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TPP1_ARATH
ID   TPP1_ARATH              Reviewed;         340 AA.
AC   O04348; Q7DM64;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Thylakoidal processing peptidase 1, chloroplastic;
DE            EC=3.4.21.89;
DE   AltName: Full=Signal peptidase I-1;
DE   Flags: Precursor;
GN   Name=TPP1; OrderedLocusNames=At2g30440; ORFNames=T6B20.20;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=9422718; DOI=10.1074/jbc.273.2.689;
RA   Chaal B.K., Mould R.M., Barbrook A.C., Gray J.C., Howe C.J.;
RT   "Characterization of a cDNA encoding the thylakoidal processing peptidase
RT   from Arabidopsis thaliana. Implications for the origin and catalytic
RT   mechanism of the enzyme.";
RL   J. Biol. Chem. 273:689-692(1998).
RN   [2]
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   [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;
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   [5]
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 (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves the thylakoid-transfer domain from a chloroplast
CC       protein. {ECO:0000269|PubMed:9422718}.
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 thylakoid membrane
CC       {ECO:0000269|PubMed:9422718}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:9422718}. Note=located in the non-appressed
CC       lamellae of the thylakoid network. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB63091.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; Y10477; CAA71502.1; -; mRNA.
DR   EMBL; U93215; AAB63091.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC08389.1; -; Genomic_DNA.
DR   EMBL; AY128354; AAM91557.1; -; mRNA.
DR   EMBL; BT020607; AAW80880.1; -; mRNA.
DR   PIR; E84708; E84708.
DR   RefSeq; NP_180603.2; NM_128597.3.
DR   AlphaFoldDB; O04348; -.
DR   SMR; O04348; -.
DR   STRING; 3702.AT2G30440.1; -.
DR   MEROPS; S26.008; -.
DR   PaxDb; O04348; -.
DR   PRIDE; O04348; -.
DR   EnsemblPlants; AT2G30440.1; AT2G30440.1; AT2G30440.
DR   GeneID; 817595; -.
DR   Gramene; AT2G30440.1; AT2G30440.1; AT2G30440.
DR   KEGG; ath:AT2G30440; -.
DR   Araport; AT2G30440; -.
DR   TAIR; locus:2064337; AT2G30440.
DR   eggNOG; KOG0171; Eukaryota.
DR   HOGENOM; CLU_025235_0_0_1; -.
DR   InParanoid; O04348; -.
DR   OMA; PMFVPKG; -.
DR   OrthoDB; 1211147at2759; -.
DR   PhylomeDB; O04348; -.
DR   PRO; PR:O04348; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O04348; baseline and differential.
DR   Genevisible; O04348; AT.
DR   GO; GO:0009534; C:chloroplast thylakoid; IDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:TAIR.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006465; P:signal peptide processing; IDA:TAIR.
DR   GO; GO:0010027; P:thylakoid membrane organization; IBA:GO_Central.
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; Transmembrane; Transmembrane helix.
FT   TRANSIT         1..52
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   TRANSIT         53..?
FT                   /note="Thylakoid"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..340
FT                   /note="Thylakoidal processing peptidase 1, chloroplastic"
FT                   /id="PRO_0000310734"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..340
FT                   /note="Lumenal, thylakoid"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        184
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   340 AA;  37853 MW;  F6763EBFC1DAA2E1 CRC64;
     MAIRITFTYS THVARNLVGT RVGPGGYCFE SLVRPRFFSH KRDFDRSPRN RPASMYGSIA
     RELIGEGSQS PLVMGLISIL KSTTGHESST MNVLGVSSFK ASSIIPFLQG SKWIKNPPVI
     DDVDKGGTVC DDDDDKESRN GGSGWVNKLL SVCSEDAKAA FTAVTVSILF RSALAEPKSI
     PSTSMYPTLD KGDRVMAEKV SYFFRKPEVS DIVIFKAPPI LLEYPEYGYS SNDVFIKRIV
     ASEGDWVEVR DGKLFVNDIV QEEDFVLEPM SYEMEPMFVP KGYVFVLGDN RNKSFDSHNW
     GPLPIENIVG RSVFRYWPPS KVSDTIYHDQ AITRGPVAVS
 
 
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