RSCA1_HUMAN
ID RSCA1_HUMAN Reviewed; 617 AA.
AC Q92681; B2RBP5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Regulatory solute carrier protein family 1 member 1;
DE AltName: Full=Transporter regulator RS1;
DE Short=hRS1;
GN Name=RSC1A1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8836035; DOI=10.1089/dna.1996.15.769;
RA Lambotte S., Veyhl M., Koehler M., Morrison-Shetlar A.I., Kinne R.K.H.,
RA Schmid M., Koepsell H.;
RT "The human gene of a protein that modifies Na(+)-D-glucose co-transport.";
RL DNA Cell Biol. 15:769-777(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-62.
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=14724758; DOI=10.1007/s00232-003-0626-y;
RA Veyhl M., Wagner C.A., Gorboulev V., Schmitt B.M., Lang F., Koepsell H.;
RT "Downregulation of the Na(+)- D-glucose cotransporter SGLT1 by protein RS1
RT (RSC1A1) is dependent on dynamin and protein kinase C.";
RL J. Membr. Biol. 196:71-81(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=16788147; DOI=10.1152/ajprenal.00067.2006;
RA Kroiss M., Leyerer M., Gorboulev V., Kuehlkamp T., Kipp H., Koepsell H.;
RT "Transporter regulator RS1 (RSC1A1) coats the trans-Golgi network and
RT migrates into the nucleus.";
RL Am. J. Physiol. 291:F1201-F1212(2006).
RN [7]
RP FUNCTION.
RX PubMed=16788146; DOI=10.1152/ajprenal.00068.2006;
RA Veyhl M., Keller T., Gorboulev V., Vernaleken A., Koepsell H.;
RT "RS1 (RSC1A1) regulates the exocytotic pathway of Na+-D-glucose
RT cotransporter SGLT1.";
RL Am. J. Physiol. 291:F1213-F1223(2006).
RN [8]
RP DOMAIN.
RX PubMed=17686765; DOI=10.1074/jbc.m705416200;
RA Vernaleken A., Veyhl M., Gorboulev V., Kottra G., Palm D.,
RA Burckhardt B.-C., Burckhardt G., Pipkorn R., Beier N., van Amsterdam C.,
RA Koepsell H.;
RT "Tripeptides of RS1 (RSC1A1) inhibit a monosaccharide-dependent exocytotic
RT pathway of Na+-D-glucose cotransporter SGLT1 with high affinity.";
RL J. Biol. Chem. 282:28501-28513(2007).
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.
CC {ECO:0000269|PubMed:14724758, ECO:0000269|PubMed:16788146,
CC ECO:0000269|PubMed:8836035}.
CC -!- SUBUNIT: Interacts with YRDC. {ECO:0000250}.
CC -!- INTERACTION:
CC Q92681; P54727: RAD23B; NbExp=3; IntAct=EBI-3940171, EBI-954531;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16788147}.
CC Nucleus {ECO:0000269|PubMed:16788147}. Golgi apparatus, trans-Golgi
CC network {ECO:0000269|PubMed:16788147}. Note=Localizes at the inner side
CC of the plasma membrane.
CC -!- TISSUE SPECIFICITY: Expressed in small intestine, kidney and brain.
CC {ECO:0000269|PubMed:8836035}.
CC -!- DOMAIN: The tripeptides QCP and QSP mediate post-transcriptional down-
CC regulation of SLC5A1 at the trans-Golgi network. They inhibit a
CC monosaccharide-dependent exocytotic pathway of SLC5A1.
CC {ECO:0000269|PubMed:17686765}.
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DR EMBL; X82877; CAA58058.1; -; Genomic_DNA.
DR EMBL; AK314753; BAG37292.1; -; mRNA.
DR EMBL; AL121992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471167; EAW51744.1; -; Genomic_DNA.
DR CCDS; CCDS161.1; -.
DR RefSeq; NP_006502.1; NM_006511.2.
DR AlphaFoldDB; Q92681; -.
DR SMR; Q92681; -.
DR BioGRID; 112162; 12.
DR IntAct; Q92681; 4.
DR STRING; 9606.ENSP00000341963; -.
DR iPTMnet; Q92681; -.
DR PhosphoSitePlus; Q92681; -.
DR BioMuta; RSC1A1; -.
DR DMDM; 74751656; -.
DR MassIVE; Q92681; -.
DR PaxDb; Q92681; -.
DR PeptideAtlas; Q92681; -.
DR PRIDE; Q92681; -.
