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ZWIP2_ARATH
ID   ZWIP2_ARATH             Reviewed;         383 AA.
AC   Q9SVY1; Q84TI0;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 161.
DE   RecName: Full=Zinc finger protein WIP2;
DE   AltName: Full=Protein NO TRANSMITTING TRACT;
DE   AltName: Full=WIP-domain protein 2 {ECO:0000303|PubMed:11782451};
DE            Short=AtWIP2 {ECO:0000303|PubMed:11782451};
GN   Name=WIP2 {ECO:0000303|PubMed:11782451}; Synonyms=NTT;
GN   OrderedLocusNames=At3g57670 {ECO:0000312|Araport:AT3G57670};
GN   ORFNames=F15B8.140 {ECO:0000312|EMBL:CAB41188.1};
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;
RX   PubMed=11782451; DOI=10.1101/gad.212702;
RA   Sagasser M., Lu G.-H., Hahlbrock K., Weisshaar B.;
RT   "A. thaliana TRANSPARENT TESTA 1 is involved in seed coat development and
RT   defines the WIP subfamily of plant zinc finger proteins.";
RL   Genes Dev. 16:138-149(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=17600712; DOI=10.1016/j.cub.2007.05.079;
RA   Crawford B.C., Ditta G., Yanofsky M.F.;
RT   "The NTT gene is required for transmitting-tract development in carpels of
RT   Arabidopsis thaliana.";
RL   Curr. Biol. 17:1101-1108(2007).
RN   [8]
RP   SUBCELLULAR LOCATION, AND ZINC-FINGER.
RX   PubMed=20541552; DOI=10.1016/j.febslet.2010.06.007;
RA   Appelhagen I., Huep G., Lu G.H., Strompen G., Weisshaar B., Sagasser M.;
RT   "Weird fingers: functional analysis of WIP domain proteins.";
RL   FEBS Lett. 584:3116-3122(2010).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH BLH9; STM;
RP   AGL8/FUL; AGL1/SHP1 AND AGL5/SHP2.
RX   PubMed=23515580; DOI=10.1007/s10059-013-0030-0;
RA   Chung K.S., Lee J.H., Lee J.S., Ahn J.H.;
RT   "Fruit indehiscence caused by enhanced expression of NO TRANSMITTING TRACT
RT   in Arabidopsis thaliana.";
RL   Mol. Cells 35:519-525(2013).
RN   [10]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=25039392; DOI=10.1111/tpj.12617;
RA   Marsch-Martinez N., Zuniga-Mayo V.M., Herrera-Ubaldo H., Ouwerkerk P.B.,
RA   Pablo-Villa J., Lozano-Sotomayor P., Greco R., Ballester P., Balanza V.,
RA   Kuijt S.J., Meijer A.H., Pereira A., Ferrandiz C., de Folter S.;
RT   "The NTT transcription factor promotes replum development in Arabidopsis
RT   fruits.";
RL   Plant J. 80:69-81(2014).
CC   -!- FUNCTION: Transcriptional regulator required for normal differentiation
CC       of the ovary transmitting tract cells and pollen tube growth. In
CC       Arabidopsis, the transmitting tract facilitates the transport of pollen
CC       tubes to the ovules for fertilization (PubMed:17600712). May play a
CC       role in the regulation of AGL8/FUL, which is required for normal
CC       pattern of cell division, expansion and differentiation during
CC       morphogenesis of the silique (PubMed:23515580). Plays a role in replum
CC       development by the activation of the homeobox protein KNAT1
CC       (PubMed:25039392). {ECO:0000269|PubMed:17600712,
CC       ECO:0000269|PubMed:23515580, ECO:0000269|PubMed:25039392}.
CC   -!- SUBUNIT: Can form homodimers. Interacts with BLH9, STM, AGL8/FUL,
CC       AGL1/SHP1 and AGL5/SHP2. {ECO:0000269|PubMed:25039392}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20541552,
CC       ECO:0000269|PubMed:23515580, ECO:0000269|PubMed:25039392}.
CC   -!- TISSUE SPECIFICITY: Expressed in developing carpels (PubMed:17600712).
CC       Expressed in the shoot apical meristem and the replum
CC       (PubMed:25039392). {ECO:0000269|PubMed:17600712}.
