SRXN1_MOUSE
ID SRXN1_MOUSE Reviewed; 136 AA.
AC Q9D975; Q3TWN6; Q91VN5;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Sulfiredoxin-1;
DE EC=1.8.98.2 {ECO:0000250|UniProtKB:Q9BYN0};
DE AltName: Full=Neoplastic progression protein 3;
GN Name=Srxn1; Synonyms=Npn3, Srx;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary carcinoma, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland, and Retina;
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 [3]
RP FUNCTION.
RX PubMed=15448164; DOI=10.1074/jbc.m409482200;
RA Chang T.-S., Jeong W., Woo H.A., Lee S.M., Park S., Rhee S.G.;
RT "Characterization of mammalian sulfiredoxin and its reactivation of
RT hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in
RT the active site to cysteine.";
RL J. Biol. Chem. 279:50994-51001(2004).
CC -!- FUNCTION: Contributes to oxidative stress resistance by reducing
CC cysteine-sulfinic acid formed under exposure to oxidants in the
CC peroxiredoxins PRDX1, PRDX2, PRDX3 and PRDX4. Does not act on PRDX5 or
CC PRDX6. May catalyze the reduction in a multi-step process by acting
CC both as a specific phosphotransferase and a thioltransferase.
CC {ECO:0000269|PubMed:15448164}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + ATP + S-hydroxy-S-oxy-L-cysteinyl-
CC [peroxiredoxin] = [protein]-disulfide + ADP + phosphate + S-hydroxy-
CC L-cysteinyl-[peroxiredoxin]; Xref=Rhea:RHEA:17545, Rhea:RHEA-
CC COMP:10593, Rhea:RHEA-COMP:10594, Rhea:RHEA-COMP:13681, Rhea:RHEA-
CC COMP:17976, ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:61973, ChEBI:CHEBI:61974,
CC ChEBI:CHEBI:456216; EC=1.8.98.2;
CC Evidence={ECO:0000250|UniProtKB:Q9BYN0};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P36077};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BYN0}.
CC -!- SIMILARITY: Belongs to the sulfiredoxin family. {ECO:0000305}.
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DR EMBL; AK007296; BAB24939.1; -; mRNA.
DR EMBL; AK089976; BAC41025.1; -; mRNA.
DR EMBL; AK159613; BAE35230.1; -; mRNA.
DR EMBL; BC011325; AAH11325.1; -; mRNA.
DR EMBL; BC049957; AAH49957.1; -; mRNA.
DR RefSeq; NP_083964.2; NM_029688.5.
DR AlphaFoldDB; Q9D975; -.
DR SMR; Q9D975; -.
DR BioGRID; 218234; 2.
DR STRING; 10090.ENSMUSP00000046196; -.
DR PhosphoSitePlus; Q9D975; -.
DR jPOST; Q9D975; -.
DR MaxQB; Q9D975; -.
DR PaxDb; Q9D975; -.
DR PRIDE; Q9D975; -.
DR ProteomicsDB; 258623; -.
DR TopDownProteomics; Q9D975; -.
DR DNASU; 76650; -.
DR GeneID; 76650; -.
DR KEGG; mmu:76650; -.
DR CTD; 140809; -.
DR MGI; MGI:104971; Srxn1.
DR eggNOG; KOG3388; Eukaryota.
DR InParanoid; Q9D975; -.
DR OrthoDB; 1471783at2759; -.
DR BRENDA; 1.8.98.2; 3474.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR BioGRID-ORCS; 76650; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Srxn1; mouse.
DR PRO; PR:Q9D975; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9D975; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016667; F:oxidoreductase activity, acting on a sulfur group of donors; IDA:UniProtKB.
DR GO; GO:0032542; F:sulfiredoxin activity; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR InterPro; IPR003115; ParB/Sulfiredoxin_dom.
DR InterPro; IPR036086; ParB/Sulfiredoxin_sf.
DR InterPro; IPR016692; Sulfiredoxin.
DR PANTHER; PTHR21348; PTHR21348; 1.
DR Pfam; PF02195; ParBc; 1.
DR PIRSF; PIRSF017267; Sulfiredoxin; 1.
DR SMART; SM00470; ParB; 1.
DR SUPFAM; SSF110849; SSF110849; 1.
PE 2: Evidence at transcript level;
KW Antioxidant; ATP-binding; Cytoplasm; Disulfide bond; Magnesium;
KW Methylation; Nucleotide-binding; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..136
FT /note="Sulfiredoxin-1"
FT /id="PRO_0000211432"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BYN0"
FT MOD_RES 11
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYN0"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYN0"
FT DISULFID 98
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P36077"
FT CONFLICT 20..22
FT /note="EGQ -> VVH (in Ref. 2; AAH11325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 136 AA; 14149 MW; D8BCDAC6277E27DE CRC64;
MGLRAGGALR RAGAGPGAPE GQGPGGAQGG SIHSGCIATV HNVPIAVLIR PLPSVLDPAK
VQSLVDTILA DPDSVPPIDV LWIKGAQGGD YYYSFGGCHR YAAYQQLQRE TIPAKLVRST
LSDLRMYLGA STPDLQ
