ID   Q6TXJ6_RAT              Unreviewed;       454 AA.
AC   Q6TXJ6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Small ribosomal subunit protein eS1 {ECO:0000256|HAMAP-Rule:MF_03122};
GN   Name=Cyld {ECO:0000313|Ensembl:ENSRNOP00000070060.1,
GN   ECO:0000313|RGD:1308346};
GN   Synonyms=LOC100362727 {ECO:0000313|RGD:1308346}, RPS3A
GN   {ECO:0000256|HAMAP-Rule:MF_03122};
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 {ECO:0000313|EMBL:AAQ96216.1};
RN   [1] {ECO:0000313|EMBL:AAQ96216.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sprague-Dawley {ECO:0000313|EMBL:AAQ96216.1};
RA   Xu C.S., Chang C.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J.,
RA   Zhao L.F., Ma H., Wang L., Wang S.F., Xing X.K., Shen G.M., Shi J.B.,
RA   Rahman S., Wang Q.N., Zhang J.B.;
RT   "Liver regeneration after PH.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000070060.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070060.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000070060.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070060.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May play a role during erythropoiesis through regulation of
CC       transcription factor DDIT3. {ECO:0000256|HAMAP-Rule:MF_03122}.
CC   -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC       consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC       contains about 33 different proteins and 1 molecule of RNA (18S). The
CC       60S subunit contains about 49 different proteins and 3 molecules of RNA
CC       (28S, 5.8S and 5S). Identified in a IGF2BP1-dependent mRNP granule
CC       complex containing untranslated mRNAs. Binds with high affinity to
CC       IPO4. Interacts with DDIT3. {ECO:0000256|HAMAP-Rule:MF_03122}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03122}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03122}. Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}. Note=Localized in cytoplasmic mRNP
CC       granules containing untranslated mRNAs. {ECO:0000256|HAMAP-
CC       Rule:MF_03122}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_03122}.
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DR   EMBL; AY383658; AAQ96216.1; -; mRNA.
DR   MEROPS; C67.001; -.
DR   Ensembl; ENSRNOT00000091626.2; ENSRNOP00000070060.1; ENSRNOG00000014048.8.
DR   RGD; 1308346; Cyld.
DR   GeneTree; ENSGT00390000018123; -.
DR   HOGENOM; CLU_602623_0_0_1; -.
DR   TreeFam; TF300037; -.
DR   Proteomes; UP000002494; Chromosome 19.
DR   Bgee; ENSRNOG00000014048; Expressed in testis and 18 other cell types or tissues.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   HAMAP; MF_03122; Ribosomal_S3Ae_euk; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001593; Ribosomal_eS1.
DR   InterPro; IPR027500; Ribosomal_eS1_euk.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR11830; 40S RIBOSOMAL PROTEIN S3A; 1.
DR   PANTHER; PTHR11830:SF28; 40S RIBOSOMAL PROTEIN S3A; 1.
DR   Pfam; PF01015; Ribosomal_S3Ae; 1.
DR   SMART; SM01397; Ribosomal_S3Ae; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; Q6TXJ6; RN.
PE   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03122};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Differentiation {ECO:0000256|HAMAP-Rule:MF_03122};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03122};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_03122};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_03122}.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03122"
FT   DOMAIN          137..448
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  52009 MW;  8828E384B9F8F69F CRC64;
     MAVRKNQHPT KGGKKGAKKK VVDPFSKKDW YDVKAPAMFN IRSIRKTLVT RTQGAKTAPD
     GLEGRVFEGR LADLQNDEDS FRKVKLNTED VQGKNFHGMD LTRDRMCSVV KKWQTTMIEA
     LVDVKTTDGY LLRLFCVGFT KKYNNQIRKI SYSQVYQIQK KMMEIMTREV QTNDLKEVVN
     KLILGSIGKD IEKVCQSIHP LHDVFVRKVK MLKKPKFELG KPMELHGEGG GSHKTTAFGG
     YLSEVVEENT PPKMEKEGLE IMIGKKKGIQ GHYNSCYLDS TLFWQCRICG GLAMYECREC
     YDDPDISAGK IKQFCKTCST QVHLHPRRLN HTYHPVSLPK DLPDWDWRHG CIPCQKMELF
     AVLCIETSHY VAFVKYGKDD SAWLFFDSMA DRDGGQNGFN IPQVTPCPEV GEYLKMSLED
     LHSLDSRRIQ GCARRLLCDA YMCMYQSPTM SLYK
//