ATL16_ARATH
ID ATL16_ARATH Reviewed; 375 AA.
AC Q9LSW9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=RING-H2 finger protein ATL16;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL16 {ECO:0000305};
GN Name=ATL16; OrderedLocusNames=At5g43420; ORFNames=MWF20.13;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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=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 [4]
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 [5]
RP IDENTIFICATION.
RX PubMed=15238540; DOI=10.1534/genetics.104.028043;
RA Serrano M., Guzman P.;
RT "Isolation and gene expression analysis of Arabidopsis thaliana mutants
RT with constitutive expression of ATL2, an early elicitor-response RING-H2
RT zinc-finger gene.";
RL Genetics 167:919-929(2004).
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).
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; AB025638; BAA97421.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94959.1; -; Genomic_DNA.
DR EMBL; BT008334; AAP37693.1; -; mRNA.
DR RefSeq; NP_199155.1; NM_123708.3.
DR AlphaFoldDB; Q9LSW9; -.
DR SMR; Q9LSW9; -.
DR BioGRID; 19612; 19.
DR IntAct; Q9LSW9; 19.
DR STRING; 3702.AT5G43420.1; -.
DR PaxDb; Q9LSW9; -.
DR PRIDE; Q9LSW9; -.
DR ProteomicsDB; 246626; -.
DR EnsemblPlants; AT5G43420.1; AT5G43420.1; AT5G43420.
DR GeneID; 834362; -.
DR Gramene; AT5G43420.1; AT5G43420.1; AT5G43420.
DR KEGG; ath:AT5G43420; -.
DR Araport; AT5G43420; -.
DR TAIR; locus:2176436; AT5G43420.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_040108_1_0_1; -.
DR InParanoid; Q9LSW9; -.
DR OMA; SFCECAV; -.
DR OrthoDB; 1510010at2759; -.
DR PhylomeDB; Q9LSW9; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LSW9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LSW9; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044600; ATL1/ATL16.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46913; PTHR46913; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Membrane; Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..375
FT /note="RING-H2 finger protein ATL16"
FT /id="PRO_0000055814"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 138..180
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 375 AA; 42316 MW; 52966E8C2340D691 CRC64;
MDLSNRRNPL RDLSFPPPPP PPIFHRASST GTSFPILAVA VIGILATAFL LVSYYVFVIK
CCLNWHRIDI LGRFSLSRRR RNDQDPLMVY SPELRSRGLD ESVIRAIPIF KFKKRYDQND
GVFTGEGEEE EEKRSQECSV CLSEFQDEEK LRIIPNCSHL FHIDCIDVWL QNNANCPLCR
TRVSCDTSFP PDRVSAPSTS PENLVMLRGE NEYVVIELGS SIGSDRDSPR HGRLLTGQER
SNSGYLLNEN TQNSISPSPK KLDRGGLPRK FRKLHKMTSM GDECIDIRRG KDEQFGSIQP
IRRSISMDSS ADRQLYLAVQ EAIRKNREVL VVGDGGGCSS SSGNVSNSKV KRSFFSFGSS
RRSRSSSKLP LYFEP
