RSCA1_PIG
ID RSCA1_PIG Reviewed; 623 AA.
AC Q29106;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 3.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Regulatory solute carrier protein family 1 member 1;
DE AltName: Full=Transporter regulator RS1;
GN Name=RSC1A1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=8227068; DOI=10.1016/s0021-9258(19)74569-4;
RA Veyhl M., Spangenberg J., Pueschel B., Poppe R., Fritzsch G., Koepsell H.;
RT "Cloning of a membrane-associated protein which modifies activity and
RT properties of the Na(+)-D-glucose cotransporter.";
RL J. Biol. Chem. 268:25041-25053(1993).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=11018680; DOI=10.1016/s0005-2736(00)00277-7;
RA Valentin M., Kuehlkamp T., Wagner K., Krohne G., Arndt P., Baumgarten K.,
RA Weber W.-M., Segal A., Veyhl M., Koepsell H.;
RT "The transport modifier RS1 is localized at the inner side of the plasma
RT membrane and changes membrane capacitance.";
RL Biochim. Biophys. Acta 1468:367-380(2000).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11562363; DOI=10.1074/jbc.m105975200;
RA Korn T., Kuehlkamp T., Track C., Schatz I., Baumgarten K., Gorboulev V.,
RA Koepsell H.;
RT "The plasma membrane-associated protein RS1 decreases transcription of the
RT transporter SGLT1 in confluent LLC-PK1 cells.";
RL J. Biol. Chem. 276:45330-45340(2001).
RN [4]
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).
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). {ECO:0000250, ECO:0000269|PubMed:11562363}.
CC -!- SUBUNIT: Interacts with YRDC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane. Nucleus. Golgi apparatus, trans-
CC Golgi network. Note=Localizes at the inner side of the plasma membrane.
CC Nuclear localization in subconfluent LLC-PK1 cells is drastically
CC decreased after cell confluence.
CC -!- TISSUE SPECIFICITY: Renal outer cortex and outer medulla, small
CC intestine and liver. {ECO:0000269|PubMed:8227068}.
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DR EMBL; X64315; CAA45596.2; -; mRNA.
DR PIR; A49112; A49112.
DR RefSeq; NP_998958.1; NM_213793.1.
DR AlphaFoldDB; Q29106; -.
DR SMR; Q29106; -.
DR STRING; 9823.ENSSSCP00000003759; -.
DR iPTMnet; Q29106; -.
DR PaxDb; Q29106; -.
DR GeneID; 396699; -.
DR KEGG; ssc:396699; -.
DR CTD; 6248; -.
DR eggNOG; ENOG502RYJA; Eukaryota.
DR InParanoid; Q29106; -.
DR OrthoDB; 817208at2759; -.
DR ChiTaRS; RSC1A1; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045920; P:negative regulation of exocytosis; IEA:InterPro.
DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cell membrane; Golgi apparatus; Membrane; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..623
FT /note="Regulatory solute carrier protein family 1 member 1"
FT /id="PRO_0000324152"
FT DOMAIN 577..617
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 623 AA; 66832 MW; BE32DE7DCE9A07F9 CRC64;
MSSLPTSDGF NHQAHPSGQR PEIGSPPSLA HSVSASVCPF KPSDPDSIEP KAVKAVKALK
ASAEFQITFE RKEQLPLQDP SDCASSADNA PANQTPAIPL QNSLKEAIVA DNLEKSAEGS
TQGLKSHLHT RQEASLSVTT TRMQEPQRLI GEKGWHPEYQ DPSQVNGLQQ HEEPRNEQHE
VVQQNAPHDP EHLCNTGDLE LLGERQQNQP KSVGLETAVR GDRPQQDVDL PGTEKNILPY
GCFGCSSSET FMEIDTVEQS LVAVLNSAGG QNTSVRNISA SDLTVDNPLM EVETLKCNPS
SEFLSNPTST QNLQLPESSV EMSGTNKEYG NHPSSLSLCG TCQPSVESAE ESCSSITAAL
KELHELLVIS SKPALENTSE EVTCRSEIVT EGQTDVKDLS ERWTQSEHLT AAQNEQCSQV
SFYQATSVSV KTEELTDTST DAGTEDVENI TSSGPGDGLL VDKENVPRSR ESVNESSLVT
LDSAKTSNQP HCTLGVEISP GLLAGEEGAL NQTSEQTESL SSSFILVKDL GQGTQNPVTN
RPETRENVCP EAAGLRQEFE PPTSHPSSSP SFLAPLIFPA ADIDRILRAG FTLQEALGAL
HRVGGNADLA LLVLLAKNIV VPT
