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ATG4B_ORYSI
ID   ATG4B_ORYSI             Reviewed;         478 AA.
AC   Q2XPP4; A2XZ28;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Cysteine protease ATG4B {ECO:0000305};
DE            EC=3.4.22.- {ECO:0000250|UniProtKB:Q9Y4P1};
DE   AltName: Full=Autophagy-related protein 4 homolog B;
DE            Short=OsAtg4 {ECO:0000303|PubMed:17082902};
DE            Short=Protein autophagy 4 {ECO:0000303|PubMed:17082902};
GN   Name=ATG4B; Synonyms=APG4, APG4B; ORFNames=OsI_017321;
OS   Oryza sativa subsp. indica (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=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP   WITH ATG8.
RX   PubMed=17082902; DOI=10.1007/s11033-006-9011-0;
RA   Su W., Ma H., Liu C., Wu J., Yang J.;
RT   "Identification and characterization of two rice autophagy associated
RT   genes, OsAtg8 and OsAtg4.";
RL   Mol. Biol. Rep. 33:273-278(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
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).
CC   -!- FUNCTION: Cysteine protease that plays a key role in autophagy by
CC       mediating both proteolytic activation and delipidation of ATG8 family
CC       proteins (PubMed:17082902). The protease activity is required for
CC       proteolytic activation of ATG8 family proteins: cleaves the C-terminal
CC       amino acid of ATG8 proteins to reveal a C-terminal glycine
CC       (PubMed:17082902). Exposure of the glycine at the C-terminus is
CC       essential for ATG8 proteins conjugation to phosphatidylethanolamine
CC       (PE) and insertion to membranes, which is necessary for autophagy (By
CC       similarity). In addition to the protease activity, also mediates
CC       delipidation of PE-conjugated ATG8 proteins (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y4P1, ECO:0000269|PubMed:17082902}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-C-terminal L-amino acid-glycyl-
CC         phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-
CC         glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine;
CC         Xref=Rhea:RHEA:67548, Rhea:RHEA-COMP:17323, Rhea:RHEA-COMP:17324,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:64612, ChEBI:CHEBI:172940,
CC         ChEBI:CHEBI:172941; Evidence={ECO:0000250|UniProtKB:Q9Y4P1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67549;
CC         Evidence={ECO:0000250|UniProtKB:Q9Y4P1};
CC   -!- SUBUNIT: Interacts with ATG8. {ECO:0000269|PubMed:17082902}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BGE6}.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed.
CC       {ECO:0000269|PubMed:17082902}.
CC   -!- SIMILARITY: Belongs to the peptidase C54 family. {ECO:0000305}.
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DR   EMBL; DQ269984; ABB77259.1; -; mRNA.
DR   EMBL; CM000129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q2XPP4; -.
DR   SMR; Q2XPP4; -.
DR   STRING; 39946.Q2XPP4; -.
DR   Proteomes; UP000007015; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR005078; Peptidase_C54.
DR   PANTHER; PTHR22624; PTHR22624; 1.
DR   Pfam; PF03416; Peptidase_C54; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Cytoplasm; Hydrolase; Protease; Protein transport;
KW   Reference proteome; Thiol protease; Transport; Ubl conjugation pathway.
FT   CHAIN           1..478
FT                   /note="Cysteine protease ATG4B"
FT                   /id="PRO_0000286903"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        164
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT   ACT_SITE        361
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P1"
FT   CONFLICT        78
FT                   /note="L -> S (in Ref. 1; ABB77259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190
FT                   /note="S -> L (in Ref. 1; ABB77259)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   478 AA;  52526 MW;  A2C7D847C12223E2 CRC64;
     MTSLPDRGVS SSSSDPLCEG NIAPCSSSSE QKEDCSLKQS KTSILSCVFN SPFNIFEAHQ
     DSSANKSPKS SSGSYDWLRV LRRIVCSGSM WRFLGTSKVL TSSDVWFLGK CYKLSSEESS
     SDSDSESGHA TFLEDFSSRI WITYRRGFDA ISDSKYTSDV NWGCMVRSSQ MLVAQALIFH
     HLGRSWRRPS EKPYNPEYIG ILHMFGDSEA CAFSIHNLLQ AGNSYGLAAG SWVGPYAMCR
     AWQTLVRTNR EQHEVVDGNE SFPMALYVVS GDEDGERGGA PVVCIDVAAQ LCCDFNKGQS
     TWSPILLLVP LVLGLDKINP RYIPLLKETF TFPQSLGILG GKPGTSTYIA GVQDDRALYL
     DPHEVQMAVD IAADNIEADT SSYHCSTVRD LALDLIDPSL AIGFYCRDKD DFDDFCSRAT
     ELVDKANGAP LFTVVQSVQP SKQMYNQDDV LGISGDGNIN VEDLDASGET GEEEWQIL
 
 
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