SBP3_ARATH
ID SBP3_ARATH Reviewed; 100 AA.
AC Q9SK39;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Probable steroid-binding protein 3;
DE Short=AtMP3;
DE AltName: Full=Membrane-associated progesterone-binding protein 2 {ECO:0000303|Ref.5};
DE Short=AtMAPR2 {ECO:0000303|Ref.5};
GN Name=MP3; Synonyms=MAPR2 {ECO:0000303|Ref.5}; OrderedLocusNames=At2g24940;
GN ORFNames=F27C12.14;
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=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
RN [5]
RP INDUCTION, AND NOMENCLATURE.
RA Kao A.L., Chang T.Y., Chang S.H., Su J.C., Yang C.C.;
RT "Characterization of a novel Arabidopsis protein family AtMAPR homologous
RT to 25-Dx/IZAg/Hpr6.6 proteins.";
RL Bot. Bull. Acad. Sin. 46:107-118(2005).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=15608331; DOI=10.1105/tpc.104.028381;
RA Yang X.-H., Xu Z.-H., Xue H.-W.;
RT "Arabidopsis membrane steroid binding protein 1 is involved in inhibition
RT of cell elongation.";
RL Plant Cell 17:116-131(2005).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [8]
RP STRUCTURE BY NMR OF 1-100.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of an Arabidopsis homologue of the mammalian membrane-
RT associated progesterone receptor.";
RL Submitted (DEC-2003) to the PDB data bank.
RN [9]
RP STRUCTURE BY NMR OF 1-100.
RX PubMed=15702529; DOI=10.1023/b:jnmr.0000048943.34504.29;
RA Song J., Vinarov D., Tyler E.M., Shahan M.N., Tyler R.C., Markley J.L.;
RT "Hypothetical protein At2g24940.1 from Arabidopsis thaliana has a
RT cytochrome b5 like fold.";
RL J. Biomol. NMR 30:215-218(2004).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:15608331}.
CC -!- INDUCTION: Down-regulated by auxin and cytokinin. {ECO:0000269|Ref.5}.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved iron-
CC binding His residues at positions 37 and 61. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC {ECO:0000305}.
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DR EMBL; AC006585; AAD23019.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07640.1; -; Genomic_DNA.
DR EMBL; BT002446; AAO00806.1; -; mRNA.
DR EMBL; BT008438; AAP37797.1; -; mRNA.
DR EMBL; AY084294; AAM60885.1; -; mRNA.
DR PIR; C84642; C84642.
DR RefSeq; NP_001318286.1; NM_001335965.1.
DR PDB; 1J03; NMR; -; A=1-100.
DR PDB; 1T0G; NMR; -; A=2-100.
DR PDBsum; 1J03; -.
DR PDBsum; 1T0G; -.
DR AlphaFoldDB; Q9SK39; -.
DR BMRB; Q9SK39; -.
DR SMR; Q9SK39; -.
DR BioGRID; 2384; 33.
DR IntAct; Q9SK39; 32.
DR STRING; 3702.AT2G24940.1; -.
DR iPTMnet; Q9SK39; -.
DR MetOSite; Q9SK39; -.
DR PaxDb; Q9SK39; -.
DR PRIDE; Q9SK39; -.
DR ProteomicsDB; 226649; -.
DR EnsemblPlants; AT2G24940.1; AT2G24940.1; AT2G24940.
DR GeneID; 817032; -.
DR Gramene; AT2G24940.1; AT2G24940.1; AT2G24940.
DR KEGG; ath:AT2G24940; -.
DR Araport; AT2G24940; -.
DR TAIR; locus:2047401; AT2G24940.
DR eggNOG; KOG1110; Eukaryota.
DR HOGENOM; CLU_042860_3_1_1; -.
DR InParanoid; Q9SK39; -.
DR OMA; PDWYDLD; -.
DR OrthoDB; 1532459at2759; -.
DR PhylomeDB; Q9SK39; -.
DR EvolutionaryTrace; Q9SK39; -.
DR PRO; PR:Q9SK39; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SK39; baseline and differential.
DR Genevisible; Q9SK39; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR Pfam; PF00173; Cyt-b5; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Lipid-binding; Nucleus; Reference proteome;
KW Steroid-binding.
FT CHAIN 1..100
FT /note="Probable steroid-binding protein 3"
FT /id="PRO_0000121750"
FT DOMAIN 1..82
FT /note="Cytochrome b5 heme-binding"
FT REGION 1..82
FT /note="Sterol-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1T0G"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:1J03"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1J03"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:1J03"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:1J03"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1J03"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:1J03"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1J03"
FT TURN 43..49
FT /evidence="ECO:0007829|PDB:1J03"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:1J03"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1J03"
FT HELIX 75..89
FT /evidence="ECO:0007829|PDB:1J03"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1J03"
SQ SEQUENCE 100 AA; 11031 MW; 3CDB7DDEC1E7D3AE CRC64;
MEFTAEQLSQ YNGTDESKPI YVAIKGRVFD VTTGKSFYGS GGDYSMFAGK DASRALGKMS
KNEEDVSPSL EGLTEKEINT LNDWETKFEA KYPVVGRVVS
