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NPGR2_ARATH
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   25-MAY-2022, entry version 139.
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.AT4G28600.1; -.
DR   iPTMnet; Q66GN3; -.
DR   PaxDb; Q66GN3; -.
DR   PRIDE; Q66GN3; -.
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; locus:2139860; AT4G28600.
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; -; 3.
DR   InterPro; IPR043376; NPG1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR44102; PTHR44102; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 7.
DR   SUPFAM; SSF48452; SSF48452; 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
 
 
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