CRP1_MAIZE
ID CRP1_MAIZE Reviewed; 668 AA.
AC A0A1D6IEG9; O81397;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Pentatricopeptide repeat-containing protein CRP1, chloroplastic {ECO:0000305};
DE AltName: Full=Protein CHLOROPLAST RNA PROCESSING 1 {ECO:0000303|PubMed:8039510};
DE Flags: Precursor;
GN Name=CRP1 {ECO:0000303|PubMed:8039510};
GN ORFNames=ZEAMMB73_Zm00001d021716 {ECO:0000312|EMBL:ONM58112.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10228173; DOI=10.1093/emboj/18.9.2621;
RA Fisk D.G., Walker M.B., Barkan A.;
RT "Molecular cloning of the maize gene crp1 reveals similarity between
RT regulators of mitochondrial and chloroplast gene expression.";
RL EMBO J. 18:2621-2630(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8039510; DOI=10.1002/j.1460-2075.1994.tb06616.x;
RA Barkan A., Walker M., Nolasco M., Johnson D.;
RT "A nuclear mutation in maize blocks the processing and translation of
RT several chloroplast mRNAs and provides evidence for the differential
RT translation of alternative mRNA forms.";
RL EMBO J. 13:3170-3181(1994).
RN [4]
RP FUNCTION.
RX PubMed=16141451; DOI=10.1105/tpc.105.034454;
RA Schmitz-Linneweber C., Williams-Carrier R., Barkan A.;
RT "RNA immunoprecipitation and microarray analysis show a chloroplast
RT pentatricopeptide repeat protein to be associated with the 5' region of
RT mRNAs whose translation it activates.";
RL Plant Cell 17:2791-2804(2005).
RN [5]
RP FUNCTION.
RX PubMed=18669444; DOI=10.1261/rna.1077708;
RA Williams-Carrier R., Kroeger T., Barkan A.;
RT "Sequence-specific binding of a chloroplast pentatricopeptide repeat
RT protein to its native group II intron ligand.";
RL RNA 14:1930-1941(2008).
RN [6]
RP FUNCTION.
RX PubMed=23735295; DOI=10.1105/tpc.113.111567;
RA Zoschke R., Watkins K.P., Barkan A.;
RT "A rapid ribosome profiling method elucidates chloroplast ribosome behavior
RT in vivo.";
RL Plant Cell 25:2265-2275(2013).
CC -!- FUNCTION: Required for the translation of the chloroplast petA and petD
CC mRNAs. Required for the processing of the petD mRNA from a
CC polycistronic precursor (PubMed:8039510). Binds with high affinity to
CC the 5'-UTR of the chloroplastic petA transcript (PubMed:18669444).
CC Activates psaC and petA translation by binding their 5'-UTRs
CC (PubMed:16141451, PubMed:23735295). {ECO:0000269|PubMed:16141451,
CC ECO:0000269|PubMed:18669444, ECO:0000269|PubMed:23735295,
CC ECO:0000269|PubMed:8039510}.
CC -!- SUBUNIT: Component of a multisubunit complex.
CC {ECO:0000269|PubMed:10228173}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:10228173}.
CC -!- DISRUPTION PHENOTYPE: Pale green leaf phenotype. Seedling lethality.
CC {ECO:0000269|PubMed:8039510}.
CC -!- SIMILARITY: Belongs to the PPR family. P subfamily. {ECO:0000305}.
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DR EMBL; AF073522; AAC25599.1; -; mRNA.
DR EMBL; CM007650; ONM58112.1; -; Genomic_DNA.
DR PIR; T01685; T01685.
DR RefSeq; NP_001105879.1; NM_001112409.2.
DR AlphaFoldDB; A0A1D6IEG9; -.
DR SMR; A0A1D6IEG9; -.
DR STRING; 4577.GRMZM2G083950_P01; -.
DR EnsemblPlants; Zm00001eb323580_T001; Zm00001eb323580_P001; Zm00001eb323580.
DR EnsemblPlants; Zm00001eb323580_T003; Zm00001eb323580_P003; Zm00001eb323580.
