MSBP2_ARATH
ID MSBP2_ARATH Reviewed; 233 AA.
AC Q9M2Z4; Q9XFM5;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Membrane steroid-binding protein 2;
DE Short=AtMP2;
DE AltName: Full=Membrane-associated progesterone-binding protein 3 {ECO:0000303|Ref.5};
DE Short=AtMAPR3 {ECO:0000303|Ref.5};
GN Name=MSBP2; Synonyms=MAPR3, MP2; OrderedLocusNames=At3g48890;
GN ORFNames=T21J18.160 {ECO:0000312|EMBL:CAB87917.1};
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].
RC STRAIN=cv. Columbia;
RA Choi J.H., Choi H., Gray P.;
RT "Plant homologues of mammalian putative progesterone-binding membrane
RT proteins.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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 [5]
RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved iron-
CC binding His residues at positions 105 and 129. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34615.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF153283; AAD34615.1; ALT_FRAME; mRNA.
DR EMBL; AL132963; CAB87917.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78470.1; -; Genomic_DNA.
DR EMBL; AY079104; AAL84988.1; -; mRNA.
DR EMBL; AF419567; AAL31899.1; -; mRNA.
DR PIR; T49285; T49285.
DR RefSeq; NP_190458.1; NM_114748.3.
DR AlphaFoldDB; Q9M2Z4; -.
DR SMR; Q9M2Z4; -.
DR BioGRID; 9368; 98.
DR IntAct; Q9M2Z4; 95.
DR STRING; 3702.AT3G48890.1; -.
DR iPTMnet; Q9M2Z4; -.
DR PaxDb; Q9M2Z4; -.
DR PRIDE; Q9M2Z4; -.
DR ProteomicsDB; 239000; -.
DR EnsemblPlants; AT3G48890.1; AT3G48890.1; AT3G48890.
DR GeneID; 824050; -.
DR Gramene; AT3G48890.1; AT3G48890.1; AT3G48890.
DR KEGG; ath:AT3G48890; -.
DR Araport; AT3G48890; -.
DR TAIR; locus:2099453; AT3G48890.
DR eggNOG; KOG1110; Eukaryota.
DR HOGENOM; CLU_042860_0_2_1; -.
DR InParanoid; Q9M2Z4; -.
DR OMA; AITHDET; -.
DR OrthoDB; 1331617at2759; -.
DR PhylomeDB; Q9M2Z4; -.
DR PRO; PR:Q9M2Z4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2Z4; baseline and differential.
DR Genevisible; Q9M2Z4; AT.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
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 Cell membrane; Lipid-binding; Membrane; Phosphoprotein; Reference proteome;
KW Steroid-binding; Transmembrane; Transmembrane helix.
FT CHAIN 1..233
FT /note="Membrane steroid-binding protein 2"
FT /id="PRO_0000121749"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 70..167
FT /note="Cytochrome b5 heme-binding"
FT REGION 70..167
FT /note="Steroid-binding"
FT /evidence="ECO:0000250"
FT REGION 169..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 225
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 233 AA; 25382 MW; CA055230BFB7040A CRC64;
MVQQIWETLK ETITAYTGLS PAAFFTVLAL AFAVYQVVSG FFVSPEVHRP RSLEVQPQSE
PLPPPVQLGE ITEEELKLYD GSDSKKPLLM AIKGQIYDVS QSRMFYGPGG PYALFAGKDA
SRALAKMSFE DQDLTGDISG LGAFELEALQ DWEYKFMSKY VKVGTIQKKD GEGKESSEPS
EAKTASAEGL STNTGEEASA ITHDETSRST GEKIAETTEK KDVATDDDDA AKE
