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SINL9_ARATH
ID   SINL9_ARATH             Reviewed;         276 AA.
AC   Q9FKD5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Putative E3 ubiquitin-protein ligase SINA-like 9;
DE            EC=2.3.2.27;
DE   AltName: Full=RING-type E3 ubiquitin transferase SINA-like 9 {ECO:0000305};
DE   AltName: Full=Seven in absentia-like protein 9;
GN   OrderedLocusNames=At5g37910; ORFNames=K18L3.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC       subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC       ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC       form of a thioester and then directly transfers the ubiquitin to
CC       targeted substrates. It probably triggers the ubiquitin-mediated
CC       degradation of different substrates. {ECO:0000250}.
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;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC       ligase activity. {ECO:0000250}.
CC   -!- DOMAIN: The SBD domain (substrate-binding domain) mediates the
CC       homodimerization and the interaction with substrate proteins. It is
CC       related to the TRAF family. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC       {ECO:0000305}.
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DR   EMBL; AB012241; BAB09037.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94246.1; -; Genomic_DNA.
DR   RefSeq; NP_198607.1; NM_123150.1.
DR   AlphaFoldDB; Q9FKD5; -.
DR   STRING; 3702.AT5G37910.1; -.
DR   PaxDb; Q9FKD5; -.
DR   PRIDE; Q9FKD5; -.
DR   EnsemblPlants; AT5G37910.1; AT5G37910.1; AT5G37910.
DR   GeneID; 833770; -.
DR   Gramene; AT5G37910.1; AT5G37910.1; AT5G37910.
DR   KEGG; ath:AT5G37910; -.
DR   Araport; AT5G37910; -.
DR   TAIR; locus:2153774; AT5G37910.
DR   eggNOG; KOG3002; Eukaryota.
DR   HOGENOM; CLU_040603_2_2_1; -.
DR   InParanoid; Q9FKD5; -.
DR   OMA; CIAPSIQ; -.
DR   OrthoDB; 918518at2759; -.
DR   PhylomeDB; Q9FKD5; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9FKD5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FKD5; baseline and differential.
DR   Genevisible; Q9FKD5; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.40.10; -; 2.
DR   InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR   InterPro; IPR044286; SINL_plant.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR013010; Znf_SIAH.
DR   PANTHER; PTHR46632; PTHR46632; 1.
DR   Pfam; PF03145; Sina; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS51081; ZF_SIAH; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..276
FT                   /note="Putative E3 ubiquitin-protein ligase SINA-like 9"
FT                   /id="PRO_0000299198"
FT   ZN_FING         38..74
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         91..149
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00455"
FT   REGION          88..274
FT                   /note="SBD"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   276 AA;  30852 MW;  0AD5D3AC2CC91EE1 CRC64;
     MVLASISEAL ISQGDGGERV AKRQRSAIVL LDLDILDCPI CCEALTSPIF QCDNGHLACG
     SCCPKLSNKC PACTLPVGHS RSRAMESVLE SILIPCPNVR FGCTKSFFYG KESAHEKECI
     FSQCSCPSSV CDYTGSYKDL YAHYKLTHST NIFWNIKRFR CANFFTTSML ISDKILIKRV
     HEKKLLLAVQ CFREPCGVYV TVSFIAPSAP EVGEFSYQLS YNVDGHTVTY ESPEVKRVCK
     VSIETPQENF MLIPHSLLRG DLLEMQVFII ENVDQE
 
 
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