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Protein

Regulatory solute carrier protein family 1 member 1

Gene

RSC1A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Mediates transcriptional and post-transcriptional regulation of SLC5A1. Inhibits a dynamin and PKC-dependent exocytotic pathway of SLC5A1. Also involved in transcriptional regulation of SLC22A2. Exhibits glucose-dependent, short-term inhibition of SLC5A1 and SLC22A2 by inhibiting the release of vesicles from the trans-Golgi network.3 Publications

GO - Molecular functioni

  • ion channel inhibitor activity Source: ProtInc

GO - Biological processi

  • negative regulation of transport Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
  • transport Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory solute carrier protein family 1 member 1
Alternative name(s):
Transporter regulator RS1
Short name:
hRS1
Gene namesi
Name:RSC1A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:10458. RSC1A1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34872.

Polymorphism and mutation databases

BioMutaiRSC1A1.
DMDMi74751656.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 617617Regulatory solute carrier protein family 1 member 1PRO_0000324150Add
BLAST

Proteomic databases

EPDiQ92681.
MaxQBiQ92681.
PaxDbiQ92681.
PeptideAtlasiQ92681.
PRIDEiQ92681.

PTM databases

iPTMnetiQ92681.
PhosphoSiteiQ92681.

Expressioni

Tissue specificityi

Expressed in small intestine, kidney and brain.1 Publication

Gene expression databases

CleanExiHS_RSC1A1.
GenevisibleiQ92681. HS.

Organism-specific databases

HPAiHPA027813.
HPA027814.
HPA028676.

Interactioni

Subunit structurei

Interacts with YRDC.By similarity

Protein-protein interaction databases

BioGridi112162. 3 interactions.
IntActiQ92681. 1 interaction.
STRINGi9606.ENSP00000341963.

Structurei

3D structure databases

ProteinModelPortaliQ92681.
SMRiQ92681. Positions 571-608.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini571 – 61141UBAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni410 – 4123Involved in post-transcriptional down-regulation of SLC5A1

Domaini

The tripeptides QCP and QSP mediate post-transcriptional down-regulation of SLC5A1 at the trans-Golgi network. They inhibit a monosaccharide-dependent exocytotic pathway of SLC5A1.1 Publication

Sequence similaritiesi

Contains 1 UBA domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IJPT. Eukaryota.
ENOG4111B03. LUCA.
GeneTreeiENSGT00390000005744.
HOGENOMiHOG000049187.
HOVERGENiHBG101192.
InParanoidiQ92681.
OMAiETREDVC.
OrthoDBiEOG77HDD7.
PhylomeDBiQ92681.
TreeFamiTF335675.

Family and domain databases

InterProiIPR015940. UBA.
[Graphical view]
SMARTiSM00165. UBA. 1 hit.
[Graphical view]
PROSITEiPS50030. UBA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92681-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSLPTSDGF NHPARSSGQS PDVGNPMSLA RSVSASVCPI KPSDSDRIEP
60 70 80 90 100
KAVKALKASA EFQLNSEKKE HLSLQDLSDH ASSADHAPTD QSPAMPMQNS
110 120 130 140 150
SEEITVAGNL EKSAERSTQG LKFHLHTRQE ASLSVTSTRM HEPQMFLGEK
160 170 180 190 200
DWHPENQNLS QVSDPQQHEE PGNEQYEVAQ QKASHDQEYL CNIGDLELPE
210 220 230 240 250
ERQQNQHKIV DLEATMKGNG LPQNVDPPSA KKSIPSSECS GCSNSETFME
260 270 280 290 300
IDTAQQSLVT LLNSTGRQNA NVKNIGALDL TLDNPLMEVE TSKCNPSSEI
310 320 330 340 350
LNDSISTQDL QPPETNVEIP GTNKEYGHYS SPSLCGSCQP SVESAEESCP
360 370 380 390 400
SITAALKELH ELLVVSSKPA SENTSEEVIC QSETIAEGQT SIKDLSERWT
410 420 430 440 450
QNEHLTQNEQ CPQVSFHQAI SVSVETEKLT GTSSDTGREA VENVNFRSLG
460 470 480 490 500
DGLSTDKEGV PKSRESINKN RSVTVTSAKT SNQLHCTLGV EISPKLLAGE
510 520 530 540 550
EDALNQTSEQ TKSLSSNFIL VKDLGQGIQN SVTDRPETRE NVCPDASRPL
560 570 580 590 600
LEYEPPTSHP SSSPAILPPL IFPATDIDRI LRAGFTLQEA LGALHRVGGN
610
ADLALLVLLA KNIVVPT
Length:617
Mass (Da):66,790
Last modified:February 1, 1997 - v1
Checksum:iAAF1D6B5F3F5F27D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti62 – 621F → L.1 Publication
Corresponds to variant rs3766163 [ dbSNP | Ensembl ].
VAR_039679
Natural varianti191 – 1911C → W.
Corresponds to variant rs34091519 [ dbSNP | Ensembl ].
VAR_039680
Natural varianti271 – 2711N → S.
Corresponds to variant rs3738648 [ dbSNP | Ensembl ].
VAR_039681

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82877 Genomic DNA. Translation: CAA58058.1.
AK314753 mRNA. Translation: BAG37292.1.
AL121992 Genomic DNA. Translation: CAI95731.1.
CH471167 Genomic DNA. Translation: EAW51744.1.
CCDSiCCDS161.1.
RefSeqiNP_006502.1. NM_006511.2.
UniGeneiHs.239459.
Hs.709169.
Hs.718857.

