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SIRP1_ORYSJ
ID   SIRP1_ORYSJ             Reviewed;         323 AA.
AC   Q6AVN2; Q0DH72;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=E3 ubiquitin-protein ligase SIRP1 {ECO:0000305};
DE            EC=2.3.2.27 {ECO:0000269|PubMed:27118216};
DE   AltName: Full=Salt-induced RING finger protein 1 {ECO:0000303|PubMed:27118216};
DE            Short=OsSIRP1 {ECO:0000303|PubMed:27118216};
GN   Name=SIRP1 {ECO:0000303|PubMed:27118216};
GN   OrderedLocusNames=Os05g0488800 {ECO:0000312|EMBL:BAS94636.1},
GN   LOC_Os05g40980 {ECO:0000305};
GN   ORFNames=OJ1119_H02.11 {ECO:0000312|EMBL:AAT77283.1},
GN   OsJ_19008 {ECO:0000312|EMBL:EEE64176.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RG   The rice full-length cDNA consortium;
RT   "Oryza sativa full length cDNA.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, AND
RP   MUTAGENESIS OF CYS-225.
RX   PubMed=27118216; DOI=10.1111/ppl.12459;
RA   Hwang S.G., Kim J.J., Lim S.D., Park Y.C., Moon J.C., Jang C.S.;
RT   "Molecular dissection of Oryza sativa salt-induced RING Finger Protein 1
RT   (OsSIRP1): possible involvement in the sensitivity response to salinity
RT   stress.";
RL   Physiol. Plantarum 158:168-179(2016).
CC   -!- FUNCTION: Possesses E3 ubiqutin-protein ligase activity in vitro. Acts
CC       as negative regulator of salinity stress tolerance mediated by the
CC       ubiquitin-proteasome degradation pathway.
CC       {ECO:0000269|PubMed:27118216}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000269|PubMed:27118216};
CC   -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27118216}.
CC   -!- INDUCTION: Induced by salt stress in roots (PubMed:27118216). Induced
CC       by heat shock, drought stress and abscisic acid (ABA)
CC       (PubMed:27118216). {ECO:0000269|PubMed:27118216}.
CC   -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC       ubiquitin-conjugating enzyme. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Plants over-expressing SIRP1 exhibit enhanced
CC       sensitivity to seed germination and root growth inhibition by salt
CC       stress. {ECO:0000269|PubMed:27118216}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF17801.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC097175; AAT77283.1; -; Genomic_DNA.
DR   EMBL; AP008211; BAF17801.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014961; BAS94636.1; -; Genomic_DNA.
DR   EMBL; CM000142; EEE64176.1; -; Genomic_DNA.
DR   EMBL; AK240640; BAH00840.1; -; mRNA.
DR   RefSeq; XP_015637458.1; XM_015781972.1.
DR   AlphaFoldDB; Q6AVN2; -.
DR   SMR; Q6AVN2; -.
DR   STRING; 4530.OS05T0488800-01; -.
DR   PaxDb; Q6AVN2; -.
DR   PRIDE; Q6AVN2; -.
DR   EnsemblPlants; Os05t0488800-01; Os05t0488800-01; Os05g0488800.
DR   GeneID; 4339152; -.
DR   Gramene; Os05t0488800-01; Os05t0488800-01; Os05g0488800.
DR   KEGG; osa:4339152; -.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_034892_4_0_1; -.
DR   InParanoid; Q6AVN2; -.
DR   OMA; DMDSHIQ; -.
DR   OrthoDB; 1249953at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000007752; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR   InterPro; IPR029040; RPABC4/Spt4.
DR   InterPro; IPR039738; SIRP1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22765:SF261; PTHR22765:SF261; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   Pfam; PF14369; zinc_ribbon_9; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF63393; SSF63393; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Metal-binding; Reference proteome; Stress response; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..323
FT                   /note="E3 ubiquitin-protein ligase SIRP1"
FT                   /id="PRO_0000440260"
FT   ZN_FING         199..240
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          248..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         225
FT                   /note="C->A: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:27118216"
SQ   SEQUENCE   323 AA;  35562 MW;  EDD8C2C3BC814DAF CRC64;
     MAEAAITRYW CHECEQAIEE AMVDEIKCPS CGGGFVEEMT DEEIERLTNR QPEPGFSQWN
     PIEHPGETMD SDDEDNDLGR EFEGFIRRHR RASTLRRVLD SIHDDLADDQ ERDSSILINA
     FNQALALQGS VLDPDEGQGD QGGSTNDDGL LEEYVLGAGL SLLLQHLAES DPSRNGTPPA
     KKEAVEALPT VKIEEVVSCS VCLDDLEVGS QAKQMPCEHK FHSSCILPWL ELHSSCPVCR
     FELPSEETKD LNEPSNIGRV EDSHEEVRAD GPGNVSESSN RPWAIVPWLN ELFSTREAQN
     AGGVSTDQQS PHTSGTNPNA GHS
 
 
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