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PLP1_ORYSI
ID   PLP1_ORYSI              Reviewed;         414 AA.
AC   B8AQW7;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Patatin-like protein 1;
DE            EC=3.1.1.-;
GN   Name=PLP1; ORFNames=OsI_11898;
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 [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: Possesses non-specific lipolytic acyl hydrolase (LAH)
CC       activity. Hydrolyzes phospholipids as well as galactolipids. May play a
CC       role in disease resistance (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The nitrogen atoms of the two glycine residues in the GGXR
CC       motif define the oxyanion hole, and stabilize the oxyanion that forms
CC       during the nucleophilic attack by the catalytic serine during substrate
CC       cleavage. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the patatin family. {ECO:0000305}.
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DR   EMBL; CM000128; EEC75405.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8AQW7; -.
DR   SMR; B8AQW7; -.
DR   STRING; 39946.B8AQW7; -.
DR   EnsemblPlants; BGIOSGA012798-TA; BGIOSGA012798-PA; BGIOSGA012798.
DR   Gramene; BGIOSGA012798-TA; BGIOSGA012798-PA; BGIOSGA012798.
DR   HOGENOM; CLU_000288_144_0_1; -.
DR   OMA; FPQKRCG; -.
DR   Proteomes; UP000007015; Chromosome 3.
DR   GO; GO:0016298; F:lipase activity; IEA:UniProt.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Lipid degradation; Lipid metabolism; Plant defense;
KW   Reference proteome.
FT   CHAIN           1..414
FT                   /note="Patatin-like protein 1"
FT                   /id="PRO_0000425825"
FT   DOMAIN          20..224
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           24..29
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           62..66
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           211..213
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        64
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        211
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ   SEQUENCE   414 AA;  44508 MW;  FC886600CD0445FB CRC64;
     MAGCVVGEPA SAPGQRVTLL AIDGGGIRGL IPGTILAFLE ARLQELDGPD ARLADYFDCI
     AGTSTGGLIT AMLAAPGDHG RPLFAASDIN RFYLDNGPRI FPQKRCGMAA AMAALTRPRY
     NGKYLQGKIR KMLGETRVRD TLTNVVIPTF DVRLLQPTIF STYDAKSMPL KNALLSDICI
     STSAAPTYLP AHCFQTTDDA TGKVREFDLI DGGVAANNPT MVAMTQITKK IMVKDKEELY
     PVKPSDCGKF LVLSLGTGST SDQGMYTARQ CSRWGIVRWL RNKGMAPIID IFMAASSDLV
     DIHAAVMFQS LHSDGDYLRI QDNTLHGDAA TVDAATRDNM RALVGIGERM LAQRVSRVNV
     ETGRYVEVPG AGSNADALRG FARQLSEERR ARLGRRNACG GGGEGEPSGV ACKR
 
 
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