ATL48_ARATH
ID ATL48_ARATH Reviewed; 349 AA.
AC Q7X843; Q9SU66;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=RING-H2 finger protein ATL48;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL48 {ECO:0000305};
DE AltName: Full=YGHL1-C3HC4 RING fusion protein;
GN Name=ATL48; OrderedLocusNames=At3g48030; ORFNames=T17F15.100;
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 [MRNA] (ISOFORM 1).
RA Abe S., Saeki T., Miyamoto K., Azama K., Cogburn L.A.;
RT "Structural analysis of YGHL1 gene and its expression in yellowtail
RT (Seriola quinqeradiata) and phylogenetic relations to vertebrate and
RT invertebrate homologs.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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:0000255|PROSITE-ProRule:PRU00836};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00836}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=HIG1-ATL48;
CC IsoId=Q7X843-1; Sequence=Displayed;
CC Name=2; Synonyms=ATL48;
CC IsoId=Q7X843-2; Sequence=VSP_014513;
CC Name=3; Synonyms=HIG1;
CC IsoId=Q7X843-3; Sequence=VSP_014514;
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; AB099346; BAC75820.1; -; mRNA.
DR EMBL; AL049658; CAB41136.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78358.1; -; Genomic_DNA.
DR EMBL; BT008566; AAP40393.1; -; mRNA.
DR EMBL; BT008679; AAP40486.1; -; mRNA.
DR PIR; T06680; T06680.
DR RefSeq; NP_190386.1; NM_114672.1. [Q7X843-1]
DR AlphaFoldDB; Q7X843; -.
DR SMR; Q7X843; -.
DR STRING; 3702.AT3G48030.1; -.
DR TCDB; 8.A.112.1.6; the respiratory supercomplex factor (rcf) family.
DR iPTMnet; Q7X843; -.
DR PaxDb; Q7X843; -.
DR PRIDE; Q7X843; -.
DR ProteomicsDB; 246642; -. [Q7X843-1]
DR EnsemblPlants; AT3G48030.1; AT3G48030.1; AT3G48030. [Q7X843-1]
DR GeneID; 823958; -.
DR Gramene; AT3G48030.1; AT3G48030.1; AT3G48030. [Q7X843-1]
DR KEGG; ath:AT3G48030; -.
DR Araport; AT3G48030; -.
DR TAIR; locus:2097890; AT3G48030.
DR eggNOG; KOG0800; Eukaryota.
DR eggNOG; KOG4431; Eukaryota.
DR HOGENOM; CLU_757271_0_0_1; -.
DR InParanoid; Q7X843; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q7X843; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q7X843; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q7X843; baseline and differential.
DR Genevisible; Q7X843; AT.
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:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR007667; Hypoxia_induced_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF04588; HIG_1_N; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS51503; HIG1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Membrane; Metal-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..349
FT /note="RING-H2 finger protein ATL48"
FT /id="PRO_0000055794"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT DOMAIN 1..85
FT /note="HIG1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
FT ZN_FING 207..249
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_014513"
FT VAR_SEQ 82..349
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_014514"
SQ SEQUENCE 349 AA; 38687 MW; A080BD4C1D9DEBBE CRC64;
MSSVEPDMED LFQEKKRVRN PLVPLGALMT AGVLTAGLIS FRRGNSQLGQ VLMRARVVVQ
GATVALMVGT GYYYGDNPWK KLLLSEIHET EALSPKSSSA ATLTLMNQKD PSSSSIVSVL
CLVISGLALI IVFLGVLYLI FKFLRKSSTL FPIPHFNYNP DLFSFSSPQL QHLFFLHDSG
LDQTAIDALP VFLYGNVTIS LEQPFDCAVC LNEFSDTDKL RLLPVCSHAF HLHCIDTWLL
SNSTCPLCRR SLSTSNVCYN HSETLVAPLS GHQQVDDGKA SLAKRVFSVR LGRFKSTNES
QSQRHDVKDE IGVRMPRRCY SMGTQQYLVC DQDFVVALSS SPREGNIGR
