RS7_RAT
ID RS7_RAT Reviewed; 194 AA.
AC P62083; P23821; P24818;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=40S ribosomal protein S7;
DE AltName: Full=S8;
GN Name=Rps7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 33-47.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2226813; DOI=10.1016/0014-5793(90)80369-t;
RA Suzuki K., Olvera J., Wool I.G.;
RT "The primary structure of rat ribosomal protein S7.";
RL FEBS Lett. 271:51-53(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Skeletal muscle;
RX PubMed=2030949; DOI=10.1093/nar/19.6.1339;
RA Guillier M., Leibovitch S.;
RT "Sequence of a cDNA encoding rat ribosomal protein homologous to Xenopus
RT laevis ribosomal protein S8.";
RL Nucleic Acids Res. 19:1339-1339(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [4]
RP PROTEIN SEQUENCE OF 1-7; 42-57; 100-106 AND 170-179, ACETYLATION AT MET-1,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Pheochromocytoma;
RA Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
RL Submitted (AUG-2006) to UniProtKB.
CC -!- FUNCTION: Required for rRNA maturation. {ECO:0000250|UniProtKB:P62081}.
CC -!- SUBUNIT: Binds IPO9 with high affinity (By similarity). Interacts with
CC NEK6 (By similarity). Interacts with DESI2 (By similarity). Interacts
CC with IPO5, IPO7 and KPNB1; these interactions may be involved in RPS7
CC nuclear import for the assembly of ribosomal subunits (By similarity).
CC {ECO:0000250|UniProtKB:P62081}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:P62081}. Cytoplasm
CC {ECO:0000250|UniProtKB:P62081}. Nucleus {ECO:0000250|UniProtKB:P62081}.
CC Note=Although RPS7 is functional within the cytoplasm, the assembly of
CC ribosomal subunits occurs in the nucleus. RPS7 nuclear import is
CC mediated by IPO5/RanBP5, IPO7/RanBP7, KPNB1/importin-beta or TPNO1/Trn
CC (By similarity). Colocalizes with NEK6 in the centrosome (By
CC similarity). {ECO:0000250|UniProtKB:P62081}.
CC -!- PTM: Phosphorylated by NEK6. {ECO:0000250|UniProtKB:P62081}.
CC -!- PTM: Ubiquitinated. Deubiquitinated by DESI2, leading to its
CC stabilization. {ECO:0000250|UniProtKB:P62081}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS7 family.
CC {ECO:0000305}.
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DR EMBL; X53377; CAA37457.1; -; mRNA.
DR EMBL; X56846; CAA40177.1; -; mRNA.
DR EMBL; BC060557; AAH60557.1; -; mRNA.
DR PIR; S12862; R3RT7.
DR RefSeq; NP_113758.2; NM_031570.2.
DR RefSeq; XP_002726666.2; XM_002726620.5.
DR RefSeq; XP_002729622.2; XM_002729576.5.
DR AlphaFoldDB; P62083; -.
DR SMR; P62083; -.
DR BioGRID; 247931; 4.
DR IntAct; P62083; 13.
DR MINT; P62083; -.
DR STRING; 10116.ENSRNOP00000011333; -.
DR iPTMnet; P62083; -.
DR PhosphoSitePlus; P62083; -.
DR SwissPalm; P62083; -.
DR jPOST; P62083; -.
DR PaxDb; P62083; -.
DR PRIDE; P62083; -.
DR GeneID; 100362830; -.
DR GeneID; 29258; -.
DR KEGG; rno:100362830; -.
DR KEGG; rno:29258; -.
DR CTD; 6201; -.
DR RGD; 61907; Rps7.
DR VEuPathDB; HostDB:ENSRNOG00000008373; -.
DR eggNOG; KOG3320; Eukaryota.
DR HOGENOM; CLU_088621_1_2_1; -.
DR InParanoid; P62083; -.
DR OMA; AAYHKVQ; -.
DR OrthoDB; 1289550at2759; -.
DR PhylomeDB; P62083; -.
DR TreeFam; TF343364; -.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-RNO-72649; Translation initiation complex formation.
DR Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-RNO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-RNO-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P62083; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000008551; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; P62083; baseline and differential.
DR Genevisible; P62083; RN.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:RGD.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:RGD.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:RGD.
DR GO; GO:0008266; F:poly(U) RNA binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; ISO:RGD.
DR GO; GO:0006364; P:rRNA processing; ISO:RGD.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR InterPro; IPR000554; Ribosomal_S7e.
DR PANTHER; PTHR11278; PTHR11278; 1.
DR Pfam; PF01251; Ribosomal_S7e; 1.
DR PROSITE; PS00948; RIBOSOMAL_S7E; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Isopeptide bond; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT CHAIN 1..194
FT /note="40S ribosomal protein S7"
FT /id="PRO_0000174192"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 74
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62081"
FT CROSSLNK 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62081"
FT CROSSLNK 74
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62081"
FT CONFLICT 2
FT /note="F -> S (in Ref. 2; CAA40177)"
FT /evidence="ECO:0000305"
FT CONFLICT 14..16
FT /note="EKP -> KKR (in Ref. 2; CAA40177)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="D -> E (in Ref. 2; CAA40177)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="A -> T (in Ref. 2; CAA40177)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="R -> W (in Ref. 2; CAA40177)"
FT /evidence="ECO:0000305"
FT CONFLICT 75..79
FT /note="IQVRL -> MAKSGK (in Ref. 2; CAA40177)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="D -> V (in Ref. 2; CAA40177)"
FT /evidence="ECO:0000305"
FT CONFLICT 180..181
FT /note="LT -> PL (in Ref. 2; CAA40177)"
FT /evidence="ECO:0000305"
FT CONFLICT 192..194
FT /note="FQL -> VSV (in Ref. 2; CAA40177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 194 AA; 22127 MW; E21089929CC061E9 CRC64;
MFSSSAKIVK PNGEKPDEFE SGISQALLEL EMNSDLKAQL RELNITAAKE IEVGGGRKAI
IIFVPVPQLK SFQKIQVRLV RELEKKFSGK HVVFIAQRRI LPKPTRKSRT KNKQKRPRSR
TLTAVHDAIL EDLVFPSEIV GKRIRVKLDG SRLIKVHLDK AQQNNVEHKV ETFSGVYKKL
TGKDVNFEFP EFQL
