OXR1_MOUSE
ID OXR1_MOUSE Reviewed; 866 AA.
AC Q4KMM3; Q5FWW1; Q99L06; Q99MK1; Q99MP4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Oxidation resistance protein 1;
DE AltName: Full=Protein C7;
GN Name=Oxr1; Synonyms=C7, Gm1238;
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 [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=11237729; DOI=10.1006/bbrc.2001.4345;
RA Fischer H., Zhang X.U., O'Brien K.P., Kylsten P., Engvall E.;
RT "C7, a novel nucleolar protein, is the mouse homologue of the Drosophila
RT late puff product L82 and an isoform of human OXR1.";
RL Biochem. Biophys. Res. Commun. 281:795-803(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=CD-1; TISSUE=Mammary gland, and Neural stem cell;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118; SER-201; SER-204;
RP SER-294; SER-334; SER-336; THR-341; SER-346 AND SER-488, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be involved in protection from oxidative damage.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:11237729}. Note=According to PubMed:11237729 it is
CC nucleolar.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q4KMM3-1; Sequence=Displayed;
CC Name=2; Synonyms=C7B;
CC IsoId=Q4KMM3-2; Sequence=VSP_039015;
CC Name=3; Synonyms=C7A;
CC IsoId=Q4KMM3-3; Sequence=VSP_039015, VSP_039016;
CC Name=4;
CC IsoId=Q4KMM3-4; Sequence=VSP_039016;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and testis.
CC {ECO:0000269|PubMed:11237729}.
CC -!- SIMILARITY: Belongs to the OXR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH03927.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH98491.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE34619.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF324899; AAK30368.1; -; mRNA.
DR EMBL; AF333985; AAK29400.1; -; mRNA.
DR EMBL; AK158703; BAE34619.1; ALT_INIT; mRNA.
DR EMBL; BC003927; AAH03927.1; ALT_INIT; mRNA.
DR EMBL; BC089183; AAH89183.1; -; mRNA.
DR EMBL; BC098491; AAH98491.1; ALT_INIT; mRNA.
DR CCDS; CCDS27448.1; -. [Q4KMM3-2]
DR CCDS; CCDS49598.1; -. [Q4KMM3-1]
DR CCDS; CCDS49600.1; -. [Q4KMM3-3]
DR CCDS; CCDS88760.1; -. [Q4KMM3-4]
DR RefSeq; NP_001123635.1; NM_001130163.1. [Q4KMM3-3]
DR RefSeq; NP_001123636.1; NM_001130164.1.
DR RefSeq; NP_001123637.1; NM_001130165.1.
DR RefSeq; NP_001123638.1; NM_001130166.1. [Q4KMM3-1]
DR RefSeq; NP_570955.1; NM_130885.2. [Q4KMM3-2]
DR RefSeq; XP_017171979.1; XM_017316490.1.
DR RefSeq; XP_017171980.1; XM_017316491.1.
DR AlphaFoldDB; Q4KMM3; -.
DR SMR; Q4KMM3; -.
DR BioGRID; 228391; 2.
DR IntAct; Q4KMM3; 1.
DR STRING; 10090.ENSMUSP00000105926; -.
DR iPTMnet; Q4KMM3; -.
DR PhosphoSitePlus; Q4KMM3; -.
DR SwissPalm; Q4KMM3; -.
DR EPD; Q4KMM3; -.
DR jPOST; Q4KMM3; -.
DR MaxQB; Q4KMM3; -.
DR PaxDb; Q4KMM3; -.
DR PeptideAtlas; Q4KMM3; -.
DR PRIDE; Q4KMM3; -.
DR ProteomicsDB; 295497; -. [Q4KMM3-1]
DR ProteomicsDB; 295498; -. [Q4KMM3-2]
DR ProteomicsDB; 295499; -. [Q4KMM3-3]
DR ProteomicsDB; 295500; -. [Q4KMM3-4]
DR Antibodypedia; 26472; 214 antibodies from 28 providers.
DR DNASU; 170719; -.
DR Ensembl; ENSMUST00000022918; ENSMUSP00000022918; ENSMUSG00000022307. [Q4KMM3-2]
DR Ensembl; ENSMUST00000090095; ENSMUSP00000087553; ENSMUSG00000022307. [Q4KMM3-3]
DR Ensembl; ENSMUST00000090096; ENSMUSP00000087554; ENSMUSG00000022307. [Q4KMM3-3]
DR Ensembl; ENSMUST00000110297; ENSMUSP00000105926; ENSMUSG00000022307. [Q4KMM3-1]
DR Ensembl; ENSMUST00000179393; ENSMUSP00000136923; ENSMUSG00000022307. [Q4KMM3-3]
DR Ensembl; ENSMUST00000230203; ENSMUSP00000155237; ENSMUSG00000022307. [Q4KMM3-4]
DR GeneID; 170719; -.