DR ProteomicsDB; 75405; -.
DR Antibodypedia; 28940; 49 antibodies from 17 providers.
DR DNASU; 6248; -.
DR Ensembl; ENST00000345034.2; ENSP00000341963.1; ENSG00000215695.2.
DR GeneID; 6248; -.
DR KEGG; hsa:6248; -.
DR MANE-Select; ENST00000345034.2; ENSP00000341963.1; NM_006511.3; NP_006502.1.
DR UCSC; uc010obn.2; human.
DR CTD; 6248; -.
DR DisGeNET; 6248; -.
DR GeneCards; RSC1A1; -.
DR HGNC; HGNC:10458; RSC1A1.
DR HPA; ENSG00000215695; Low tissue specificity.
DR MIM; 601966; gene.
DR neXtProt; NX_Q92681; -.
DR OpenTargets; ENSG00000215695; -.
DR PharmGKB; PA34872; -.
DR VEuPathDB; HostDB:ENSG00000215695; -.
DR eggNOG; KOG0012; Eukaryota.
DR GeneTree; ENSGT00390000005744; -.
DR HOGENOM; CLU_032729_0_0_1; -.
DR InParanoid; Q92681; -.
DR OMA; ERWTQSE; -.
DR OrthoDB; 817208at2759; -.
DR PhylomeDB; Q92681; -.
DR TreeFam; TF335675; -.
DR PathwayCommons; Q92681; -.
DR Reactome; R-HSA-549127; Organic cation transport.
DR Reactome; R-HSA-8981373; Intestinal hexose absorption.
DR SignaLink; Q92681; -.
DR BioGRID-ORCS; 6248; 13 hits in 1026 CRISPR screens.
DR ChiTaRS; RSC1A1; human.
DR GenomeRNAi; 6248; -.
DR Pharos; Q92681; Tbio.
DR PRO; PR:Q92681; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q92681; protein.
DR Bgee; ENSG00000215695; Expressed in smooth muscle tissue and 94 other tissues.
DR Genevisible; Q92681; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0045920; P:negative regulation of exocytosis; IEA:InterPro.
DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0042997; P:negative regulation of Golgi to plasma membrane protein transport; IDA:ARUK-UCL.
DR GO; GO:0032243; P:negative regulation of nucleoside transport; IDA:ARUK-UCL.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0051051; P:negative regulation of transport; IDA: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..617
FT /note="Regulatory solute carrier protein family 1 member 1"
FT /id="PRO_0000324150"
FT DOMAIN 571..611
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..412
FT /note="Involved in post-transcriptional down-regulation of
FT SLC5A1"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 62
FT /note="F -> L (in dbSNP:rs3766163)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_039679"
FT VARIANT 191
FT /note="C -> W (in dbSNP:rs34091519)"
FT /id="VAR_039680"
FT VARIANT 271
FT /note="N -> S (in dbSNP:rs3738648)"
FT /id="VAR_039681"
SQ SEQUENCE 617 AA; 66790 MW; AAF1D6B5F3F5F27D CRC64;
MSSLPTSDGF NHPARSSGQS PDVGNPMSLA RSVSASVCPI KPSDSDRIEP KAVKALKASA
EFQLNSEKKE HLSLQDLSDH ASSADHAPTD QSPAMPMQNS SEEITVAGNL EKSAERSTQG
LKFHLHTRQE ASLSVTSTRM HEPQMFLGEK DWHPENQNLS QVSDPQQHEE PGNEQYEVAQ
QKASHDQEYL CNIGDLELPE ERQQNQHKIV DLEATMKGNG LPQNVDPPSA KKSIPSSECS
GCSNSETFME IDTAQQSLVT LLNSTGRQNA NVKNIGALDL TLDNPLMEVE TSKCNPSSEI
LNDSISTQDL QPPETNVEIP GTNKEYGHYS SPSLCGSCQP SVESAEESCP SITAALKELH
ELLVVSSKPA SENTSEEVIC QSETIAEGQT SIKDLSERWT QNEHLTQNEQ CPQVSFHQAI
SVSVETEKLT GTSSDTGREA VENVNFRSLG DGLSTDKEGV PKSRESINKN RSVTVTSAKT
SNQLHCTLGV EISPKLLAGE EDALNQTSEQ TKSLSSNFIL VKDLGQGIQN SVTDRPETRE
NVCPDASRPL LEYEPPTSHP SSSPAILPPL IFPATDIDRI LRAGFTLQEA LGALHRVGGN
ADLALLVLLA KNIVVPT
