ATL31_ARATH
ID ATL31_ARATH Reviewed; 368 AA.
AC Q8LGA5; Q0WUY7;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=E3 ubiquitin-protein ligase ATL31;
DE EC=2.3.2.27 {ECO:0000269|PubMed:19702666};
DE AltName: Full=Protein CARBON/NITROGEN INSENSITIVE 1;
DE AltName: Full=Protein SUPER SURVIVAL 1;
DE AltName: Full=RING-H2 finger protein ATL31;
DE AltName: Full=RING-type E3 ubiquitin transferase ATL31 {ECO:0000305};
DE Flags: Precursor;
GN Name=ATL31; Synonyms=CNI1, SSV1; OrderedLocusNames=At5g27420;
GN ORFNames=F21A20.130;
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;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY ORGANIZATION.
RX PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
RA Kosarev P., Mayer K.F.X., Hardtke C.S.;
RT "Evaluation and classification of RING-finger domains encoded by the
RT Arabidopsis genome.";
RL Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
RN [6]
RP NOMENCLATURE, AND GENE FAMILY ORGANIZATION.
RX PubMed=16557337; DOI=10.1007/s00239-005-0038-y;
RA Serrano M., Parra S., Alcaraz L.D., Guzman P.;
RT "The ATL gene family from Arabidopsis thaliana and Oryza sativa comprises a
RT large number of putative ubiquitin ligases of the RING-H2 type.";
RL J. Mol. Evol. 62:434-445(2006).
RN [7]
RP INDUCTION BY CHITIN.
RX PubMed=17722694; DOI=10.1094/mpmi-20-8-0900;
RA Libault M., Wan J., Czechowski T., Udvardi M., Stacey G.;
RT "Identification of 118 Arabidopsis transcription factor and 30 ubiquitin-
RT ligase genes responding to chitin, a plant-defense elicitor.";
RL Mol. Plant Microbe Interact. 20:900-911(2007).
RN [8]
RP FUNCTION.
RA Sato T., Maekawa S., Sonoda Y., Yamaguchi J.;
RT "Isolation of a novel RING-type ubiquitin ligase SSV1 that regulates
RT carbon/nitrogen response at early post-germinative growth stage in
RT Arabidopsis thaliana.";
RL (In) Proceedings of the 20th international conference on Arabidopsis
RL research, pp.abstract#543, Edinburgh (2009).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, SUBCELLULAR LOCATION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=19702666; DOI=10.1111/j.1365-313x.2009.04006.x;
RA Sato T., Maekawa S., Yasuda S., Sonoda Y., Katoh E., Ichikawa T.,
RA Nakazawa M., Seki M., Shinozaki K., Matsui M., Goto D.B., Ikeda A.,
RA Yamaguchi J.;
RT "CNI1/ATL31, a RING-type ubiquitin ligase that functions in the
RT carbon/nitrogen response for growth phase transition in Arabidopsis
RT seedlings.";
RL Plant J. 60:852-864(2009).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that is required for the plant
CC C/N response during seedling growth transition. May be involved in the
CC early steps of the plant defense signaling pathway.
CC {ECO:0000269|PubMed:19702666, ECO:0000269|Ref.8}.
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:19702666};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19702666}; Single-
CC pass membrane protein {ECO:0000269|PubMed:19702666}.
CC -!- INDUCTION: Up-regulated by chitin. Down-regulated by abscisic acid
CC (ABA). {ECO:0000269|PubMed:17722694, ECO:0000269|PubMed:19702666}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitivity to C/N conditions during post-
CC germinative growth. {ECO:0000269|PubMed:19702666}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC007123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93685.1; -; Genomic_DNA.
DR EMBL; AK226995; BAE99061.1; -; mRNA.
DR EMBL; AY084377; AAM60957.1; -; mRNA.
DR RefSeq; NP_198094.1; NM_122624.4.
DR AlphaFoldDB; Q8LGA5; -.
DR SMR; Q8LGA5; -.
DR BioGRID; 18075; 6.
DR STRING; 3702.AT5G27420.1; -.
DR iPTMnet; Q8LGA5; -.
DR PaxDb; Q8LGA5; -.
DR PRIDE; Q8LGA5; -.
DR ProteomicsDB; 246632; -.
DR EnsemblPlants; AT5G27420.1; AT5G27420.1; AT5G27420.
DR GeneID; 832801; -.
DR Gramene; AT5G27420.1; AT5G27420.1; AT5G27420.
DR KEGG; ath:AT5G27420; -.
DR Araport; AT5G27420; -.
DR TAIR; locus:2146330; AT5G27420.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_035191_1_0_1; -.
DR InParanoid; Q8LGA5; -.
DR OMA; SFLWRNT; -.
DR OrthoDB; 776201at2759; -.
DR PhylomeDB; Q8LGA5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8LGA5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8LGA5; baseline and differential.
DR Genevisible; Q8LGA5; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0043562; P:cellular response to nitrogen levels; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0098542; P:defense response to other organism; IEP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
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 Membrane; Metal-binding; Phosphoprotein; Plant defense; Reference proteome;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..368
FT /note="E3 ubiquitin-protein ligase ATL31"
FT /id="PRO_0000030716"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 124..166
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 342..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8RXX9"
FT CONFLICT 98
FT /note="A -> V (in Ref. 4; AAM60957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 40291 MW; 4DFEBCA90986D626 CRC64;
MDPIKHISLP VLVLFLLLSV SAGQPGTPDQ RHDPYAYSGS LSPAMAVVVV VVIAALFFMG
FFTVYIRHCT GAVDGSVTPA GGARRRVTNA TVARGLDAET IETFPTFVYS EVKTQKIGKG
ALECAICLNE FEDDETLRLL PKCDHVFHPH CIGAWLQGHV TCPVCRTNLA EQTPEPEVVV
ETDLEAQQQS AVPVPVVELP RVKFPRSHTT GHSVVLPGES TDRFTLRVPE ELRKKIMANW
KLNRSNSVFV LPRGGSSRSG KQVDRSRAKS DRWLFRKTPS FLWRNRDDGS IRLGGTGSVR
GNSVTSPSGD SVRADRWAFL RNPSFLWRNT TPVPSPRVEV NNKDGEGTSS VQHIGTVGST
SGSLRLPV
