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AT12B_ARATH
ID   AT12B_ARATH             Reviewed;          94 AA.
AC   Q9LVK3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Ubiquitin-like protein ATG12B;
DE   AltName: Full=Autophagy-related protein 12b;
DE            Short=APG12-like protein b;
DE            Short=AtAPG12b;
GN   Name=ATG12B; Synonyms=APG12, APG12B; OrderedLocusNames=At3g13970;
GN   ORFNames=MDC16.9;
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 [MRNA], NOMENCLATURE, AND GENE FAMILY.
RX   PubMed=12114572; DOI=10.1104/pp.011024;
RA   Hanaoka H., Noda T., Shirano Y., Kato T., Hayashi H., Shibata D.,
RA   Tabata S., Ohsumi Y.;
RT   "Leaf senescence and starvation-induced chlorosis are accelerated by the
RT   disruption of an Arabidopsis autophagy gene.";
RL   Plant Physiol. 129:1181-1193(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-94.
RX   PubMed=16874047; DOI=10.4161/auto.1.2.1859;
RA   Suzuki N.N., Yoshimoto K., Fujioka Y., Ohsumi Y., Inagaki F.;
RT   "The crystal structure of plant ATG12 and its biological implication in
RT   autophagy.";
RL   Autophagy 1:119-126(2005).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16040659; DOI=10.1104/pp.105.060673;
RA   Thompson A.R., Doelling J.H., Suttangkakul A., Vierstra R.D.;
RT   "Autophagic nutrient recycling in Arabidopsis directed by the ATG8 and
RT   ATG12 conjugation pathways.";
RL   Plant Physiol. 138:2097-2110(2005).
CC   -!- FUNCTION: Ubiquitin-like protein involved in cytoplasm to vacuole
CC       transport (Cvt) and autophagy vesicles formation. Conjugation with ATG5
CC       through a ubiquitin-like conjugating system involving also ATG7 as an
CC       E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme,
CC       is essential for its function. ATG12/ATG5 conjugate has an essential
CC       role in plant nutrient recycling. {ECO:0000269|PubMed:16040659}.
CC   -!- INTERACTION:
CC       Q9LVK3; Q0WWQ1: ATG3; NbExp=2; IntAct=EBI-8276588, EBI-8276607;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16040659}.
CC   -!- SIMILARITY: Belongs to the ATG12 family. {ECO:0000305}.
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DR   EMBL; AB073185; BAB88397.1; -; mRNA.
DR   EMBL; AB019229; BAB02327.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75446.1; -; Genomic_DNA.
DR   EMBL; BT024653; ABD57478.1; -; mRNA.
DR   EMBL; AK118997; BAC43573.1; -; mRNA.
DR   RefSeq; NP_188013.2; NM_112251.4.
DR   PDB; 1WZ3; X-ray; 1.80 A; A/B=1-94.
DR   PDB; 7EU4; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-94.
DR   PDBsum; 1WZ3; -.
DR   PDBsum; 7EU4; -.
DR   AlphaFoldDB; Q9LVK3; -.
DR   SMR; Q9LVK3; -.
DR   BioGRID; 5945; 1.
DR   IntAct; Q9LVK3; 1.
DR   MINT; Q9LVK3; -.
DR   STRING; 3702.AT3G13970.1; -.
DR   PaxDb; Q9LVK3; -.
DR   PRIDE; Q9LVK3; -.
DR   EnsemblPlants; AT3G13970.1; AT3G13970.1; AT3G13970.
DR   GeneID; 820611; -.
DR   Gramene; AT3G13970.1; AT3G13970.1; AT3G13970.
DR   KEGG; ath:AT3G13970; -.
DR   Araport; AT3G13970; -.
DR   TAIR; locus:2088182; AT3G13970.
DR   eggNOG; KOG3439; Eukaryota.
DR   HOGENOM; CLU_106795_3_1_1; -.
DR   InParanoid; Q9LVK3; -.
DR   OMA; HADNKES; -.
DR   OrthoDB; 1525971at2759; -.
DR   PhylomeDB; Q9LVK3; -.
DR   EvolutionaryTrace; Q9LVK3; -.
DR   PRO; PR:Q9LVK3; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LVK3; baseline and differential.
DR   GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IBA:GO_Central.
DR   GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0006914; P:autophagy; IGI:TAIR.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR   GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007242; Atg12.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR13385; PTHR13385; 1.
DR   Pfam; PF04110; APG12; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Autophagy; Cytoplasm; Isopeptide bond;
KW   Protein transport; Reference proteome; Transport; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q8S924"
FT   CHAIN           2..94
FT                   /note="Ubiquitin-like protein ATG12B"
FT                   /id="PRO_0000250543"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8S924"
FT   CROSSLNK        94
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-128 in ATG5)"
FT                   /evidence="ECO:0000250"
FT   STRAND          2..5
FT                   /evidence="ECO:0007829|PDB:7EU4"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:7EU4"
FT   STRAND          11..18
FT                   /evidence="ECO:0007829|PDB:1WZ3"
FT   STRAND          29..33
FT                   /evidence="ECO:0007829|PDB:1WZ3"
FT   HELIX           39..49
FT                   /evidence="ECO:0007829|PDB:1WZ3"
FT   STRAND          55..62
FT                   /evidence="ECO:0007829|PDB:1WZ3"
FT   HELIX           70..77
FT                   /evidence="ECO:0007829|PDB:1WZ3"
FT   STRAND          82..89
FT                   /evidence="ECO:0007829|PDB:1WZ3"
SQ   SEQUENCE   94 AA;  10358 MW;  5BA77795F9C89D6A CRC64;
     MATESPNSVQ KIVVHLRATG GAPILKQSKF KVSGSDKFAN VIDFLRRQLH SDSLFVYVNS
     AFSPNPDESV IDLYNNFGFD GKLVVNYACS MAWG
 
 
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