ATL81_ARATH
ID ATL81_ARATH Reviewed; 332 AA.
AC Q9LQM2; Q1G3T2;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=RING-H2 finger protein ATL81;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase ATL81 {ECO:0000305};
DE Flags: Precursor;
GN Name=ATL81; OrderedLocusNames=At1g32361; ORFNames=F27G20.11, F5D14.13;
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=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 GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17229318; DOI=10.1186/1471-2164-8-18;
RA Moskal W.A. Jr., Wu H.C., Underwood B.A., Wang W., Town C.D., Xiao Y.-L.;
RT "Experimental validation of novel genes predicted in the un-annotated
RT regions of the Arabidopsis genome.";
RL BMC Genomics 8:18-18(2007).
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).
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; AC007767; AAF81333.1; -; Genomic_DNA.
DR EMBL; AC084110; AAG60172.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31469.1; -; Genomic_DNA.
DR EMBL; DQ487502; ABF59330.1; -; Genomic_DNA.
DR EMBL; EF183179; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; E86448; E86448.
DR RefSeq; NP_001117398.1; NM_001123926.1.
DR AlphaFoldDB; Q9LQM2; -.
DR SMR; Q9LQM2; -.
DR STRING; 3702.AT1G32361.1; -.
DR PaxDb; Q9LQM2; -.
DR PRIDE; Q9LQM2; -.
DR ProteomicsDB; 246651; -.
DR EnsemblPlants; AT1G32361.1; AT1G32361.1; AT1G32361.
DR GeneID; 6240625; -.
DR Gramene; AT1G32361.1; AT1G32361.1; AT1G32361.
DR KEGG; ath:AT1G32361; -.
DR Araport; AT1G32361; -.
DR TAIR; locus:4515102621; AT1G32361.
DR eggNOG; KOG0800; Eukaryota.
DR HOGENOM; CLU_035191_3_1_1; -.
DR InParanoid; Q9LQM2; -.
DR OMA; LYCVRGT; -.
DR OrthoDB; 1010823at2759; -.
DR PhylomeDB; Q9LQM2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LQM2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQM2; 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; 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 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..332
FT /note="RING-H2 finger protein ATL81"
FT /id="PRO_0000030702"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 154..196
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 332 AA; 38390 MW; C93348BA5D48ECBF CRC64;
MYDLTFLLIS LFPIDITLPT RQPQNKPFLL PQATYETSHN ISDPAVSLHG LKMSISTTET
DNFKPVHTLV SSPVTIVLTG SLLFIIFTGF FSFFFCGCLF RKLMRIWNNH RNRNRPSNLI
QPSNPPENLG LDSKIIESFP EYPYSVKDHG TDQCSICLTE FMDDDTIRLI STCNHSFHTI
CIDLWFEGHK TCPVCRRELD VEDRTSLEKP LEVPEIDLVR SEIHDEPLPR DTVTIIVHEE
HPSTTIGSLE HTDEIESYER RMKASNLRFW RSHSTGHSIV VKTENEQEEE EEEEKDEIKI
RIEISGECQF EDHKMTLPNR KLYCVRGTYS VG