Genome annotation databases

EnsembliENST00000345034; ENSP00000341963; ENSG00000215695.
GeneIDi6248.
KEGGihsa:6248.
UCSCiuc010obn.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82877 Genomic DNA. Translation: CAA58058.1.
AK314753 mRNA. Translation: BAG37292.1.
AL121992 Genomic DNA. Translation: CAI95731.1.
CH471167 Genomic DNA. Translation: EAW51744.1.
CCDSiCCDS161.1.
RefSeqiNP_006502.1. NM_006511.2.
UniGeneiHs.239459.
Hs.709169.
Hs.718857.

3D structure databases

ProteinModelPortaliQ92681.
SMRiQ92681. Positions 571-608.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112162. 3 interactions.
IntActiQ92681. 1 interaction.
STRINGi9606.ENSP00000341963.

PTM databases

iPTMnetiQ92681.
PhosphoSiteiQ92681.

Polymorphism and mutation databases

BioMutaiRSC1A1.
DMDMi74751656.

Proteomic databases

EPDiQ92681.
MaxQBiQ92681.
PaxDbiQ92681.
PeptideAtlasiQ92681.
PRIDEiQ92681.

Protocols and materials databases

DNASUi6248.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000345034; ENSP00000341963; ENSG00000215695.
GeneIDi6248.
KEGGihsa:6248.
UCSCiuc010obn.2. human.

Organism-specific databases

CTDi6248.
GeneCardsiRSC1A1.
HGNCiHGNC:10458. RSC1A1.
HPAiHPA027813.
HPA027814.
HPA028676.
MIMi601966. gene.
neXtProtiNX_Q92681.
PharmGKBiPA34872.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IJPT. Eukaryota.
ENOG4111B03. LUCA.
GeneTreeiENSGT00390000005744.
HOGENOMiHOG000049187.
HOVERGENiHBG101192.
InParanoidiQ92681.
OMAiETREDVC.
OrthoDBiEOG77HDD7.
PhylomeDBiQ92681.
TreeFamiTF335675.

Miscellaneous databases

GenomeRNAii6248.
PROiQ92681.
SOURCEiSearch...

Gene expression databases

CleanExiHS_RSC1A1.
GenevisibleiQ92681. HS.

Family and domain databases

InterProiIPR015940. UBA.
[Graphical view]
SMARTiSM00165. UBA. 1 hit.
[Graphical view]
PROSITEiPS50030. UBA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human gene of a protein that modifies Na(+)-D-glucose co-transport."
    Lambotte S., Veyhl M., Koehler M., Morrison-Shetlar A.I., Kinne R.K.H., Schmid M., Koepsell H.
    DNA Cell Biol. 15:769-777(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-62.
    Tissue: Hippocampus.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Downregulation of the Na(+)- D-glucose cotransporter SGLT1 by protein RS1 (RSC1A1) is dependent on dynamin and protein kinase C."
    Veyhl M., Wagner C.A., Gorboulev V., Schmitt B.M., Lang F., Koepsell H.
    J. Membr. Biol. 196:71-81(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Transporter regulator RS1 (RSC1A1) coats the trans-Golgi network and migrates into the nucleus."
    Kroiss M., Leyerer M., Gorboulev V., Kuehlkamp T., Kipp H., Koepsell H.
    Am. J. Physiol. 291:F1201-F1212(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "RS1 (RSC1A1) regulates the exocytotic pathway of Na+-D-glucose cotransporter SGLT1."
    Veyhl M., Keller T., Gorboulev V., Vernaleken A., Koepsell H.
    Am. J. Physiol. 291:F1213-F1223(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Tripeptides of RS1 (RSC1A1) inhibit a monosaccharide-dependent exocytotic pathway of Na+-D-glucose cotransporter SGLT1 with high affinity."
    Vernaleken A., Veyhl M., Gorboulev V., Kottra G., Palm D., Burckhardt B.-C., Burckhardt G., Pipkorn R., Beier N., van Amsterdam C., Koepsell H.
    J. Biol. Chem. 282:28501-28513(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.

Entry informationi

Entry nameiRSCA1_HUMAN
AccessioniPrimary (citable) accession number: Q92681
Secondary accession number(s): B2RBP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: February 1, 1997
Last modified: July 6, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.