WAVH1_ARATH
ID WAVH1_ARATH Reviewed; 683 AA.
AC Q9ZQ46;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=E3 ubiquitin-protein ligase WAVH1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:15644464};
DE AltName: Full=Protein WAV3 homolog 1 {ECO:0000303|PubMed:22122664};
DE AltName: Full=RING-type E3 ubiquitin transferase WAVH1 {ECO:0000305};
GN Name=WAVH1 {ECO:0000303|PubMed:22122664};
GN OrderedLocusNames=At2g22680 {ECO:0000312|Araport:AT2G22680};
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 [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
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 FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=22122664; DOI=10.1111/j.1365-313x.2011.04870.x;
RA Sakai T., Mochizuki S., Haga K., Uehara Y., Suzuki A., Harada A., Wada T.,
RA Ishiguro S., Okada K.;
RT "The wavy growth 3 E3 ligase family controls the gravitropic response in
RT Arabidopsis roots.";
RL Plant J. 70:303-314(2012).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in the regulation of
CC root growth. Acts as positive regulator of root gravitropism. Possesses
CC E3 protein ligase activity in vitro. {ECO:0000269|PubMed:22122664}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:15644464};
CC -!- TISSUE SPECIFICITY: Expressed in root tips and leaf primordia.
CC {ECO:0000269|PubMed:22122664}.
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DR EMBL; DQ086852; AAZ14056.1; -; Genomic_DNA.
DR EMBL; AC006340; AAD15576.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07340.1; -; Genomic_DNA.
DR EMBL; AY091112; AAM14062.1; -; mRNA.
DR EMBL; AY142578; AAN13147.1; -; mRNA.
DR PIR; E84615; E84615.
DR RefSeq; NP_179853.1; NM_127833.5.
DR AlphaFoldDB; Q9ZQ46; -.
DR SMR; Q9ZQ46; -.
DR IntAct; Q9ZQ46; 6.
DR STRING; 3702.AT2G22680.1; -.
DR iPTMnet; Q9ZQ46; -.
DR PaxDb; Q9ZQ46; -.
DR PRIDE; Q9ZQ46; -.
DR ProteomicsDB; 242746; -.
DR EnsemblPlants; AT2G22680.1; AT2G22680.1; AT2G22680.
DR GeneID; 816799; -.
DR Gramene; AT2G22680.1; AT2G22680.1; AT2G22680.
DR KEGG; ath:AT2G22680; -.
DR Araport; AT2G22680; -.
DR TAIR; locus:2065999; AT2G22680.
DR eggNOG; ENOG502QVJZ; Eukaryota.
DR HOGENOM; CLU_006228_3_0_1; -.
DR InParanoid; Q9ZQ46; -.
DR OMA; QKNPFAT; -.
DR OrthoDB; 274565at2759; -.
DR PhylomeDB; Q9ZQ46; -.
DR PRO; PR:Q9ZQ46; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQ46; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0009630; P:gravitropism; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00092; VWA; 1.
DR Pfam; PF17123; zf-RING_11; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50234; VWFA; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..683
FT /note="E3 ubiquitin-protein ligase WAVH1"
FT /id="PRO_0000443505"
FT DOMAIN 302..438
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT ZN_FING 130..176
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 683 AA; 74401 MW; AB239552684E2B4B CRC64;
MLNGWRRAFC TSIPKETNQN DVDDDGLVGL RHKSTSRFGF FSTPSTPRSD SGTGTYSLRC
RTSTATAVST TSSLPGTPKL KCKTTTTGET TPRNRSLVSL LTPSSSSISP ASFTLLKSKL
RFKQSSSNKC GICLQSVKSG QGTAIFTAEC SHTFHFPCVT SRAAANHNRL ASCPVCGSSL
LPEIRNYAKP ESQIKPEIKN KSLRVYNDDE ALISSPISPA GFHTILESDE NEDCEEFTGF
SVNTPSPLTA KLLTDRNVDV KLSPESAIVA SGKGYETYSV VMKVKSPPFP TARGFARRVP
VDLVAVLDVS GRNSGGKLEM LKQTMRIVLS NLREMDRLSI IAFSSSSKRL SPLRRMTANG
RRSARRIVDI ITVPGSVSGV GIDFSGEGMS VNDALKKAVK VLDDRRQKNP FTAVFVLTDR
QAHQVAQLAH SRIPIHTIWL SHAIPEDAFA RTINGYLSLS VQDLGLQLGI VSGLGQGEIT
SVYSLSGRPA WLGTGSIRLG DMYAEEERAL LVEIKSPVNN SLTGSRSHKI MTVRSRYVDP
TTQELRNPED RALLIPTPLT VRSSSNPNIS RLRNLHVSTR AVAESRRLIE RNHYSGAHRL
LTSARALLVQ HGLSSSDACI RGLDAEIADL NSVKGRHVAA SESLESLTPT SAWKAAERLA
KVAMVRKHMN RVSDLHGFEN ARF
