PTC52_ARATH
ID PTC52_ARATH Reviewed; 559 AA.
AC Q8W496; Q93WJ7; Q9SZZ3;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Protochlorophyllide-dependent translocon component 52, chloroplastic;
DE AltName: Full=ACD1-like protein;
DE AltName: Full=Protein TIC 55-IV;
DE AltName: Full=Translocon at the inner envelope membrane of chloroplasts 55-IV;
DE Flags: Precursor;
GN Name=PTC52; Synonyms=ACD1-like, TIC55-IV; OrderedLocusNames=At4g25650;
GN ORFNames=L73G19.30;
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] (ISOFORM 2).
RX PubMed=12481072; DOI=10.1104/pp.008441;
RA Gray J., Janick-Buckner D., Buckner B., Close P.S., Johal G.S.;
RT "Light-dependent death of maize lls1 cells is mediated by mature
RT chloroplasts.";
RL Plant Physiol. 130:1894-1907(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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] (ISOFORMS 1 AND 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 [5]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=18349143; DOI=10.1073/pnas.0800378105;
RA Bartsch S., Monnet J., Selbach K., Quigley F., Gray J., von Wettstein D.,
RA Reinbothe S., Reinbothe C.;
RT "Three thioredoxin targets in the inner envelope membrane of chloroplasts
RT function in protein import and chlorophyll metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:4933-4938(2008).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=19995737; DOI=10.1093/mp/ssp079;
RA Boij P., Patel R., Garcia C., Jarvis P., Aronsson H.;
RT "In vivo studies on the roles of Tic55-related proteins in chloroplast
RT protein import in Arabidopsis thaliana.";
RL Mol. Plant 2:1397-1409(2009).
CC -!- FUNCTION: Part of a translocon most abundantly expressed in etiolated
CC plants and involved in the protochlorophyllide-dependent import of the
CC precursor NADPH:protochlorophyllide oxidoreductase A (pPORA).
CC {ECO:0000269|PubMed:18349143}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00628};
CC -!- ACTIVITY REGULATION: Down-regulated by light.
CC {ECO:0000269|PubMed:18349143}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8W496-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8W496-2; Sequence=VSP_041956;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:19995737}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43696.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81375.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY344062; AAR05798.1; -; mRNA.
DR EMBL; AL050400; CAB43696.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161563; CAB81375.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85088.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85089.1; -; Genomic_DNA.
DR EMBL; AF424575; AAL11569.1; -; mRNA.
DR EMBL; AY056168; AAL07017.1; -; mRNA.
DR EMBL; AY062731; AAL32809.1; -; mRNA.
DR EMBL; BT002586; AAO00946.1; -; mRNA.
DR PIR; T09557; T09557.
DR RefSeq; NP_567725.1; NM_118697.4. [Q8W496-2]
DR RefSeq; NP_849444.1; NM_179113.2. [Q8W496-1]
DR AlphaFoldDB; Q8W496; -.
DR SMR; Q8W496; -.
DR STRING; 3702.AT4G25650.2; -.
DR iPTMnet; Q8W496; -.
DR PaxDb; Q8W496; -.
DR PRIDE; Q8W496; -.
DR ProMEX; Q8W496; -.
DR ProteomicsDB; 226043; -. [Q8W496-1]
DR EnsemblPlants; AT4G25650.1; AT4G25650.1; AT4G25650. [Q8W496-2]
DR EnsemblPlants; AT4G25650.2; AT4G25650.2; AT4G25650. [Q8W496-1]
DR GeneID; 828670; -.
DR Gramene; AT4G25650.1; AT4G25650.1; AT4G25650. [Q8W496-2]
DR Gramene; AT4G25650.2; AT4G25650.2; AT4G25650. [Q8W496-1]
DR KEGG; ath:AT4G25650; -.
DR Araport; AT4G25650; -.
DR TAIR; locus:2131406; AT4G25650.
DR eggNOG; ENOG502QR6Q; Eukaryota.
DR InParanoid; Q8W496; -.
DR OMA; EPPCRLE; -.
DR OrthoDB; 1199207at2759; -.
DR PhylomeDB; Q8W496; -.
DR BioCyc; ARA:AT4G25650-MON; -.
DR PRO; PR:Q8W496; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W496; baseline and differential.
DR Genevisible; Q8W496; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010277; F:chlorophyllide a oxygenase [overall] activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR013626; PaO.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR Pfam; PF08417; PaO; 1.
DR Pfam; PF00355; Rieske; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Alternative splicing; Chloroplast; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Plastid; Plastid inner membrane; Protein transport;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Transport.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 56..559
FT /note="Protochlorophyllide-dependent translocon component
FT 52, chloroplastic"
FT /id="PRO_0000413679"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 85..195
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 44..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 483..486
FT /note="Redox-active motif"
FT COMPBIAS 44..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 129
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 147
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 150
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 248
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT BINDING 253
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255"
FT VAR_SEQ 264..286
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12481072,
FT ECO:0000303|PubMed:14593172"
FT /id="VSP_041956"
SQ SEQUENCE 559 AA; 63819 MW; EC51FA19EBF344E4 CRC64;
MEAALAACAL PSLRILNTKP RFRCSFSNPS LPISPNSLIT RKSSRFTTAV SSPPSSSAAT
STNSPPEPEA LFEPGSDKFD WYANWYPVMP ICDLDKKVPH GKKVMGIDLV VWWDRNEKQW
KVMDDTCPHR LAPLSDGRID QWGRLQCVYH GWCFNGSGDC KLIPQAPPDG PPVHTFKQAC
VAVYPSTVQH EIIWFWPNSD PKYKNIIETN KPPYIPELED PSFTKLMGNR DIPYGYDVLV
ENLMDPAHVP YAHYGLMRFP KPKGKYIICI SNSCFNPFTN LQILLAEKID REGGKPLEIN
VKKLDNKGFF SKQEWGYSNF IAPCVYRSST DPLPEQEHEY PAPAASDKAA LSKRRLSLIF
ICIPVSPGRS RLIWTFPRNF GVFIDKIVPR WVFHIGQNTI LDSDLHLLHV EERKILERGP
ENWQKACFIP TKSDANVVTF RRWFNKYSEA RVDWRGKFDP FLLPPTPPRE QLFDRYWSHV
ENCSSCKKAH KYLNALEVIL QIASVAMIGV MAVLKQTTMS NVARIAVLVA AVLSFAASKW
LSHFIYKTFH YHDYNHAVV
