ID ATL37_ARATH Reviewed; 357 AA.
AC Q9M0R4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=Putative RING-H2 finger protein ATL37;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL37 {ECO:0000305};
DE Flags: Precursor;
GN Name=ATL37; OrderedLocusNames=At4g09130; ORFNames=F23J3.160, T8A17.9;
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 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 [4]
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).
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily.
CC {ECO:0000305}.
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DR EMBL; AC005359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161514; CAB78037.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82725.1; -; Genomic_DNA.
DR PIR; E85092; E85092.
DR RefSeq; NP_192652.1; NM_116982.3.
DR AlphaFoldDB; Q9M0R4; -.
DR SMR; Q9M0R4; -.
DR PaxDb; 3702-AT4G09130-1; -.
DR EnsemblPlants; AT4G09130.1; AT4G09130.1; AT4G09130.
DR GeneID; 826491; -.
DR Gramene; AT4G09130.1; AT4G09130.1; AT4G09130.
DR KEGG; ath:AT4G09130; -.
DR Araport; AT4G09130; -.
DR TAIR; AT4G09130; ATL37.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_035191_1_0_1; -.
DR InParanoid; Q9M0R4; -.
DR OMA; NVQRGVQ; -.
DR OrthoDB; 406070at2759; -.
DR PhylomeDB; Q9M0R4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9M0R4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0R4; baseline and differential.
DR Genevisible; Q9M0R4; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd16461; RING-H2_EL5-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46539; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 1.
DR PANTHER; PTHR46539:SF2; RING FINGER PROTEIN 150 ISOFORM X1; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM01197; FANCL_C; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..357
FT /note="Putative RING-H2 finger protein ATL37"
FT /id="PRO_0000030710"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 120..162
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 172..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8RXX9"
SQ SEQUENCE 357 AA; 40001 MW; 8F6B55DF62E8B320 CRC64;
MTIFTRDFSH RILACVLLPL FLFQCLPYVT CQQGSESAGR NGKSKESSII GIVLLSLFLL
LLVVYCLNYG CCIEENETGG HEVLHSRVRR GIDKDVIESF PAFLYSEVKA FKIGNGGVEC
AICLCEFEDE EPLRWMPPCS HTFHANCIDE WLSSRSTCPV CRANLSLKSG DSFPHPSMDV
ETGNAQRGVQ ESPDERSLTG SSVTCNNNAN YTTPRSRSTG LLSSWHVPEL FLPRSHSTGH
SLVQPCQNID RFTLQLPEEV QRQLVSLNLI KRSHIALPRA RSSRQGYRSG SVGNERTGFS
QGRQTLRRAI STSLSFSFQP APVRSTLDRD NLMRETSQAN DKDFGERSFQ RLMPEKN
//
