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AT21B_ARATH
ID   AT21B_ARATH             Reviewed;         362 AA.
AC   P0CH02; Q3EBF2;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Putative RING-H2 finger protein ATL21B;
DE            EC=2.3.2.27 {ECO:0000305};
DE   AltName: Full=RING-type E3 ubiquitin transferase ATL21B {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ATL21B; OrderedLocusNames=At2g46494; ORFNames=F11C10, F13A10;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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).
RN   [3]
RP   GENE FAMILY ORGANIZATION.
RX   PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
RA   Kosarev P., Mayer K.F.X., Hardtke C.S.;
RT   "Evaluation and classification of RING-finger domains encoded by the
RT   Arabidopsis genome.";
RL   Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
RN   [4]
RP   NOMENCLATURE, AND GENE FAMILY ORGANIZATION.
RX   PubMed=16557337; DOI=10.1007/s00239-005-0038-y;
RA   Serrano M., Parra S., Alcaraz L.D., Guzman P.;
RT   "The ATL gene family from Arabidopsis thaliana and Oryza sativa comprises a
RT   large number of putative ubiquitin ligases of the RING-H2 type.";
RL   J. Mol. Evol. 62:434-445(2006).
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:0000305};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC       ubiquitin-conjugating enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AC006418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC006526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002685; AEC10706.1; -; Genomic_DNA.
DR   RefSeq; NP_001189761.1; NM_001202832.1.
DR   AlphaFoldDB; P0CH02; -.
DR   SMR; P0CH02; -.
DR   PaxDb; P0CH02; -.
DR   PRIDE; P0CH02; -.
DR   EnsemblPlants; AT2G46494.1; AT2G46494.1; AT2G46494.
DR   GeneID; 10723138; -.
DR   Gramene; AT2G46494.1; AT2G46494.1; AT2G46494.
DR   KEGG; ath:AT2G46494; -.
DR   Araport; AT2G46494; -.
DR   TAIR; locus:6530298193; AT2G46494.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_046769_0_0_1; -.
DR   OMA; DYHANET; -.
DR   OrthoDB; 998495at2759; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:P0CH02; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P0CH02; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR032872; WAK_assoc_C.
DR   InterPro; IPR025287; WAK_GUB.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF13947; GUB_WAK_bind; 1.
DR   Pfam; PF14380; WAK_assoc; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Membrane; Metal-binding; Reference proteome; Signal; Transferase;
KW   Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..362
FT                   /note="Putative RING-H2 finger protein ATL21B"
FT                   /id="PRO_0000396121"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         316..358
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   362 AA;  40919 MW;  4641CE9A003697E5 CRC64;
     MIISKQLFLL FFLLFFIFPL RHASNPSKCS SSNSRPHRCG PLEVPIRFPF CDHPLFNLLC
     TNLNNTVLQL PMSGTFFVQY IDYRKQQIYI NDPENCLAKR LLTFNISGSP FSPRFDTLYT
     FLTCPNELVL PSWYPSIPCL SNSTSSFFAT SNFALAESML PSCQIVKRIY VPADSPFAET
     RFSSYLNQSL LLEWNSPNCR GCEIDYLRCG FKNKASPEVK CFGAKKSGHL SRAVVAVLIC
     LSIIGAVILF VTCIAIRIHN TPRRRHWAVP AAAATVMQQP REVMATRGLD QSTIEKYKTM
     ELGESRRPPG TNGIVCPICL SEYVSKETVR FIPECDHCFH AKCIDVWLKI HGSCPLCRNS
     RA
 
 
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