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AT21A_ARATH
ID   AT21A_ARATH             Reviewed;         372 AA.
AC   P0CH01; Q3EBF2;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Putative RING-H2 finger protein ATL21A;
DE            EC=2.3.2.27 {ECO:0000305};
DE   AltName: Full=RING-type E3 ubiquitin transferase ATL21A {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ATL21A; OrderedLocusNames=At2g46495; 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; AEC10707.1; -; Genomic_DNA.
DR   RefSeq; NP_850456.2; NM_180125.3.
DR   AlphaFoldDB; P0CH01; -.
DR   SMR; P0CH01; -.
DR   STRING; 3702.AT2G46495.1; -.
DR   iPTMnet; P0CH01; -.
DR   PaxDb; P0CH01; -.
DR   PRIDE; P0CH01; -.
DR   EnsemblPlants; AT2G46495.1; AT2G46495.1; AT2G46495.
DR   GeneID; 819259; -.
DR   Gramene; AT2G46495.1; AT2G46495.1; AT2G46495.
DR   KEGG; ath:AT2G46495; -.
DR   Araport; AT2G46495; -.
DR   TAIR; locus:504956082; AT2G46495.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_046769_0_0_1; -.
DR   OrthoDB; 998495at2759; -.
DR   PhylomeDB; P0CH01; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:P0CH01; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P0CH01; 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; IPR025287; WAK_GUB.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF13947; GUB_WAK_bind; 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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..372
FT                   /note="Putative RING-H2 finger protein ATL21A"
FT                   /id="PRO_0000396120"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         320..362
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   372 AA;  41591 MW;  6CB022460895D5CD CRC64;
     MTFSKQLFLY LFFLFPLLHA SHPQQCSSSS CGRDDVHVRF PFWLLSKQPE LCGHAGFNLQ
     CTASPKTALK LPNSGTFLVR EIDYLSQQIR LYDPENCLAR KLLTFDISRS PFSALYLVSY
     TFLSCPNEVA KSSRFDSIPC LGNSTTSFLA TTSLDLAKSM LPSCQIVKTL DVPVSRRVIA
     KKSRFSTDVN DKDLWLKWDS PSCSDCERDF LRCGFRSNTS LQVKCFPFEN SGYNTEPQVL
     KIILLSIIGP LTIFATCIAV GVCTSERFAS LIQRNVAIAA LQPNEVIVTT GLDESIIESY
     KKTELGESRR LPGNNDDIVC PICLSEYASK ETVRCIPECD HCFHSECIDV WLKIHGSCPL
     CRNSPSPARQ AV
 
 
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