OXR1_BOVIN
ID OXR1_BOVIN Reviewed; 872 AA.
AC A5PKL1;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Oxidation resistance protein 1;
GN Name=OXR1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in protection from oxidative damage.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the OXR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI42528.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC142527; AAI42528.1; ALT_INIT; mRNA.
DR AlphaFoldDB; A5PKL1; -.
DR SMR; A5PKL1; -.
DR STRING; 9913.ENSBTAP00000050917; -.
DR PaxDb; A5PKL1; -.
DR PeptideAtlas; A5PKL1; -.
DR PRIDE; A5PKL1; -.
DR eggNOG; KOG2372; Eukaryota.
DR HOGENOM; CLU_007095_2_0_1; -.
DR InParanoid; A5PKL1; -.
DR OrthoDB; 1578762at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Mitochondrion; Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..872
FT /note="Oxidation resistance protein 1"
FT /id="PRO_0000393586"
FT DOMAIN 98..141
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 212..268
FT /note="GRAM"
FT DOMAIN 711..872
FT /note="TLDc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01234"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..576
FT /note="Mediates oxidative antimutator activity"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..86
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 MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N573"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMM3"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N573"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N573"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N573"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N573"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMM3"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMM3"
FT MOD_RES 341
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMM3"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMM3"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4KMM3"
SQ SEQUENCE 872 AA; 98112 MW; D718451449979ED8 CRC64;
MSVTNLSWLK KKSQSVDITA PGFNPLAGAG KQMPQASKPP APKTPIIEEE QNNAANSQKH
PSRRSELKRF YTIDTGQKKT LDKKDGRRMS FQKPKGTVKY TVESRDSLNS IALKFDTTPN
ELVQLNKLFS RAVVTGQVLY VPDPEYVSSV ESSPSLSPIS PLSPTSSEAE LEKTTTPDVV
HPKEPTPSSA FTAVRPVRVV SSTSEEEEAF TEKFLKINCR YITSSKGTVS GVLLVTPNNI
MFDPHKTDPL VQENGCEEYG IMCPMEEVMS AAMYKEILDS KIKESLPIEI DQLSGRDFCH
LKKVTRSNTD ELDSRIRDAA NDSASTAPRS TEESLSEDVF TESELSPVRE ELISLDELRH
DKSSGASSES VQTITQSGVE CLAVISEAAS TPDHLKSGSG HTANEVGTLS LKTGLNNLEM
PTKEGDQAAD NLQKISGLKE QSTGIKKDNQ DFPLDENSLH QEEVEKESMP CGEAIELKQK
QVVDKGKQGR EQNQDSETEV EELRKLWKSH SMQQTKQQRE TMQQVSQKEI KHKIATADIE
GSALLKEKRR HRLHKFLCLR VRKPMRKTFV SQASATMQQY AQRDKKHEYW FAVPQERTDH
LYAFFIQWSP ETYAEDTGEY TKEPGFIVVK KIEESETNED STNEAAAREW EVVSVAEYHR
RIDALNTEEL RTLCRRLQIT TREDINSKQS TPVKADLESE SFRPNLSDPS HLLLPDQIIK
LTKHLPPRTI GYPWTLVYGT RKHGTSLKTL YRTMTGLDTP VLMVIKDSDW QVFGAFASQP
FKVSDGFYGN GETFVFTFCP EFEVFKWTGD NMFFIKGDMD SLAFGGGGGE FALWLDGDLY
HGRSHSCKTF GNHTLSKKED FCIQDIEIWA FK