CC   -!- DISRUPTION PHENOTYPE: Reduced fertility, fruit length and seed set
CC       (PubMed:17600712). Reduced replum width and cell number
CC       (PubMed:25039392). {ECO:0000269|PubMed:17600712,
CC       ECO:0000269|PubMed:25039392}.
CC   -!- MISCELLANEOUS: The fruits of the gain-of-function mutant ntt-3D (T-DNA
CC       tagging) fail to dehisce. {ECO:0000269|PubMed:23515580}.
CC   -!- SIMILARITY: Belongs to the WIP C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF254447; AAL55722.1; -; mRNA.
DR   EMBL; AL049660; CAB41188.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79685.1; -; Genomic_DNA.
DR   EMBL; BT005772; AAO64176.1; -; mRNA.
DR   EMBL; BT021089; AAX12859.1; -; mRNA.
DR   EMBL; AK228585; BAF00501.1; -; mRNA.
DR   PIR; T06753; T06753.
DR   RefSeq; NP_191326.1; NM_115627.4.
DR   AlphaFoldDB; Q9SVY1; -.
DR   BioGRID; 10251; 9.
DR   IntAct; Q9SVY1; 36.
DR   STRING; 3702.AT3G57670.1; -.
DR   PaxDb; Q9SVY1; -.
DR   PRIDE; Q9SVY1; -.
DR   EnsemblPlants; AT3G57670.1; AT3G57670.1; AT3G57670.
DR   GeneID; 824936; -.
DR   Gramene; AT3G57670.1; AT3G57670.1; AT3G57670.
DR   KEGG; ath:AT3G57670; -.
DR   Araport; AT3G57670; -.
DR   TAIR; locus:2076641; AT3G57670.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_052255_0_1_1; -.
DR   InParanoid; Q9SVY1; -.
DR   OMA; HIHPKEE; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q9SVY1; -.
DR   PRO; PR:Q9SVY1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SVY1; baseline and differential.
DR   Genevisible; Q9SVY1; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0001709; P:cell fate determination; IMP:TAIR.
DR   GO; GO:1990058; P:fruit replum development; IMP:UniProtKB.
DR   GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR   GO; GO:0080022; P:primary root development; IGI:TAIR.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR   GO; GO:0010500; P:transmitting tissue development; IMP:TAIR.
DR   InterPro; IPR043584; WIP1/2/3/4/5/6.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45878; PTHR45878; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..383
FT                   /note="Zinc finger protein WIP2"
FT                   /id="PRO_0000431316"
FT   ZN_FING         217..239
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         264..296
FT                   /note="C2H2-type 2; atypical"
FT                   /evidence="ECO:0000303|PubMed:20541552"
FT   ZN_FING         301..323
FT                   /note="C2H2-type 3; atypical"
FT                   /evidence="ECO:0000303|PubMed:20541552"
FT   ZN_FING         327..352
FT                   /note="C2H2-type 4; atypical"
FT                   /evidence="ECO:0000303|PubMed:20541552"
FT   REGION          19..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           293..296
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VWG3"
FT   MOTIF           336..339
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VWG3"
FT   COMPBIAS        27..41
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..68
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..118
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        117
FT                   /note="D -> G (in Ref. 4; AAO64176 and 6; BAF00501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="D -> G (in Ref. 4; AAO64176 and 6; BAF00501)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   383 AA;  43337 MW;  9DDDCEE6E66A4506 CRC64;
     MTDPYSNFFT DWFKSNPFHH YPNSSTNPSP HPLPPVTPPS SFFFFPQSGD LRRPPPPPTP
     PPSPPLREAL PLLSLSPANK QQDHHHNHDH LIQEPPSTSM DVDYDHHHQD DHHNLDDDDH
     DVTVALHIGL PSPSAQEMAS LLMMSSSSSS SRTTHHHEDM NHKKDLDHEY SHGAVGGGED
     DDEDSVGGDG GCRISRLNKG QYWIPTPSQI LIGPTQFSCP VCFKTFNRYN NMQMHMWGHG
     SQYRKGPESL RGTQPTGMLR LPCYCCAPGC RNNIDHPRAK PLKDFRTLQT HYKRKHGIKP
     FMCRKCGKAF AVRGDWRTHE KNCGKLWYCI CGSDFKHKRS LKDHIKAFGN GHGAYGIDGF
     DEEDEPASEV EQLDNDHESM QSK
 
 
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