ID NPGR2_ARATH Reviewed; 739 AA.
AC Q66GN3; Q9M0H1;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 24-JAN-2024, entry version 144.
DE RecName: Full=Protein NPGR2 {ECO:0000303|PubMed:12928497};
DE AltName: Full=NO POLLEN GERMINATION RELATED 2 {ECO:0000303|PubMed:12928497};
GN Name=NPGR2 {ECO:0000303|PubMed:12928497};
GN OrderedLocusNames=At4g28600 {ECO:0000312|Araport:AT4G28600};
GN ORFNames=T5F17.50 {ECO:0000312|EMBL:CAB81448.1};
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 {ECO:0000312|EMBL:AAU05492.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE, INTERACTION WITH
RP CALMODULIN, AND TISSUE SPECIFICITY.
RX PubMed=12928497; DOI=10.1073/pnas.1734110100;
RA Golovkin M., Reddy A.;
RT "A calmodulin-binding protein from Arabidopsis has an essential role in
RT pollen germination.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10558-10563(2003).
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].
RC STRAIN=cv. Columbia;
RA Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH CALMODULIN.
RX PubMed=11782485; DOI=10.1074/jbc.m111626200;
RA Reddy V.S., Ali G.S., Reddy A.S.N.;
RT "Genes encoding calmodulin-binding proteins in the Arabidopsis genome.";
RL J. Biol. Chem. 277:9840-9852(2002).
CC -!- SUBUNIT: Interacts with calmodulin in a calcium-dependent manner.
CC {ECO:0000269|PubMed:11782485, ECO:0000269|PubMed:12928497}.
CC -!- TISSUE SPECIFICITY: Expressed in pollen, flowers and fruits.
CC {ECO:0000269|PubMed:12928497}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB81448.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81448.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL161573; CAB81448.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85511.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67320.1; -; Genomic_DNA.
DR EMBL; BT015369; AAU05492.1; -; mRNA.
DR EMBL; BT020340; AAV85695.1; -; mRNA.
DR PIR; T10654; T10654.
DR RefSeq; NP_001329155.1; NM_001341925.1.
DR RefSeq; NP_194589.2; NM_119002.6.
DR AlphaFoldDB; Q66GN3; -.
DR SMR; Q66GN3; -.
DR STRING; 3702.Q66GN3; -.
DR iPTMnet; Q66GN3; -.
DR PaxDb; 3702-AT4G28600-1; -.
DR ProteomicsDB; 250543; -.
DR EnsemblPlants; AT4G28600.1; AT4G28600.1; AT4G28600.
DR EnsemblPlants; AT4G28600.2; AT4G28600.2; AT4G28600.
DR GeneID; 828978; -.
DR Gramene; AT4G28600.1; AT4G28600.1; AT4G28600.
DR Gramene; AT4G28600.2; AT4G28600.2; AT4G28600.
DR KEGG; ath:AT4G28600; -.
DR Araport; AT4G28600; -.
DR TAIR; AT4G28600; NPGR2.
DR eggNOG; KOG4162; Eukaryota.
DR HOGENOM; CLU_024601_0_0_1; -.
DR InParanoid; Q66GN3; -.
DR PhylomeDB; Q66GN3; -.
DR PRO; PR:Q66GN3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q66GN3; baseline and differential.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:TAIR.
DR GO; GO:0098857; C:membrane microdomain; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005516; F:calmodulin binding; TAS:TAIR.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR InterPro; IPR043376; NPG1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44102; PROTEIN NPG1; 1.
DR PANTHER; PTHR44102:SF12; PROTEIN NPGR2; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF14559; TPR_19; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..739
FT /note="Protein NPGR2"
FT /id="PRO_0000438624"
FT REPEAT 90..127
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 162..195
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 215..248
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 465..498
FT /note="TPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 500..533
FT /note="TPR 5"
FT /evidence="ECO:0000255"
FT REPEAT 536..569
FT /note="TPR 6"
FT /evidence="ECO:0000255"
FT REPEAT 592..625
FT /note="TPR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 626..659
FT /note="TPR 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT REPEAT 697..733
FT /note="TPR 9"
FT /evidence="ECO:0000255"
FT REGION 32..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 82733 MW; CCF82B32474ED75E CRC64;
MKNSEIRPEK LHLRKLRKSL RKIRMKCLCS GEQMRHREEE DKKSEVGVGR DYNGSSALST
AESENAKKLD NGNIEEAELS LRETSSLNYE EARALLGRIE YQKGNIEAAL RVFEGIDING
ITVKMKTALT VREDRKHRRR SKGGFSTAPS PAMSKHAVSL LFEAIFLKAK SLQRLGRFQE
AAESCRVILD IVETSLAEGA SDNVTGDIKL QETLTKAVEL LPELWKLADS PRDAILSYRR
ALLNHWKLDP ETTARIQKEY AVFLLYSGEE AVPPNLRSQT EGSFIPRNNV EEAILLLMLL
LRKVNLKRIS WDAAILDHLS FALTIAGDLT ALAKQFEELS PELLDQRELY HTLSLCYQGA
GEGLVALGLL RKLFSEREDP NRTSGLLMAS KICGERSGLA EEGLDYARKA IGNLGKECSQ
LDGAARFVLG ITLTESSRMA VTETERIARQ SEGIQALESA DMTNPRVVHR LALENAEQRK
LDSALAYAKE ALKLGAESDL EVWLLLARVL SAQKRFSDAE TIVDAALNET GKWEQGKLLR
LKAKLRLAKG EVKDAIKTYT QLLALLQVQS KSFNSAKKLP KGYVKELMSL ELGTWHDLAH
IYINLSQWRD AESCLSRSRL IAPYSSVRYH IEGVLYNRRG QLEEAMEAFT TALDIDPMHV
PSLTSKAEIL LEVGNRSGIA VVRSFLMEAL RIDRLNHSAW YNLGKMFKAE GSVSSMQEAV
ECFQAAVTLE ETMPVEPFR
//
