BTSL2_ARATH
ID BTSL2_ARATH Reviewed; 1259 AA.
AC F4HVS0; Q0WVS5; Q9SSG0; Q9SSG1;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Zinc finger protein BRUTUS-like At1g74770 {ECO:0000305};
GN OrderedLocusNames=At1g74770 {ECO:0000312|Araport:AT1G74770};
GN ORFNames=F25A4.26 {ECO:0000312|EMBL:AAD55299.1},
GN F25A4.27 {ECO:0000312|EMBL:AAD55300.1};
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), GENE FAMILY, AND NOMENCLATURE.
RC TISSUE=Flower, Leaf, and 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=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 [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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 71-1259 (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable E3 ubiquitin-protein ligase that may regulate the
CC response to iron deficiency and thus contributes to iron homeostasis.
CC {ECO:0000250|UniProtKB:Q8LPQ5}.
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Binds zinc and iron ions. {ECO:0000250|UniProtKB:Q8LPQ5}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q8LPQ5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4HVS0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4HVS0-2; Sequence=VSP_058561;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55299.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ086838; AAZ14062.1; -; mRNA.
DR EMBL; AC008263; AAD55299.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC008263; AAD55300.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35630.1; -; Genomic_DNA.
DR EMBL; BT011670; AAS47676.1; -; mRNA.
DR EMBL; AK226665; BAE98773.1; -; mRNA.
DR PIR; A96777; A96777.
DR PIR; H96776; H96776.
DR RefSeq; NP_177615.2; NM_106135.3. [F4HVS0-1]
DR AlphaFoldDB; F4HVS0; -.
DR SMR; F4HVS0; -.
DR IntAct; F4HVS0; 1.
DR STRING; 3702.AT1G74770.1; -.
DR iPTMnet; F4HVS0; -.
DR PaxDb; F4HVS0; -.
DR PRIDE; F4HVS0; -.
DR EnsemblPlants; AT1G74770.1; AT1G74770.1; AT1G74770. [F4HVS0-1]
DR GeneID; 843816; -.
DR Gramene; AT1G74770.1; AT1G74770.1; AT1G74770. [F4HVS0-1]
DR KEGG; ath:AT1G74770; -.
DR Araport; AT1G74770; -.
DR TAIR; locus:2027176; AT1G74770.
DR eggNOG; KOG1940; Eukaryota.
DR HOGENOM; CLU_003967_0_0_1; -.
DR InParanoid; F4HVS0; -.
DR OMA; LFRECFS; -.
DR OrthoDB; 1303946at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:F4HVS0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HVS0; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IGI:TAIR.
DR GO; GO:0033212; P:iron import into cell; IMP:TAIR.
DR GO; GO:0098711; P:iron ion import across plasma membrane; IMP:TAIR.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0034756; P:regulation of iron ion transport; IMP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR012312; Hemerythrin-like.
DR InterPro; IPR039512; RCHY1_zinc-ribbon.
DR InterPro; IPR008913; Znf_CHY.
DR InterPro; IPR037274; Znf_CHY_sf.
DR InterPro; IPR017921; Znf_CTCHY.
DR InterPro; IPR037275; Znf_CTCHY_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01814; Hemerythrin; 1.
DR Pfam; PF05495; zf-CHY; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF14599; zinc_ribbon_6; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF161219; SSF161219; 1.
DR SUPFAM; SSF161245; SSF161245; 1.
DR PROSITE; PS51266; ZF_CHY; 1.
DR PROSITE; PS51270; ZF_CTCHY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Iron; Ligase; Membrane; Metal-binding; Nucleus;
KW Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1259
FT /note="Zinc finger protein BRUTUS-like At1g74770"
FT /id="PRO_0000437682"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 1018..1087
FT /note="CHY-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT ZN_FING 1089..1152
FT /note="CTCHY-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT ZN_FING 1153..1195
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 904..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..933
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1025
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1027
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1038
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1039
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1045
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1048
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1049
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1055
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1067
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1070
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1080
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1085
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1094
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1097
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT SITE 90
FT /note="Required for iron-dependent instability"
FT /evidence="ECO:0000250|UniProtKB:Q8LPQ5"
FT VAR_SEQ 1..1004
FT /note="Missing (in isoform 2)"
FT /id="VSP_058561"
SQ SEQUENCE 1259 AA; 144923 MW; 8F959F4DD9E34E6A CRC64;
MGGGNLHSLP PENASVSASY AVTVGNTKLS DAPVLFFVYC HKAFRAQLVE LRRFATDAAE
ADSFSGDLAV ELSRKFEFLK LVYKYHSAAE DEVIFLALDK RVKNIVSNYS LEHAGTDDLF
TSIFHWLHVL EEEIGSRSDV LREVILCIGT IQSSICQHML KEERQVFPLL IEKFSFREQA
SLVWQFICSV PVMVLEDFLP WMISHLSHEE KIEVENCIKD VAPNEDSLQQ VISSWLLDDS
QSSCGTPTEI MKGVQYVNVS KSLKKSPESH PSSGCFQRFW EWSKKSLSIP NVGRSPIHGL
RLFQNAIEKD LRDIQEGLCQ AKFQTLILDL DVLMARLNFL ADVLVSYSNA FKKFFHPVLE
EMTARRSSTA KQFNIDDCLE NFQRLLYKSA DDKTKTDNFL LQLQEELESL IIQVTKQFAI
QRTEVFPIIS KNCNHEMQKQ LLYTSIHVLP LGLLKCVILW FSAHLSEEES QSILHFLSLE
DSSPKKSFPR LLLQWLRFGY SGKTSVERFW KQLDVMFKVR CSCQKEHTEE ASGSFSNQTQ
LQLCKVSKDV YPRKKDKSST CFMSMDLAVG DMYETPYSSR MNQQMTFSGK LKPPLHLPDF
FGEKNMDDPM IMDVKPIDLL FFFHKAMKMD LDYLVCGSTR LAADFRFLAE FQQRFHMIKF
LYQIHSDAED EIAFPALEAK GQLKNISHSF SIDHELETKH FDKVSFILNE MSELNMLVST
INTTAADHDR KMKYERLCLS LREICKSMHK LLSEHIQHEE TELWGLFRNC FSIEEQEKII
GCMLGRISGE ILQDMIPWLM ESLTSDEQLA AMSLWRQATR KTMFVEWLTE WYNGHVLQEE
AGEANNDPFG DSDPLEIVWK YLFEASADGE KGSMRSSLLK LPKTNFTGIM NQPPPNYKVE
VGKKEEKDLE RSESKKICRG SNQEGDKEQT DKMSQKVSQF GPSKKYEQLL TMSEEELVVV
IKKISCDSSL DPQKKDYIKQ NLLMSRWNIS QRTYNLEPSS LSSNMETVHG QHPSYRDPHS
LIFGCNHYKR NCKLLAPCCD KLFTCIRCHD EEADHSVDRK QITKMMCMKC LLIQPIGANC
SNTSCKSSMG KYFCKICKLY DDERKIYHCP YCNLCRVGKG LGIDYFHCMK CNACMSRTLV
EHVCREKCLE DNCPICHEYI FTSSSPVKAL PCGHLMHSTC FQEYTCSHYT CPVCSKSLGD
MQVYFKMLDA LLAEEKMPDE YSNKTQVILC NDCGRKGNAP YHWLYHKCTT CGSYNSRLL
