BAH1L_ARATH
ID BAH1L_ARATH Reviewed; 335 AA.
AC Q8GW10; Q9ZV14;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Probable E3 ubiquitin-protein ligase BAH1-like;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING finger protein 178;
DE AltName: Full=RING-type E3 ubiquitin transferase BAH1-like {ECO:0000305};
GN Name=RF178; OrderedLocusNames=At2g38920; ORFNames=T7F6.9;
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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to sequences.;
CC Name=1;
CC IsoId=Q8GW10-1; Sequence=Displayed;
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme.
CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC79605.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC005770; AAC79605.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09612.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62802.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62803.1; -; Genomic_DNA.
DR EMBL; AK119158; BAC43727.1; -; mRNA.
DR EMBL; BT006237; AAP12886.1; -; mRNA.
DR PIR; A84811; A84811.
DR RefSeq; NP_001324931.1; NM_001336750.1. [Q8GW10-1]
DR RefSeq; NP_001324932.1; NM_001336749.1. [Q8GW10-1]
DR RefSeq; NP_181426.2; NM_129450.3. [Q8GW10-1]
DR AlphaFoldDB; Q8GW10; -.
DR SMR; Q8GW10; -.
DR STRING; 3702.AT2G38920.1; -.
DR PaxDb; Q8GW10; -.
DR PRIDE; Q8GW10; -.
DR EnsemblPlants; AT2G38920.1; AT2G38920.1; AT2G38920. [Q8GW10-1]
DR EnsemblPlants; AT2G38920.5; AT2G38920.5; AT2G38920. [Q8GW10-1]
DR EnsemblPlants; AT2G38920.6; AT2G38920.6; AT2G38920. [Q8GW10-1]
DR GeneID; 818477; -.
DR Gramene; AT2G38920.1; AT2G38920.1; AT2G38920. [Q8GW10-1]
DR Gramene; AT2G38920.5; AT2G38920.5; AT2G38920. [Q8GW10-1]
DR Gramene; AT2G38920.6; AT2G38920.6; AT2G38920. [Q8GW10-1]
DR KEGG; ath:AT2G38920; -.
DR Araport; AT2G38920; -.
DR TAIR; locus:2064935; AT2G38920.
DR eggNOG; ENOG502QQHB; Eukaryota.
DR InParanoid; Q8GW10; -.
DR OMA; LCQCQSC; -.
DR OrthoDB; 878914at2759; -.
DR PhylomeDB; Q8GW10; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8GW10; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GW10; baseline and differential.
DR Genevisible; Q8GW10; AT.
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; IPR033326; BAH1.
DR InterPro; IPR004331; SPX_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46764; PTHR46764; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS51382; SPX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..335
FT /note="Probable E3 ubiquitin-protein ligase BAH1-like"
FT /id="PRO_0000398777"
FT DOMAIN 1..163
FT /note="SPX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00714"
FT ZN_FING 231..280
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 335 AA; 38859 MW; A0E2ACF104DE657F CRC64;
MKFGETFTEY LHGEEEWFLE KCRFVEYKKL KKVLKKCKTC NSTKSDDGQI IPSATSSSLS
DSCECKACPW CDQMFFEELM KEATDIAGFF RSRVRHLLHL HVATGMQRYM IRLRRCFTDE
KQALVQEGQI LIQYITMNAI AIRKILKKYD KVHSSENGKN FKLKMRAERI ELLHSPWLIE
LGAFYLNSGL DNVGNFKNSF GRVACENLNE DQPVLKLMLP NSIELEYDLT CAICLETVFN
PYALKCGHIF CNSCACSAAS VLIFQGIKAA PRHSKCPICR EAGVYAEAVH MIELHLLLKT
RSKEYWKERM MNERSEMVKQ SKMFWNEQTK HMIGY
