CTPA1_ARATH
ID CTPA1_ARATH Reviewed; 489 AA.
AC F4KHG6; Q8W484; Q9FL23;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Carboxyl-terminal-processing peptidase 1, chloroplastic;
DE EC=3.4.21.102;
DE AltName: Full=D1 C-terminal processing protease 1;
DE AltName: Full=Photosystem II D1 protein processing peptidase 1;
DE Flags: Precursor;
GN Name=CTPA1; OrderedLocusNames=At5g46390; ORFNames=MPL12.19;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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] (ISOFORM 2).
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 PROTEIN SEQUENCE OF 68-75, AND SUBCELLULAR LOCATION.
RX PubMed=11719511; DOI=10.1074/jbc.m108575200;
RA Schubert M., Petersson U.A., Haas B.J., Funk C., Schroeder W.P.,
RA Kieselbach T.;
RT "Proteome map of the chloroplast lumen of Arabidopsis thaliana.";
RL J. Biol. Chem. 277:8354-8365(2002).
RN [5]
RP REVIEW.
RX PubMed=16895613; DOI=10.1186/1471-2164-7-200;
RA Tripathi L.P., Sowdhamini R.;
RT "Cross genome comparisons of serine proteases in Arabidopsis and rice.";
RL BMC Genomics 7:200-200(2006).
CC -!- FUNCTION: Protease involved in the C-terminal processing of the
CC chloroplastic D1 protein of photosystem II. This proteolytic processing
CC is necessary to allow the light-driven assembly of the tetranuclear
CC manganese cluster, which is responsible for photosynthetic water
CC oxidation. {ECO:0000250|UniProtKB:O04073}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The enzyme shows specific recognition of a C-terminal
CC tripeptide, Xaa-Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa
CC is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves
CC at a variable distance from the C-terminus. A typical cleavage is
CC -Ala-Ala-|-Arg-Ala-Ala-Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala.;
CC EC=3.4.21.102;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen
CC {ECO:0000269|PubMed:11719511}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4KHG6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4KHG6-2; Sequence=VSP_054870, VSP_054871;
CC -!- SIMILARITY: Belongs to the peptidase S41A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11094.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB010698; BAB11094.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95377.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95378.1; -; Genomic_DNA.
DR EMBL; AY062767; AAL32845.1; -; mRNA.
DR EMBL; AY081650; AAM10212.1; -; mRNA.
DR RefSeq; NP_199451.2; NM_124009.2. [F4KHG6-2]
DR RefSeq; NP_974893.1; NM_203164.3. [F4KHG6-1]
DR AlphaFoldDB; F4KHG6; -.
DR SMR; F4KHG6; -.
DR IntAct; F4KHG6; 1.
DR STRING; 3702.AT5G46390.2; -.
DR MEROPS; S41.A02; -.
DR PaxDb; F4KHG6; -.
DR PRIDE; F4KHG6; -.
DR ProteomicsDB; 220454; -. [F4KHG6-1]
DR EnsemblPlants; AT5G46390.1; AT5G46390.1; AT5G46390. [F4KHG6-2]
DR EnsemblPlants; AT5G46390.2; AT5G46390.2; AT5G46390. [F4KHG6-1]
DR GeneID; 834682; -.
DR Gramene; AT5G46390.1; AT5G46390.1; AT5G46390. [F4KHG6-2]
DR Gramene; AT5G46390.2; AT5G46390.2; AT5G46390. [F4KHG6-1]
DR KEGG; ath:AT5G46390; -.
DR Araport; AT5G46390; -.
DR TAIR; locus:2170443; AT5G46390.
DR eggNOG; ENOG502QT7D; Eukaryota.
DR HOGENOM; CLU_017295_0_1_1; -.
DR InParanoid; F4KHG6; -.
DR OMA; TFNQVDW; -.
DR OrthoDB; 1370241at2759; -.
DR PRO; PR:F4KHG6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KHG6; baseline and differential.
DR Genevisible; F4KHG6; AT.
DR GO; GO:0009543; C:chloroplast thylakoid lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0031977; C:thylakoid lumen; HDA:TAIR.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00225; prc; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Direct protein sequencing; Hydrolase;
KW Plastid; Protease; Reference proteome; Serine protease; Thylakoid;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT TRANSIT ?..67
FT /note="Thylakoid"
FT /evidence="ECO:0000269|PubMed:11719511"
FT CHAIN 68..489
FT /note="Carboxyl-terminal-processing peptidase 1,
FT chloroplastic"
FT /id="PRO_0000429321"
FT DOMAIN 189..273
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 403
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 428
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT VAR_SEQ 396..428
FT /note="MVNNRTASASEIVASALHDNCKAVLVGERTYGK -> CDESCKPVNLSHYYV
FT ILHLALIRILIIVAGNGK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_054870"
FT VAR_SEQ 429..489
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_054871"
SQ SEQUENCE 489 AA; 53033 MW; E421EF7DE41FBAB8 CRC64;
MRLLLPFSSP LSATSSPSTP QFIPELPPPS QFDYSGLTKI LKKSVIGTLT GALSLTLVFS
SPISSVAATN DPYLSVNPPS SSFESSLNHF DSAPEDCPNE EEADTEIQDD DIEPQLVTNE
GIVEEAWEIV NGAFLDTRSH SWTPETWQKQ KDDILASPIK SRSKAHEVIK NMLASLGDQY
TRFLSPDEFS RMSKYDITGI GINLREVSDG GGNVKLKVLG LVLDSAADIA GVKQGDEILA
VNGMDVSGKS SFEVSSLLQG PSKTFVVLKV KHGKCGPVKS LKIQRQVNAQ TPVSYRLEKV
DNGTVSVGYI RLKEFNALAR KDLVIAMKRL LDKGASYFVM DLRDNLGGLV QAGIETAKLF
LDEGDTVIYT AGRDPEAQKT VVSDKKPLIT APLIVMVNNR TASASEIVAS ALHDNCKAVL
VGERTYGKGL IQSVYELRDG SGVVVTIGKY VTPNHMDING GGIEPDFRNL PAWDEVKERL
SKCSILQQS
