ATL22_ARATH
ID ATL22_ARATH Reviewed; 377 AA.
AC Q9SKK8;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=RING-H2 finger protein ATL22;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL22 {ECO:0000305};
DE Flags: Precursor;
GN Name=ATL22; OrderedLocusNames=At2g25410; ORFNames=F13B15.7;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-377.
RC STRAIN=cv. Columbia;
RX PubMed=16244158; DOI=10.1104/pp.105.063479;
RA Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT reveals numerous transcript variants.";
RL Plant Physiol. 139:1323-1337(2005).
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 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; AC006300; AAD20701.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07698.1; -; Genomic_DNA.
DR EMBL; AY461616; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A84648; A84648.
DR RefSeq; NP_565593.1; NM_128098.3.
DR AlphaFoldDB; Q9SKK8; -.
DR SMR; Q9SKK8; -.
DR PaxDb; Q9SKK8; -.
DR PRIDE; Q9SKK8; -.
DR EnsemblPlants; AT2G25410.1; AT2G25410.1; AT2G25410.
DR GeneID; 817079; -.
DR Gramene; AT2G25410.1; AT2G25410.1; AT2G25410.
DR KEGG; ath:AT2G25410; -.
DR Araport; AT2G25410; -.
DR TAIR; locus:2040085; AT2G25410.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_046769_0_0_1; -.
DR InParanoid; Q9SKK8; -.
DR OMA; PAREGCN; -.
DR OrthoDB; 998495at2759; -.
DR PhylomeDB; Q9SKK8; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SKK8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKK8; 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:0030247; F:polysaccharide binding; IEA:InterPro.
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; IPR025287; WAK_GUB.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13947; GUB_WAK_bind; 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; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..377
FT /note="RING-H2 finger protein ATL22"
FT /id="PRO_0000396123"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 327..369
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 377 AA; 42390 MW; A7099154F50C65B8 CRC64;
MTSKLLPLLL NLIFLFFFPL LNASEQKPCY SFSCSQESVV ARFPFSLFSY QPESCGYSGF
NLICKDDANT TLKLPKSEPF LVKEIDYETQ RIRLNDPENC LARRLLNFDP SGSPFSFLRS
RNYTFLICPK EANITASFRA IDCLGNTTSS FFVVQFENLG SMPSSCHIFK ILPLPFSWFV
AYTTYPDGQN SRDMWLKWDS PDCRDCERRT NSRCGFKNNT SHQVECFSSV NPGLHNTGLQ
VLKIMCLSLV GPLTALTFCV GLVMCSSERV SSQIQQAVVA RLSGSVTSQP SNEVARIGLD
ESTIESYKKV ELGESRRLPT GSNDVVCPIC LSEYATKETV RCLPECEHCF HTECIDAWLK
LHSSCPVCRS NPSPLRD