DR GeneID; 732792; -.
DR Gramene; Zm00001eb323580_T001; Zm00001eb323580_P001; Zm00001eb323580.
DR Gramene; Zm00001eb323580_T003; Zm00001eb323580_P003; Zm00001eb323580.
DR KEGG; zma:732792; -.
DR eggNOG; KOG4197; Eukaryota.
DR OMA; HCKAGRH; -.
DR OrthoDB; 1344243at2759; -.
DR Proteomes; UP000007305; Chromosome 7.
DR ExpressionAtlas; A0A1D6IEG9; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0042644; C:chloroplast nucleoid; IEA:EnsemblPlants.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0042651; C:thylakoid membrane; IEA:EnsemblPlants.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:EnsemblPlants.
DR GO; GO:0010239; P:chloroplast mRNA processing; IEA:EnsemblPlants.
DR GO; GO:0009658; P:chloroplast organization; IEA:EnsemblPlants.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR Gene3D; 1.25.40.10; -; 5.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR033443; PPR_long.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF01535; PPR; 2.
DR Pfam; PF13041; PPR_2; 2.
DR Pfam; PF13812; PPR_3; 1.
DR Pfam; PF17177; PPR_long; 1.
DR TIGRFAMs; TIGR00756; PPR; 10.
DR PROSITE; PS51375; PPR; 14.
PE 1: Evidence at protein level;
KW Chloroplast; mRNA processing; Plastid; Reference proteome; Repeat;
KW RNA-binding; Transit peptide; Translation regulation.
FT TRANSIT 1..64
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 65..668
FT /note="Pentatricopeptide repeat-containing protein CRP1,
FT chloroplastic"
FT /id="PRO_0000441906"
FT REPEAT 154..188
FT /note="PPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 189..226
FT /note="PPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 227..261
FT /note="PPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 262..297
FT /note="PPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 298..332
FT /note="PPR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 333..367
FT /note="PPR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 368..402
FT /note="PPR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 403..437
FT /note="PPR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 438..472
FT /note="PPR 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 473..507
FT /note="PPR 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 508..542
FT /note="PPR 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 543..577
FT /note="PPR 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 578..612
FT /note="PPR 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT REPEAT 613..647
FT /note="PPR 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00708"
FT CONFLICT 98
FT /note="A -> V (in Ref. 1; AAC25599)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="A -> G (in Ref. 1; AAC25599)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 668 AA; 73223 MW; 03967CE801134282 CRC64;
MPASLLPPTF LPHHLRRLAP AGCTTSSVTS SSVSIPASRY DFEPLLAYLS SPSVSASLTS
PSPPASVPAP EHRLAASYSA VPSHEWHALL RDLAASDASL PLAFALLPFL HRHRLCFPLD
LLLSSLLHSL SVSGRLLPHS LLLSFPPSLS DPPSPLLLNS LLAASAAASR PAVALRLLSL
LREHDFLPDL ASYSHLLASL LNTRDPPDAA LLERLLGDLR ESRLEPDAPL FSDLISAFAR
AALPDAALEL LASAQAIGLT PRSNAVTALI SALGTAGRVA EAEALFLEFF LAGEIKPRTR
AYNALLKGYV RIASLKNAEQ VLDEMSQCGV APDEATYSLL VDAYTRAGRW ESARILLKEM
EADGVKPSSY VFSRILAGFR DRGDWQKAFA VLREMQASGV RPDRHFYNVM IDTFGKYNCL
GHAMDAFNKM REEGIEPDVV TWNTLIDAHC KGGRHDRAAE LFEEMRESNC PPGTTTYNIM
INLLGEQEHW EGVEAMLSEM KEQGLVPNII TYTTLVDVYG RSGRYKEAID CIEAMKADGL
KPSPTMYHAL VNAYAQRGLA DHALNVVKAM KADGLEVSIL VLNSLINAFG EDRRVVEAFS
VLQFMRENGL RPDVITYTTL MKALIRVEQF DKVPVIYEEM ITSGCAPDRK ARAMLRSGLK
YIKHMRVA
