PLAT3_ORYSJ
ID PLAT3_ORYSJ Reviewed; 749 AA.
AC Q852M4; Q0DMV8; Q10C93; Q10C95;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable glutamate carboxypeptidase PLA3 {ECO:0000305};
DE EC=3.4.17.21 {ECO:0000305};
DE AltName: Full=Protein GOLIATH {ECO:0000303|PubMed:19228340};
DE AltName: Full=Protein PLASTOCHRON3 {ECO:0000303|PubMed:19228340};
GN Name=PLA3 {ECO:0000303|PubMed:19228340};
GN Synonyms=GO {ECO:0000303|PubMed:19228340};
GN OrderedLocusNames=Os03g0790600 {ECO:0000312|EMBL:BAS86774.1},
GN LOC_Os03g57660 {ECO:0000312|EMBL:ABF99278.1};
GN ORFNames=OSJNBa0087O09.17 {ECO:0000312|EMBL:AAO24914.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF GLY-387.
RX PubMed=19228340; DOI=10.1111/j.1365-313x.2009.03841.x;
RA Kawakatsu T., Taramino G., Itoh J., Allen J., Sato Y., Hong S.-K., Yule R.,
RA Nagasawa N., Kojima M., Kusaba M., Sakakibara H., Sakai H., Nagato Y.;
RT "PLASTOCHRON3/GOLIATH encodes a glutamate carboxypeptidase required for
RT proper development in rice.";
RL Plant J. 58:1028-1040(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: Involved in the regular timing (plastochron) of lateral
CC organs formation. May regulate the rate of leaf initiation and the
CC duration of vegetative phase. Seems to be redundant to the function of
CC PLASTOCHRON1 and PLASTOCHRON2, but to act in an independent pathway.
CC May be required for the synthesis of small signaling molecules that
CC have a role in regulating meristem function. Involved in plant hormone
CC homeostasis. {ECO:0000269|PubMed:19228340}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an unsubstituted, C-terminal glutamyl residue,
CC typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.;
CC EC=3.4.17.21; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q04609};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q04609};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in developing embryos, roots, leaf blade,
CC vegetative shoot apex, inflorescence apex and flowers.
CC {ECO:0000269|PubMed:19228340}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO24914.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABF99277.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABF99278.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF13430.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAH22722.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAS86774.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB447403; BAH22722.1; ALT_SEQ; mRNA.
DR EMBL; AC087096; AAO24914.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF99277.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF99278.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008209; BAF13430.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014959; BAS86774.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q852M4; -.
DR SMR; Q852M4; -.
DR STRING; 4530.OS03T0790600-01; -.
DR MEROPS; M28.007; -.
DR PRIDE; Q852M4; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_0_1_1; -.
DR InParanoid; Q852M4; -.
DR BRENDA; 3.4.17.11; 4460.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404; PTHR10404; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Cell membrane; Developmental protein; Glycoprotein;
KW Growth regulation; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..749
FT /note="Probable glutamate carboxypeptidase PLA3"
FT /id="PRO_0000439195"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 47..67
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..749
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT REGION 278..574
FT /note="Catalytic"
FT /evidence="ECO:0000305"
FT ACT_SITE 427
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT BINDING 540
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q04609"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 738
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 387
FT /note="G->E: In pla3-1; shortened plastochron, precocious
FT leaf maturation, inflorescence branches converted into
FT vegetative shoots; pleiotropic phenotypes such as enlarged
FT embryo, seed viviparity, defects in shoot apical meristem
FT (SAM) maintenance and aberrant leaf morphology."
FT /evidence="ECO:0000269|PubMed:19228340"
SQ SEQUENCE 749 AA; 81009 MW; BB70C45AFBB75C6B CRC64;
MPALTRALRC ALLAARVALA REKARRAFAS HGEMLSQPAA ALARLPPASV RVLVGFGAAL
LVSLVVLHRR PAARGAAGGG GPAEYDPAAR FLALSEGANA TIAADLRALT AGPHLAGTGA
AAGAAARVLS GFRAAGLRTL TREYTPLLSY PGHASLALLR ADRTLLAHLS LDEPADVGRR
LVRPYHAYAP SGGAVAEAVF VNLGREEDYL TLERLGVSVR GRVAVAIRGG GYRGGVVRRA
AERSAAAVLI AGHADGGVER GTVILGGPGD PLTPGWAATA GAERLDFDHE DVKRRFPAIP
SMPVSGKTAS AIIRTLGGPA LPADWQTGVG LPVDVGGVGP GPTLVNFTYQ EDRKMGMIQD
IFAIIKGYEE PDRYVILGNH RDAWTYGAVD PNSGTSALLD IARRLGIMLQ SGWTPRRTII
LCSWDAEEFG MIGSTEWVEE NLEDLQSKAV AYLNVDCAVQ GIGLFAGSTP QLDNLLVDVT
RQVKDPDVEG KTVHDTWNKM TGGINIERLA RTDSDFAPFL HHAGIPCMDL YYGKEFPGYH
TALDSYHWME KHGDPLFLRH VAIVEIWGLL ALRLADDPVL PFDYQTYASQ LQEHANAFSS
MMENSKWVHL LNRSIEDLSD AGLEFLKEAK KLQDQNISDG YSLMRRRLLN DRLLLAERSF
LQADGLQGRG WFKHLMYSPP EDYESKLSFF PGVADAISRS SNRSAKEQQA AVRHEVRKIS
RAIQRAADVL RGEFSNRNES LYSSLSVAP
