ATL10_ARATH
ID ATL10_ARATH Reviewed; 251 AA.
AC P0C034; Q4PSZ7; Q9M9C1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=RING-H2 finger protein ATL10;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL10 {ECO:0000305};
GN Name=ATL10; OrderedLocusNames=At1g49220; ORFNames=F27J15.37;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF69723.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g49220 has been split into 2 genes: At1g49220 and At1g49230.; Evidence={ECO:0000305};
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DR EMBL; AC016041; AAF69723.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32406.1; -; Genomic_DNA.
DR EMBL; DQ056489; AAY78646.1; -; mRNA.
DR PIR; G96528; G96528.
DR RefSeq; NP_175348.1; NM_103812.1.
DR AlphaFoldDB; P0C034; -.
DR SMR; P0C034; -.
DR STRING; 3702.AT1G49220.1; -.
DR PaxDb; P0C034; -.
DR PRIDE; P0C034; -.
DR EnsemblPlants; AT1G49220.1; AT1G49220.1; AT1G49220.
DR GeneID; 841345; -.
DR Gramene; AT1G49220.1; AT1G49220.1; AT1G49220.
DR KEGG; ath:AT1G49220; -.
DR Araport; AT1G49220; -.
DR TAIR; locus:2028506; AT1G49220.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_013137_9_0_1; -.
DR InParanoid; P0C034; -.
DR OMA; TRFMISE; -.
DR OrthoDB; 535233at2759; -.
DR PhylomeDB; P0C034; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P0C034; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P0C034; baseline and differential.
DR Genevisible; P0C034; 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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR044602; ATL10/ATL75-79.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46905; PTHR46905; 2.
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..251
FT /note="RING-H2 finger protein ATL10"
FT /id="PRO_0000055768"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 135..177
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 251 AA; 27809 MW; FCB92CE8AAAF0405 CRC64;
MSANELPSSA QAFQEQFLGG FVSRKLLLHN PFDHNTQRAF AVAPSPLITH ENNLSGNVMM
LLSILICGII CCLGLHYIIR CALRRSTRFM ISEPVPSLSS TRGSSNKGIK KKALRMFPVV
SYSPEMNLPG LDEECVICLS DFVSGEQLRL LPKCNHGFHV RCIDKWLQQH LTCPKCRNCL
VETCQKILGD FSQADSVTAE PTEIVIVTIV PLEPTEIVIV TIAPLEPTEI VIVMIAPLEP
EGRVNTIREI S
