SHGR9_ARATH
ID SHGR9_ARATH Reviewed; 283 AA.
AC Q8GXF8; Q9LZ10;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=E3 ubiquitin-protein ligase SGR9, amyloplastic;
DE EC=2.3.2.27;
DE AltName: Full=Protein SHOOT GRAVITROPISM 9;
DE AltName: Full=RING-type E3 ubiquitin transferase SGR9 {ECO:0000305};
DE Flags: Precursor;
GN Name=SGR9; OrderedLocusNames=At5g02750; ORFNames=F9G14.60;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-232 AND TRP-244,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21602290; DOI=10.1105/tpc.110.079442;
RA Nakamura M., Toyota M., Tasaka M., Morita M.T.;
RT "An Arabidopsis E3 ligase, SHOOT GRAVITROPISM9, modulates the interaction
RT between statoliths and F-actin in gravity sensing.";
RL Plant Cell 23:1830-1848(2011).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates. Modulates
CC amyloplast dynamics and sedimentation in statocytes during
CC inflorescence, hypocotyl and root gravitropism, probably by regulating
CC amyloplast interaction with actin filaments (AFs) in endodermal cells.
CC {ECO:0000269|PubMed:21602290}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Plastid, amyloplast
CC {ECO:0000269|PubMed:21602290}. Note=Localized at amyloplasts within
CC gravity-sensing cells.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, hypocotyls, roots and
CC stems. Present especially in hypocotyl and inflorescence endodermis, as
CC well as in root cap columella, tissues that act as statocytes.
CC {ECO:0000269|PubMed:21602290}.
CC -!- PTM: Auto-ubiquitinated as part of the enzymatic reaction.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Reduced gravitropism, altered amyloplasts
CC sedimentation but increased amyloplasts saltatory movement. Abnormal
CC interactions between amyloplasts and actin filaments (AFs) in
CC endodermal cells. {ECO:0000269|PubMed:21602290}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB86029.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL162973; CAB86029.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED90513.1; -; Genomic_DNA.
DR EMBL; AK118262; BAC42880.1; -; mRNA.
DR EMBL; BT005552; AAO63972.1; -; mRNA.
DR PIR; T48296; T48296.
DR RefSeq; NP_195895.2; NM_120353.3.
DR AlphaFoldDB; Q8GXF8; -.
DR SMR; Q8GXF8; -.
DR STRING; 3702.AT5G02750.1; -.
DR PaxDb; Q8GXF8; -.
DR PRIDE; Q8GXF8; -.
DR EnsemblPlants; AT5G02750.1; AT5G02750.1; AT5G02750.
DR GeneID; 831806; -.
DR Gramene; AT5G02750.1; AT5G02750.1; AT5G02750.
DR KEGG; ath:AT5G02750; -.
DR Araport; AT5G02750; -.
DR TAIR; locus:2151241; AT5G02750.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_067430_0_0_1; -.
DR InParanoid; Q8GXF8; -.
DR OMA; FHWHCAL; -.
DR OrthoDB; 1249953at2759; -.
DR PhylomeDB; Q8GXF8; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8GXF8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GXF8; baseline and differential.
DR GO; GO:0009501; C:amyloplast; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0009630; P:gravitropism; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Amyloplast; Metal-binding; Plastid; Reference proteome; Transferase;
KW Transit peptide; Ubl conjugation; Zinc; Zinc-finger.
FT TRANSIT 1..32
FT /note="Amyloplast"
FT /evidence="ECO:0000255"
FT CHAIN 33..283
FT /note="E3 ubiquitin-protein ligase SGR9, amyloplastic"
FT /id="PRO_0000429062"
FT ZN_FING 214..255
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MUTAGEN 232
FT /note="C->A: Reduced E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:21602290"
FT MUTAGEN 244
FT /note="W->A: Reduced E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:21602290"
SQ SEQUENCE 283 AA; 32149 MW; FB240029A4809498 CRC64;
MEDENTTIIM ASLSALSPSH LTNLTHSILS ISHHHRRRLG AVLSSPTLFS LTLRHLLSLS
LPDKTHLIAN HLLSLLHPLL IHRKHHSSYA VTMKLRDLDA VVLLLFLCET HQLHPDVLEA
SADNWREILG NTYSNNMLSN NSGLWTCDAG ILMPYIETLV RCKRFVDIMG GYNHLRRRDQ
KEGYQVPAAR AAVVALRAVE VFNVAASNAG EVECVICKEE MSEGRDVCEM PCQHFFHWKC
ILPWLSKKNT CPFCRFQLPT DDVFSEIQRL WEILVKSSEL HVA