DR KEGG; mmu:170719; -.
DR UCSC; uc007vot.2; mouse. [Q4KMM3-1]
DR UCSC; uc007vpa.1; mouse. [Q4KMM3-3]
DR CTD; 55074; -.
DR MGI; MGI:2179326; Oxr1.
DR VEuPathDB; HostDB:ENSMUSG00000022307; -.
DR eggNOG; KOG2372; Eukaryota.
DR GeneTree; ENSGT00940000155187; -.
DR HOGENOM; CLU_007095_2_0_1; -.
DR InParanoid; Q4KMM3; -.
DR OMA; SGKDFCH; -.
DR OrthoDB; 767847at2759; -.
DR PhylomeDB; Q4KMM3; -.
DR TreeFam; TF313530; -.
DR BioGRID-ORCS; 170719; 4 hits in 69 CRISPR screens.
DR ChiTaRS; Oxr1; mouse.
DR PRO; PR:Q4KMM3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q4KMM3; protein.
DR Bgee; ENSMUSG00000022307; Expressed in medial dorsal nucleus of thalamus and 247 other tissues.
DR ExpressionAtlas; Q4KMM3; baseline and differential.
DR Genevisible; Q4KMM3; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:MGI.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0071447; P:cellular response to hydroperoxide; IMP:MGI.
DR GO; GO:1900408; P:negative regulation of cellular response to oxidative stress; IDA:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IDA:MGI.
DR GO; GO:1902083; P:negative regulation of peptidyl-cysteine S-nitrosylation; IDA:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR006571; TLDc_dom.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF07534; TLD; 1.
DR SMART; SM00257; LysM; 1.
DR SMART; SM00584; TLDc; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS51886; TLDC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..866
FT /note="Oxidation resistance protein 1"
FT /id="PRO_0000231646"
FT DOMAIN 98..141
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 213..268
FT /note="GRAM"
FT DOMAIN 705..866
FT /note="TLDc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01234"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..570
FT /note="Mediates oxidative antimutator activity"
FT /evidence="ECO:0000250"
FT REGION 682..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N573"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N573"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..88
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11237729,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039015"
FT VAR_SEQ 646..672
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11237729,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039016"
FT CONFLICT 107..109
FT /note="SLN -> PLY (in Ref. 1; AAK29400)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="L -> H (in Ref. 1; AAK29400)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="S -> A (in Ref. 3; AAH89183/AAH98491)"
FT /evidence="ECO:0000305"
FT CONFLICT 435..437
FT /note="TEV -> PEI (in Ref. 3; AAH89183/AAH98491)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="S -> L (in Ref. 3; AAH89183/AAH98491)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="D -> G (in Ref. 3; AAH98491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 866 AA; 95912 MW; 15FB6B37144B1668 CRC64;
MSVSNLSWLK KKSQSVDITA PGFNPLGGAG KQAPQASKPP APKTPIIEEE QNNSANTQKH
PSRKSELKRF YTIDTGQKKT LDKKDGRRMS FQKPKGTIEY TVESRDSLNS IALKFDTTPN
ELVQLNKLFS RAVVTGQVLY VPDPEYVSSV ESSPSLSPVS PLSPTSSEAE FDKTTTPDVA
HPKEAPPAST VSGIRPARVV SSTSEEEEAF TEKFLKINCK YITIGKGTVS GVLLVTPNNI
MFDPHKTDPL VQENGCEEYG IMCPMEEVMS AAMYKEILDS KIKESLPIEL DQLSGRGSCH
SKKATGVSAE DADPRARDQG NDSASTAPRS TEESLSEDAF TESELSPIRE ELLSSEPRQE
KSSDASSESV QTVSQMEVQS LTATSEAANV PDRTSSNPGA LSHETGLSGL ETATKGGDKA
TESLQEVSGP KEQSTEVKGQ DNQDSSHQES SLQQEAGEDS VSSGETVELK EKPAVLKDQQ
GQELKRDSET EVEELRKLWK THSMQQAKQQ RDTIQQVSQR ESKHSSAAAD AHGEGSSLLK
EKRRHRLHKF LCLRVGKPMR KTFVSQASAT MQQYAQRDKK HEYWFAVPQE RTDHLYAFFI
QWSPEIYAED SGEYTREPGF IVVKKMDESE ANEAPAGEAA AREWEVVSVA EYHRRIDALN
TEELRTLCRR LQITTREDIN SKQVAPAKAD LEPESFRPNL SDPSELLLPD QIEKLTKHLP
PRTIGYPWTL VYGTGKHGTS LKTLYRTMTG LDTPVLMVIK DSDGQVFGAL ASEPFKVSDG
FYGTGETFVF TFCPEFEVFK WTGDNMFFIK GDMDSLAFGG GGGEFALWLD GDLYHGRSHS
CKTFGNHTLS KKEDFFIQDI EIWAFE
