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EDA40_ARATH
ID   EDA40_ARATH             Reviewed;         739 AA.
AC   F4JSV3; Q8GYZ4; Q9SZJ1;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase EDA40 {ECO:0000305};
DE            EC=2.3.2.27 {ECO:0000305};
DE   AltName: Full=Protein EMBRYO SAC DEVELOPMENT ARREST 40 {ECO:0000303|PubMed:15634699};
DE   AltName: Full=RING-type E3 ubiquitin transferase EDA40 {ECO:0000305};
GN   Name=EDA40 {ECO:0000303|PubMed:15634699};
GN   OrderedLocusNames=At4g37890 {ECO:0000312|Araport:AT4G37890};
GN   ORFNames=F20D10.10 {ECO:0000312|EMBL:CAB37529.1};
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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 DISRUPTION PHENOTYPE.
RX   PubMed=15634699; DOI=10.1242/dev.01595;
RA   Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA   Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT   "Genetic and molecular identification of genes required for female
RT   gametophyte development and function in Arabidopsis.";
RL   Development 132:603-614(2005).
CC   -!- FUNCTION: Probable E3 ubiquitin-protein ligase involved in female
CC       gametophyte development. Required for fusion of polar nuclei in the
CC       embryo sac. {ECO:0000269|PubMed:15634699}.
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:0000305};
CC   -!- DISRUPTION PHENOTYPE: Embryo sac development arrest. Unfused polar
CC       nuclei. {ECO:0000269|PubMed:15634699}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB37529.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB80454.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL035538; CAB37529.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161592; CAB80454.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86849.1; -; Genomic_DNA.
DR   EMBL; AK117301; BAC41972.1; -; mRNA.
DR   EMBL; BT005963; AAO64898.1; -; mRNA.
DR   PIR; T05616; T05616.
DR   RefSeq; NP_195502.2; NM_119950.2.
DR   AlphaFoldDB; F4JSV3; -.
DR   SMR; F4JSV3; -.
DR   IntAct; F4JSV3; 1.
DR   STRING; 3702.AT4G37890.1; -.
DR   iPTMnet; F4JSV3; -.
DR   PaxDb; F4JSV3; -.
DR   PRIDE; F4JSV3; -.
DR   ProteomicsDB; 247061; -.
DR   EnsemblPlants; AT4G37890.1; AT4G37890.1; AT4G37890.
DR   GeneID; 829945; -.
DR   Gramene; AT4G37890.1; AT4G37890.1; AT4G37890.
DR   KEGG; ath:AT4G37890; -.
DR   Araport; AT4G37890; -.
DR   TAIR; locus:2121008; AT4G37890.
DR   eggNOG; ENOG502QVJZ; Eukaryota.
DR   InParanoid; F4JSV3; -.
DR   OrthoDB; 274565at2759; -.
DR   PRO; PR:F4JSV3; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JSV3; baseline and differential.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0010197; P:polar nucleus fusion; IMP:TAIR.
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; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Reference proteome; Transferase; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..739
FT                   /note="Probable E3 ubiquitin-protein ligase EDA40"
FT                   /id="PRO_0000443507"
FT   DOMAIN          357..459
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   ZN_FING         169..214
FT                   /note="RING-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          19..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        370
FT                   /note="E -> G (in Ref. 3; BAC41972 and 4; AAO64898)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   739 AA;  81479 MW;  45692DF3A6929B48 CRC64;
     MMNGLRRTFW SSIHKKKDNN RVDDSLDRQK PTTTSRFGFF SNPSTPRSET RPDSVTCSPT
     IPCQSWSATA ISTPSPSLPA SPKLQCDTSG DVTPTRNRSP LSFLSVSSSS STPSSPKSPA
     SFSLLKSKLC FTKVRILNRN NQVNIFKNNS KLTFLRLCYE QSSISSSKCG ICLQSAKAGR
     GTAIFTAECS HTFHFPCVAS RAGDRNLLSD CPVCGASWRE TSLLPLSLSS SLHESGSESD
     SKIRESKNNN KSLRVYNDDE PLISSPISRT GFNTIPESNE DEEEEDNDDG EFKGFYVNTP
     SPLTTKKMLT DSVTGHVDVK LSSEAAIVAV GRGNETYSVL MKIKSPSLPT ARRSPVDLVT
     VIDVSGGNIE MVKRAMRQVI SSLRETDRLS MVSFSSSSKR LTPLRRMTAN GRRLARRIVD
     DISGDGDGMS VNDAVKKAAK VIEDRRQKNL FTTIFVLTDR NRNSAHQAQL AQPDFVTSTR
     FSHLEIPTHT IWLGACNHAL PEDVFAKRIK SLLSLSVQDL TLNLGLVSGS GQGKVTSVYS
     LSGRPVWLGS GLIRLGDMYG DEEREVLVEL KSPSSSRSQR IMTVRSRHVD PTTQEIKNYE
     DRALMIPRPT TVRSSDPSIA RLRNLHVSTR AVAESRRLVE VNDYSGAERM LTSARALLVQ
     YGLSSSDSCL RGLEAELADL NRLRGRHVAV KSPEPVVQKS EPLTPTSAWR AAERLAKVAI
     MRKHMNRVSD LHGFENARF
 
 
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