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PLSP1_ARATH
ID   PLSP1_ARATH             Reviewed;         291 AA.
AC   Q8H0W1; Q66GJ6; Q9LV44;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Chloroplast processing peptidase;
DE            EC=3.4.21.89;
DE   AltName: Full=Signal peptidase I-3;
DE   Flags: Precursor;
GN   Name=PLSP1; OrderedLocusNames=At3g24590; ORFNames=MOB24.17;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16275749; DOI=10.1083/jcb.200506171;
RA   Inoue K., Baldwin A.J., Shipman R.L., Matsui K., Theg S.M., Ohme-Takagi M.;
RT   "Complete maturation of the plastid protein translocation channel requires
RT   a type I signal peptidase.";
RL   J. Cell Biol. 171:425-430(2005).
CC   -!- FUNCTION: Involved in the maturation of the plastid protein
CC       translocation channel. Required for the biogenesis of plastid internal
CC       membranes. May also function as a thylakoidal processing peptidase.
CC       {ECO:0000269|PubMed:16275749}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC         from secreted and periplasmic proteins.; EC=3.4.21.89;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast envelope
CC       {ECO:0000269|PubMed:16275749}. Plastid, chloroplast thylakoid membrane
CC       {ECO:0000269|PubMed:16275749}. Note=May be located at the envelope
CC       membranes in premature chloroplast and at the thylakoidal membrane in
CC       mature chloroplasts.
CC   -!- DISRUPTION PHENOTYPE: Plants are albino and seedling lethal.
CC       {ECO:0000269|PubMed:16275749}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB02011.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB020746; BAB02011.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002686; AEE76927.1; -; Genomic_DNA.
DR   EMBL; BT002007; AAN72018.1; -; mRNA.
DR   EMBL; BT015406; AAU05529.1; -; mRNA.
DR   RefSeq; NP_001319633.1; NM_001338695.1.
DR   RefSeq; NP_189102.3; NM_113370.3.
DR   AlphaFoldDB; Q8H0W1; -.
DR   SMR; Q8H0W1; -.
DR   STRING; 3702.AT3G24590.1; -.
DR   MEROPS; S26.A02; -.
DR   PaxDb; Q8H0W1; -.
DR   PRIDE; Q8H0W1; -.
DR   ProteomicsDB; 234732; -.
DR   EnsemblPlants; AT3G24590.1; AT3G24590.1; AT3G24590.
DR   GeneID; 822055; -.
DR   Gramene; AT3G24590.1; AT3G24590.1; AT3G24590.
DR   KEGG; ath:AT3G24590; -.
DR   Araport; AT3G24590; -.
DR   TAIR; locus:2091717; AT3G24590.
DR   eggNOG; KOG0171; Eukaryota.
DR   HOGENOM; CLU_028723_2_1_1; -.
DR   InParanoid; Q8H0W1; -.
DR   OMA; LPEWLNI; -.
DR   OrthoDB; 1211147at2759; -.
DR   PhylomeDB; Q8H0W1; -.
DR   BRENDA; 3.4.21.89; 399.
DR   PRO; PR:Q8H0W1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8H0W1; baseline and differential.
DR   Genevisible; Q8H0W1; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0009526; C:plastid envelope; IDA:TAIR.
DR   GO; GO:0055035; C:plastid thylakoid membrane; IDA:TAIR.
DR   GO; GO:0008233; F:peptidase activity; IDA:TAIR.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0051604; P:protein maturation; IMP:TAIR.
DR   GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR   GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   PANTHER; PTHR43390; PTHR43390; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; SSF51306; 1.
DR   TIGRFAMs; TIGR02227; sigpep_I_bact; 1.
DR   PROSITE; PS00501; SPASE_I_1; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Hydrolase; Membrane; Plastid; Protease; Reference proteome;
KW   Thylakoid; Transit peptide.
FT   TRANSIT         1..67
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           68..291
FT                   /note="Chloroplast processing peptidase"
FT                   /id="PRO_0000310736"
FT   REGION          69..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000250"
FT   CONFLICT        209
FT                   /note="L -> Q (in Ref. 3; AAN72018)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   291 AA;  32554 MW;  FB353211D47FC737 CRC64;
     MMVMISLHFS TPPLAFLKSD SNSRFLKNPN PNFIQFTPKS QLLFPQRLNF NTGTNLNRRT
     LSCYGIKDSS ETTKSAPSLD SGDGGGGDGG DDDKGEVEEK NRLFPEWLDF TSDDAQTVFV
     AIAVSLAFRY FIAEPRYIPS LSMYPTFDVG DRLVAEKVSY YFRKPCANDI VIFKSPPVLQ
     EVGYTDADVF IKRIVAKEGD LVEVHNGKLM VNGVARNEKF ILEPPGYEMT PIRVPENSVF
     VMGDNRNNSY DSHVWGPLPL KNIIGRSVFR YWPPNRVSGT VLEGGCAVDK Q
 
 
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