BTSL1_ARATH
ID BTSL1_ARATH Reviewed; 1254 AA.
AC F4IDY5; Q67YB6; Q9LMD9;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Zinc finger protein BRUTUS-like At1g18910 {ECO:0000305};
GN OrderedLocusNames=At1g18910 {ECO:0000312|Araport:AT1G18910};
GN ORFNames=F14D16.3 {ECO:0000312|EMBL:AAF79306.1};
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 [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 MRNA] OF 1163-1254.
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INDUCTION BY IRON DEFICIENCY.
RX PubMed=15539473; DOI=10.1105/tpc.104.024315;
RA Colangelo E.P., Guerinot M.L.;
RT "The essential basic helix-loop-helix protein FIT1 is required for the iron
RT deficiency response.";
RL Plant Cell 16:3400-3412(2004).
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 -!- INDUCTION: Induced by iron deficiency. {ECO:0000269|PubMed:15539473}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79306.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC068602; AAF79306.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29781.1; -; Genomic_DNA.
DR EMBL; AK176552; BAD44315.1; -; mRNA.
DR PIR; A86323; A86323.
DR RefSeq; NP_173325.2; NM_101748.3.
DR AlphaFoldDB; F4IDY5; -.
DR SMR; F4IDY5; -.
DR STRING; 3702.AT1G18910.1; -.
DR PaxDb; F4IDY5; -.
DR PRIDE; F4IDY5; -.
DR EnsemblPlants; AT1G18910.1; AT1G18910.1; AT1G18910.
DR GeneID; 838472; -.
DR Gramene; AT1G18910.1; AT1G18910.1; AT1G18910.
DR KEGG; ath:AT1G18910; -.
DR Araport; AT1G18910; -.
DR TAIR; locus:2011266; AT1G18910.
DR eggNOG; KOG1940; Eukaryota.
DR HOGENOM; CLU_003967_0_0_1; -.
DR InParanoid; F4IDY5; -.
DR OMA; DPLDIVW; -.
DR OrthoDB; 1303946at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:F4IDY5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IDY5; 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:0010106; P:cellular response to iron ion starvation; IEP:UniProtKB.
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:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0034756; P:regulation of iron ion transport; IMP:TAIR.
DR GO; GO:0010039; P:response to iron ion; IGI:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:TAIR.
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 Iron; Ligase; Membrane; Metal-binding; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..1254
FT /note="Zinc finger protein BRUTUS-like At1g18910"
FT /id="PRO_0000437681"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 1013..1082
FT /note="CHY-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT ZN_FING 1084..1147
FT /note="CTCHY-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT ZN_FING 1148..1190
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1020
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1022
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1033
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1034
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1040
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1043
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1044
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1050
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1062
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1065
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601"
FT BINDING 1075
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 1089
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1092
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT BINDING 1139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965"
FT SITE 98
FT /note="Required for iron-dependent instability"
FT /evidence="ECO:0000250|UniProtKB:Q8LPQ5"
SQ SEQUENCE 1254 AA; 144092 MW; 3A3C588AAF083978 CRC64;
MGVGDPLPLP PEKNRREVNK PPDIASTSSS SASAVNNARL SDAPILLFVY FHKAFRAQLA
ELQFLAGDTV RSGSDLAVEL RSKFEFLKLV YKYHSAAEDE VIFSALDTRV KNIVFNYSLE
HDATDDLFTS VFHWLNVLEE EQGNRADVLR EVVLCIGTIQ SSICQHMLKE ERQVFPLMIE
NFSFEEQASL VWQFICSVPV MVLEEIFPWM TSLLSPKEKS EVETCFKEVV PNELSLQLVI
NSWLIDDSQS SLTALTKIMK GVQSVEVSEN MTNSQTNSSS SGVFQRFWQW SKKMSFSSPN
TGHILVHGIH LWHNAIRKDL VDIQKGLCQL TFPSLSLDLN VLVVRLNFLA DVLIFYSNAF
KTFFYPVFED MVDQQHSSSS KQFTIDGHVE NFKKSLDLET RAGSDNFVIT LQEKLESLIL
TVAKQFSIEE TEVFPIISKN CNIEMQRQLL YRSIHFLPLG LLKCVIMWFS AQLPEDECQS
IIHYLSSEDS FPNKPFAHLL LQWFRFGYSG KTPVESFWNE LSFMFKPRCS FEEELTEEAS
GSFFQQSPQK LFKVSDPYSM DPPAGYMNET PYSSAMNQQI LIPGKLRPLL HLPDLFGDKT
IGEHLTMDLK PIDLIFYFHK AMKKDLDYLV RGSARLATDY SFLGEFQQRF HLIKFLYQIH
SDAEDEIAFP ALEAKGKLQN ISQSYSIDHE LEVEHLNKVS FLLNELAELN MLVLDHKNVK
YEKLCMSLQD ICKSIHKLLS EHLHREETEL WCLFRDCFTI EEQEKIIACM LGRISGEILQ
DMIPWLMESL IPDEQHAVMS LWRQATRKTM FGEWLTEWYN SHAVEEETEE ANKDPSENSD
PLDVVWSYLF EGAADEYKGS ICSKPLEETE LKGIMNKPLG KAAPNNKVEF GNKEENHLEI
SGSKKVCTGA DETKYKEQTD SNAQAFQMSH NTSQSGQDSR YECLLSMSQE DVEATIRRIS
RDSSLDPQKK SYIIQNLLMS RWIATQRIYN LEPSILSSNR EAVPGQNPSY RDPHKLIFGC
KHYKRSCKLL APCCNKLYTC IRCHDEEVDH LLDRKQITKM MCMKCMIIQP VGASCSNISC
SSSMGKYYCK ICKLFDDDRE IYHCPYCNLC RLGKGLSIDY FHCMKCNACM SRLIVEHVCR
EKCLEDNCPI CHEYIFTSNS PVKALPCGHV MHSTCFQEYT CSHYTCPICS KSLGDMQVYF
RMLDALLAEQ KMPDEYLNQT QVILCNDCGR KGNAPYHWLY HKCSSCASYN TRLF
