HCS2_ARATH
ID HCS2_ARATH Reviewed; 329 AA.
AC F4I4W2; Q8S4V5; Q8S4V7; Q9SHR6;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Biotin--protein ligase 2;
DE EC=6.3.4.-;
DE AltName: Full=Holocarboxylase synthetase 2;
GN Name=HCS2; OrderedLocusNames=At1g37150; ORFNames=F28L22.1;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11784724; DOI=10.1074/jbc.m111110200;
RA Denis L., Grossemy M., Douce R., Alban C.;
RT "Molecular characterization of a second copy of holocarboxylase synthetase
RT gene (hcs2) in Arabidopsis thaliana.";
RL J. Biol. Chem. 277:10435-10444(2002).
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18156294; DOI=10.1104/pp.107.111534;
RA Puyaubert J., Denis L., Alban C.;
RT "Dual targeting of Arabidopsis holocarboxylase synthetase1: a small
RT upstream open reading frame regulates translation initiation and protein
RT targeting.";
RL Plant Physiol. 146:478-491(2008).
CC -!- FUNCTION: Seems to have no or limited implication in biotin-dependent
CC carboxylase biotinylation in planta. {ECO:0000269|PubMed:18156294}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4I4W2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4I4W2-2; Sequence=VSP_053917, VSP_053918;
CC -!- TISSUE SPECIFICITY: Highly expressed in seeds. Expressed in roots,
CC leaves, stems, flowers and siliques. {ECO:0000269|PubMed:11784724}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:18156294}.
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF19230.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF414938; AAL93109.1; -; mRNA.
DR EMBL; AF414941; AAL93112.1; -; mRNA.
DR EMBL; AC007505; AAF19230.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31896.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31897.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58157.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58160.1; -; Genomic_DNA.
DR PIR; G86490; G86490.
DR RefSeq; NP_001320613.1; NM_001333189.1. [F4I4W2-2]
DR RefSeq; NP_001320616.1; NM_001333190.1. [F4I4W2-2]
DR RefSeq; NP_850957.1; NM_180626.2. [F4I4W2-1]
DR RefSeq; NP_850958.1; NM_180627.2. [F4I4W2-2]
DR AlphaFoldDB; F4I4W2; -.
DR SMR; F4I4W2; -.
DR STRING; 3702.AT1G37150.2; -.
DR PaxDb; F4I4W2; -.
DR PRIDE; F4I4W2; -.
DR ProteomicsDB; 247352; -. [F4I4W2-1]
DR EnsemblPlants; AT1G37150.2; AT1G37150.2; AT1G37150. [F4I4W2-1]
DR EnsemblPlants; AT1G37150.3; AT1G37150.3; AT1G37150. [F4I4W2-2]
DR EnsemblPlants; AT1G37150.7; AT1G37150.7; AT1G37150. [F4I4W2-2]
DR EnsemblPlants; AT1G37150.8; AT1G37150.8; AT1G37150. [F4I4W2-2]
DR GeneID; 840632; -.
DR Gramene; AT1G37150.2; AT1G37150.2; AT1G37150. [F4I4W2-1]
DR Gramene; AT1G37150.3; AT1G37150.3; AT1G37150. [F4I4W2-2]
DR Gramene; AT1G37150.7; AT1G37150.7; AT1G37150. [F4I4W2-2]
DR Gramene; AT1G37150.8; AT1G37150.8; AT1G37150. [F4I4W2-2]
DR KEGG; ath:AT1G37150; -.
DR Araport; AT1G37150; -.
DR TAIR; locus:2029642; AT1G37150.
DR eggNOG; KOG1536; Eukaryota.
DR InParanoid; F4I4W2; -.
DR OMA; NIANSKP; -.
DR PRO; PR:F4I4W2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I4W2; baseline and differential.
DR Genevisible; F4I4W2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IBA:GO_Central.
DR CDD; cd16442; BPL; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR003142; BPL_C.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR Pfam; PF02237; BPL_C; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00121; birA_ligase; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Ligase; Reference proteome.
FT CHAIN 1..329
FT /note="Biotin--protein ligase 2"
FT /id="PRO_0000425973"
FT DOMAIN 67..251
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT BINDING 84..85
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250"
FT BINDING 111..113
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250"
FT VAR_SEQ 292..297
FT /note="GLTSSG -> LLEMTM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11784724"
FT /id="VSP_053917"
FT VAR_SEQ 298..329
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11784724"
FT /id="VSP_053918"
FT CONFLICT 266
FT /note="W -> C (in Ref. 1; AAL93109)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="R -> K (in Ref. 1; AAL93109)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="V -> I (in Ref. 1; AAL93109)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 37152 MW; B233D4D4EA3B7AFA CRC64;
MDIDASCSLV LYGKSSVETD TATRLKNNNV LKLPDNSKVS IFLQSEIKNL VRDDDSSFNL
SLFMNSISTH RFGRFLIWSP YLSSTHDVVS HNFSEIPVGS VCVSDIQLKG RGRTKNVWES
PKGCLMYSFT LEMEDGRVVP LIQYVVSLAV TEAVKDVCDK KGLSYNDVKI KWPNDLYLNG
LKIGGILCTS TYRSRKFLVS VGVGLNVDNE QPTTCLNAVL KDVCPPSNLL KREEILGAFF
KKFENFFDLF MEQGFKSLEE LYYRTWLHSG QRVIAEEKNE DQVVQNVVTI QGLTSSGYLL
AIGDDNVMYE LHPDGNSFDF FKGLVRRKL
