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BZP18_ARATH
ID   BZP18_ARATH             Reviewed;         367 AA.
AC   O22873; O23726;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 157.
DE   RecName: Full=bZIP transcription factor 18 {ECO:0000305};
DE            Short=AtbZIP18 {ECO:0000303|PubMed:11906833};
DE            Short=bZIP protein 18 {ECO:0000305};
GN   Name=BZIP18 {ECO:0000303|PubMed:11906833};
GN   OrderedLocusNames=At2g40620 {ECO:0000312|Araport:AT2G40620};
GN   ORFNames=T2P4.3 {ECO:0000312|EMBL:AAB87576.1};
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Leaf {ECO:0000312|EMBL:CAB06697.1};
RX   PubMed=9356517; DOI=10.1073/pnas.94.23.12722;
RA   Babiychuk E., Fuangthong M., Van Montagu M., Inze D., Kushnir S.;
RT   "Efficient gene tagging in Arabidopsis thaliana using a gene trap
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:12722-12727(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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;
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   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11906833; DOI=10.1016/s1360-1385(01)02223-3;
RA   Jakoby M., Weisshaar B., Droege-Laser W., Vicente-Carbajosa J.,
RA   Tiedemann J., Kroj T., Parcy F.;
RT   "bZIP transcription factors in Arabidopsis.";
RL   Trends Plant Sci. 7:106-111(2002).
RN   [6]
RP   INTERACTION WITH NEAP1.
RX   PubMed=27630107; DOI=10.1093/jxb/erw332;
RA   Pawar V., Poulet A., Detourne G., Tatout C., Vanrobays E., Evans D.E.,
RA   Graumann K.;
RT   "A novel family of plant nuclear envelope-associated proteins.";
RL   J. Exp. Bot. 67:5699-5710(2016).
RN   [7]
RP   SUBUNIT, TISSUE SPECIFICITY, INTERACTION WITH BZIP34 AND BZIP61, DISRUPTION
RP   PHENOTYPE, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=27896439; DOI=10.1007/s00497-016-0295-5;
RA   Gibalova A., Steinbachova L., Hafidh S., Blahova V., Gadiou Z.,
RA   Michailidis C., Muller K., Pleskot R., Duplakova N., Honys D.;
RT   "Characterization of pollen-expressed bZIP protein interactions and the
RT   role of ATbZIP18 in the male gametophyte.";
RL   Plant Reprod. 30:1-17(2017).
CC   -!- FUNCTION: Transcription factor that may participate with bZIP34 in the
CC       gametophytic control of pollen development.
CC       {ECO:0000269|PubMed:27896439}.
CC   -!- SUBUNIT: Interacts with NEAP1 (PubMed:27630107). Forms homodimer and
CC       heterodimer with bZIP34 and bZIP61 (PubMed:27896439).
CC       {ECO:0000269|PubMed:27630107, ECO:0000269|PubMed:27896439}.
CC   -!- INTERACTION:
CC       O22873; Q9LZW4: CIPK14; NbExp=3; IntAct=EBI-4438646, EBI-307576;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC       Nucleus, nucleoplasm {ECO:0000269|PubMed:27896439}. Cytoplasm,
CC       perinuclear region {ECO:0000269|PubMed:27896439}. Cytoplasm
CC       {ECO:0000269|PubMed:27896439}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Strongly expressed in mature pollen.
CC       {ECO:0000269|PubMed:27896439}.
CC   -!- DISRUPTION PHENOTYPE: Pollen morphological defects.
CC       {ECO:0000269|PubMed:27896439}.
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DR   EMBL; Z86093; CAB06697.1; -; mRNA.
DR   EMBL; AC002336; AAB87576.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09855.1; -; Genomic_DNA.
DR   EMBL; AY074269; AAL66966.1; -; mRNA.
DR   EMBL; AY096746; AAM20380.1; -; mRNA.
DR   PIR; G84831; G84831.
DR   PIR; T52624; T52624.
DR   RefSeq; NP_181594.1; NM_129624.5.
DR   AlphaFoldDB; O22873; -.
DR   SMR; O22873; -.
DR   IntAct; O22873; 2.
DR   STRING; 3702.AT2G40620.1; -.
DR   iPTMnet; O22873; -.
DR   PaxDb; O22873; -.
DR   PRIDE; O22873; -.
DR   ProteomicsDB; 240296; -.
DR   EnsemblPlants; AT2G40620.1; AT2G40620.1; AT2G40620.
DR   GeneID; 818657; -.
DR   Gramene; AT2G40620.1; AT2G40620.1; AT2G40620.
DR   KEGG; ath:AT2G40620; -.
DR   Araport; AT2G40620; -.
DR   TAIR; locus:2061908; AT2G40620.
DR   eggNOG; ENOG502QQKB; Eukaryota.
DR   HOGENOM; CLU_026205_1_0_1; -.
DR   InParanoid; O22873; -.
DR   OMA; PNIQMPQ; -.
DR   OrthoDB; 1087497at2759; -.
DR   PhylomeDB; O22873; -.
DR   PRO; PR:O22873; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O22873; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0031490; F:chromatin DNA binding; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR   CDD; cd14703; bZIP_plant_RF2; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR044759; bZIP_RF2.
DR   InterPro; IPR046347; bZIP_sf.
DR   Pfam; PF00170; bZIP_1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..367
FT                   /note="bZIP transcription factor 18"
FT                   /id="PRO_0000441690"
FT   DOMAIN          148..211
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          150..171
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          176..190
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          294..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          166..245
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9MA75"
FT   CONFLICT        7
FT                   /note="P -> S (in Ref. 1; CAB06697)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   367 AA;  40667 MW;  6298ACCE225F26AA CRC64;
     MEDPSNPQPN QSNLSQCPPL ATAPTPAPVR GPYHRRAHSE VQFRLPEDLD LSEPFGGFDE
     LGSEDDLFCS YMDIEKLGSG SGSASDSAGP SAPRSDNPFS AENGGAEAGN SRPRHRHSLS
     VDGSSTLESI EAKKAMAPDK LAELWVVDPK RAKRIIANRQ SAARSKERKA RYILELERKV
     QTLQTEATTL SAQLSLFQRD TTGLSSENTE LKLRLQVMEQ QAKLRDALNE QLKKEVERLK
     FATGEVSPAD AYNLGMAHMQ YQQQPQQSFF QHHHQQQTDA QNLQQMTHQF HLFQPNNNQN
     QSSRTNPPTA HQLMHHATSN APAQSHSYSE AMHEDHLGRL QGLDISSCGR GSNFGRSDTV
     SESSSTM
 
 
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