XB35_ARATH
ID XB35_ARATH Reviewed; 462 AA.
AC Q4FE47; Q8L9Z0; Q94AX6; Q9LTC1;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Putative E3 ubiquitin-protein ligase XBAT35;
DE EC=2.3.2.27;
DE AltName: Full=Ankyrin repeat domain and RING finger-containing protein XBAT35;
DE AltName: Full=Protein XB3 homolog 5;
DE AltName: Full=RING-type E3 ubiquitin transferase XBAT35;
GN Name=XBAT35; OrderedLocusNames=At3g23280; ORFNames=K14B15.19;
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), AND FUNCTION.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: No E3 ubiquitin-protein ligase activity observed when
CC associated with the E2 enzyme UBC8 in vitro.
CC {ECO:0000269|PubMed:15644464}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4FE47-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4FE47-2; Sequence=VSP_039535;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95741.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ086844; AAZ14068.1; -; mRNA.
DR EMBL; AB025608; BAA95741.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76746.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76747.1; -; Genomic_DNA.
DR EMBL; AY045637; AAK73995.1; -; mRNA.
DR EMBL; AY059650; AAL31143.1; -; mRNA.
DR EMBL; AY088137; AAM65682.1; -; mRNA.
DR RefSeq; NP_566724.1; NM_113229.4. [Q4FE47-1]
DR RefSeq; NP_850628.1; NM_180297.4. [Q4FE47-2]
DR AlphaFoldDB; Q4FE47; -.
DR SMR; Q4FE47; -.
DR BioGRID; 7239; 2.
DR IntAct; Q4FE47; 3.
DR STRING; 3702.AT3G23280.1; -.
DR iPTMnet; Q4FE47; -.
DR PaxDb; Q4FE47; -.
DR PRIDE; Q4FE47; -.
DR ProteomicsDB; 242396; -. [Q4FE47-1]
DR EnsemblPlants; AT3G23280.1; AT3G23280.1; AT3G23280. [Q4FE47-1]
DR EnsemblPlants; AT3G23280.2; AT3G23280.2; AT3G23280. [Q4FE47-2]
DR GeneID; 821907; -.
DR Gramene; AT3G23280.1; AT3G23280.1; AT3G23280. [Q4FE47-1]
DR Gramene; AT3G23280.2; AT3G23280.2; AT3G23280. [Q4FE47-2]
DR KEGG; ath:AT3G23280; -.
DR Araport; AT3G23280; -.
DR TAIR; locus:2086263; AT3G23280.
DR eggNOG; ENOG502S3SA; Eukaryota.
DR InParanoid; Q4FE47; -.
DR OMA; SLFCGWM; -.
DR OrthoDB; 896321at2759; -.
DR PhylomeDB; Q4FE47; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q4FE47; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q4FE47; baseline and differential.
DR Genevisible; Q4FE47; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00023; Ank; 2.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ANK repeat; Metal-binding; Reference proteome;
KW Repeat; Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..462
FT /note="Putative E3 ubiquitin-protein ligase XBAT35"
FT /id="PRO_0000395743"
FT REPEAT 6..35
FT /note="ANK 1"
FT REPEAT 39..69
FT /note="ANK 2"
FT REPEAT 75..104
FT /note="ANK 3"
FT ZN_FING 411..450
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 277..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..293
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 222..246
FT /note="IPSRRMKKRRVCASHGRRRPQVVRQ -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_039535"
FT CONFLICT 21
FT /note="E -> G (in Ref. 4; AAM65682)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="F -> L (in Ref. 4; AAM65682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 50055 MW; F489217368DD39CD CRC64;
MGQQQSKGEL LYQQVSYGNS EGIRALHRDG GDLEWMDREG KTPLILACMN SELFDVAKTL
IELGSNVNAY RPGRHAGTPL HHAAKRGLEN TVKLLLSHGA NPLVLNDDCQ TPLEVARVKG
FSNVVRAIEK HICLFSGWMR EFYGPTFLDL FAPQLLSRRV WVVIVPTGSR NPTKPFKLEL
VVYASLQDAQ PRTVMPLWKA NLEEPKAKQS DTSVMIVDNS TIPSRRMKKR RVCASHGRRR
PQVVRQTRLK FAPSTEGDSQ QLKWFCDACK GIPQPMHPPV FLQAPPSAPP PPSEDGLAMG
MNASLHTTMS DPSNLNHHSI GQASSSSGPS SSTAPPSGKA SAFGFNSHGI GIVLESSPSA
PPLTDDDIAT VDDGPIHYPS IDSTPVDLPS AASLPASTEG ERKEDGNTGT CAICLDAPSE
AVCVPCGHVA GCMSCLKEIK SKNWGCPVCR AKIDQVIKLY RV
