ENSMUSG00000078515.
DR GeneID; 69994; -.
DR KEGG; mmu:69994; -.
DR UCSC; uc012dod.1; mouse.
DR CTD; 6248; -.
DR MGI; MGI:3526447; Rsc1a1.
DR VEuPathDB; HostDB:ENSMUSG00000040715; -.
DR VEuPathDB; HostDB:ENSMUSG00000078515; -.
DR eggNOG; ENOG502RYJA; Eukaryota.
DR GeneTree; ENSGT00390000005744; -.
DR HOGENOM; CLU_032729_0_0_1; -.
DR InParanoid; Q9ER99; -.
DR OMA; ERWTQSE; -.
DR OrthoDB; 817208at2759; -.
DR PhylomeDB; Q9ER99; -.
DR TreeFam; TF335675; -.
DR Reactome; R-MMU-549127; Organic cation transport.
DR Reactome; R-MMU-8981373; Intestinal hexose absorption.
DR BioGRID-ORCS; 69994; 0 hits in 39 CRISPR screens.
DR PRO; PR:Q9ER99; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9ER99; protein.
DR Bgee; ENSMUSG00000040715; Expressed in ectoplacental cone and 52 other tissues.
DR ExpressionAtlas; Q9ER99; baseline and differential.
DR Genevisible; Q9ER99; MM.
DR GO; GO:0005903; C:brush border; IDA:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019871; F:sodium channel inhibitor activity; ISO:MGI.
DR GO; GO:0050892; P:intestinal absorption; IMP:MGI.
DR GO; GO:0045920; P:negative regulation of exocytosis; IEA:InterPro.
DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; ISO:MGI.
DR GO; GO:0042997; P:negative regulation of Golgi to plasma membrane protein transport; ISO:MGI.
DR GO; GO:0032243; P:negative regulation of nucleoside transport; IMP:ARUK-UCL.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0051051; P:negative regulation of transport; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR039222; RSC1A1.
DR InterPro; IPR015940; UBA.
DR PANTHER; PTHR15397; PTHR15397; 1.
DR SMART; SM00165; UBA; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Golgi apparatus; Membrane; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..582
FT /note="Regulatory solute carrier protein family 1 member 1"
FT /id="PRO_0000324151"
FT DOMAIN 536..576
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 135
FT /note="R -> H (in Ref. 4; AAI50753)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="A -> V (in Ref. 4; AAI50753)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="C -> G (in Ref. 4; AAI50753)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="A -> T (in Ref. 4; AAI50753)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="G -> S (in Ref. 4; AAI50753)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="S -> P (in Ref. 4; AAI50753)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="D -> G (in Ref. 4; AAI50753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 582 AA; 61251 MW; F51458B600B9E82E CRC64;
MSSLPTSDGF DHPAPSGQSP EVGSPTSLAR SVSASVCAIK PGDPNSIESL AMEATKASAE
FQTNSKKTDP PPLQVLPDLA SSAEQSLAMP FHKSSKEAVV AGNLEKSVEK GTQGLRVYLH
TRQDASLTLT TTGMREPQIF AEEKSWHPEN QTPSPVNGLQ QHRETGSVQR EAGQQSVPQD
QGCLCDAEDL ELHEEVVSLE ALRKGELQRH AHLPSAEKGL PASGLCSCPC SEALMEVDTA
EQSLVAMCSS TGRQDAVIKS PSVAHLASDN PTMEVETLQS NPSCEPVEHS ILTRELQLPE
DNVDMSTMDN KDDNSSSLLS GHGQPSVESA EEFCSSVTVA LKELHELLVI SCKPASEESP
EHVTCQSEIG AESQPSVSDL SGRRVQSVHL TPSDQYSQGS CHQATSESGK TEIVGTAPCA
AVEDEASTSF EGLGDGLSPD REDVRRSTES ARKSCSVAIT SAKLSEQLPC TSGVEIAPEL
AASEGAHSQP SEHVHNPGPD RPETSSVCPG AGLPRSGLDQ PPTQSLSTPS VLPPFIFPAA
DVDRILGAGF TLQEALGALH RVGGNADLAL LVLLAKNIVV PT
