ATL49_ARATH
ID ATL49_ARATH Reviewed; 423 AA.
AC Q9ZV53;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Putative RING-H2 finger protein ATL49;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 16;
DE AltName: Full=RING-type E3 ubiquitin transferase ATL49 {ECO:0000305};
GN Name=ATL49; Synonyms=MEE16; OrderedLocusNames=At2g18650; ORFNames=MSF3.3;
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 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 FUNCTION.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
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 -!- FUNCTION: May be involved in female gametophyte development.
CC {ECO:0000269|PubMed:15634699}.
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; AC005724; AAD08934.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06789.1; -; Genomic_DNA.
DR PIR; H84566; H84566.
DR RefSeq; NP_179455.1; NM_127421.2.
DR AlphaFoldDB; Q9ZV53; -.
DR SMR; Q9ZV53; -.
DR STRING; 3702.AT2G18650.1; -.
DR iPTMnet; Q9ZV53; -.
DR PaxDb; Q9ZV53; -.
DR PRIDE; Q9ZV53; -.
DR EnsemblPlants; AT2G18650.1; AT2G18650.1; AT2G18650.
DR GeneID; 816380; -.
DR Gramene; AT2G18650.1; AT2G18650.1; AT2G18650.
DR KEGG; ath:AT2G18650; -.
DR Araport; AT2G18650; -.
DR TAIR; locus:2054049; AT2G18650.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_034332_0_0_1; -.
DR InParanoid; Q9ZV53; -.
DR OMA; YEYIMDQ; -.
DR OrthoDB; 945746at2759; -.
DR PhylomeDB; Q9ZV53; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9ZV53; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZV53; baseline and differential.
DR Genevisible; Q9ZV53; 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:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane; Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..423
FT /note="Putative RING-H2 finger protein ATL49"
FT /id="PRO_0000055777"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 126..168
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 213..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 47287 MW; D305615B04028965 CRC64;
MNKILPEMKS TQNLISSSPP PPLIPLKSNT SLSNLNSKIT PNILLIIIIL SIIFFISGLL
HILVKFLLTP SRESREDYFD NVTALQGQLQ QLFNLHDSGV DQSLIDTLPV FHYKSIVGLK
ISPFDCPVCL CEFETEDKLR LLPKCSHAFH VECIDTWLLS HSTCPLCRSN LLSGFSSHHN
LSSSYLLVLE SEQSSRDMVP VLESNSQLGY DVNNDSESTR IRSGRKSCDP DGDMDGLDEK
VVPLEVKLGK FRNIDHVGEG SDQKKNSISG NSKNVDGRRC LSMGSYEYIM DQEATLKVHV
STKKLSGKDR VPSHRTVMSE CGFDPTVKGI EKSVVERESF SLSKIWLRGK KEKQKGTSAR
DSDCSFVSSS SLRFPNHRIP PEESLKSENS ESLETKTPSF ARRTMHWLAG RQNKIVQPST
SNV
