MSBP1_ARATH
ID MSBP1_ARATH Reviewed; 220 AA.
AC Q9XFM6; Q9LTJ7;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Membrane steroid-binding protein 1;
DE Short=AtMP1;
DE AltName: Full=Membrane-associated progesterone-binding protein 5 {ECO:0000303|Ref.7};
DE Short=AtMAPR5 {ECO:0000303|Ref.7};
GN Name=MSBP1; Synonyms=MAPR5 {ECO:0000303|Ref.7}, MP1;
GN OrderedLocusNames=At5g52240; ORFNames=F17P19.14;
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 [MRNA], CHARACTERIZATION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BAK1.
RX PubMed=19532123; DOI=10.1038/cr.2009.66;
RA Song L., Shi Q.M., Yang X.H., Xu Z.H., Xue H.W.;
RT "Membrane steroid-binding protein 1 (MSBP1) negatively regulates
RT brassinosteroid signaling by enhancing the endocytosis of BAK1.";
RL Cell Res. 19:864-876(2009).
CC -!- FUNCTION: MSBP1 can bind to multiple steroid compounds with different
CC affinities. Negatively regulates cell elongation and brassinosteroid
CC signaling. May act as a coreceptor with BAK1 and enhances its
CC endocytosis. {ECO:0000269|PubMed:19532123}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=Kinetic studies indicated that MSBP1 has highest affinity to
CC progesterone, followed by 5-alpha-dihydrotestosterone, 24-epi-
CC brassinolide and stigmasterol.;
CC -!- SUBUNIT: Interacts with BAK1 (via extracellular region).
CC {ECO:0000269|PubMed:19532123}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}. Endosome membrane {ECO:0000305};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9XFM6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, stems, roots, leaves,
CC flower and silique stalks, pistils and stigmas, but not in anthers.
CC {ECO:0000269|PubMed:15608331}.
CC -!- DEVELOPMENTAL STAGE: Expressed under darkness or light during initial
CC stages of germination. Highly expressed in hypocotyls during days 3 to
CC 7 after germination under light but almost undetectable in darkness.
CC -!- INDUCTION: Not induced by phytohormones and strongly suppressed in
CC darkness.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved iron-
CC binding His residues at positions 109 and 133. {ECO:0000305}.
CC -!- MISCELLANEOUS: Regulated by both phytochromes and cryptochromes.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC {ECO:0000305}.
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DR EMBL; AF153284; AAD34616.1; -; mRNA.
DR EMBL; AB025603; BAA97467.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96190.1; -; Genomic_DNA.
DR EMBL; BT000922; AAN41322.1; -; mRNA.
DR EMBL; AY086811; AAM63860.1; -; mRNA.
DR RefSeq; NP_200037.1; NM_124603.4. [Q9XFM6-1]
DR AlphaFoldDB; Q9XFM6; -.
DR SMR; Q9XFM6; -.
DR BioGRID; 20545; 57.
DR IntAct; Q9XFM6; 52.
DR STRING; 3702.AT5G52240.1; -.
DR iPTMnet; Q9XFM6; -.
DR PaxDb; Q9XFM6; -.
DR PRIDE; Q9XFM6; -.
DR ProteomicsDB; 250873; -. [Q9XFM6-1]
DR EnsemblPlants; AT5G52240.1; AT5G52240.1; AT5G52240. [Q9XFM6-1]
DR GeneID; 835300; -.
DR Gramene; AT5G52240.1; AT5G52240.1; AT5G52240. [Q9XFM6-1]
DR KEGG; ath:AT5G52240; -.
DR Araport; AT5G52240; -.
DR TAIR; locus:2145101; AT5G52240.
DR eggNOG; KOG1110; Eukaryota.
DR HOGENOM; CLU_042860_0_2_1; -.
DR InParanoid; Q9XFM6; -.
DR OrthoDB; 1331617at2759; -.
DR PhylomeDB; Q9XFM6; -.
DR PRO; PR:Q9XFM6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XFM6; baseline and differential.
DR Genevisible; Q9XFM6; AT.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; 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; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005496; F:steroid binding; IDA:TAIR.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:TAIR.
DR GO; GO:1901141; P:regulation of lignin biosynthetic process; IMP:TAIR.
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 Alternative splicing; Cell membrane; Endosome; Lipid-binding; Membrane;
KW Reference proteome; Signal-anchor; Steroid-binding; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..220
FT /note="Membrane steroid-binding protein 1"
FT /id="PRO_0000121748"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 74..171
FT /note="Cytochrome b5 heme-binding"
FT REGION 74..171
FT /note="Steroid-binding"
FT /evidence="ECO:0000250"
FT REGION 174..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 142
FT /note="V -> I (in Ref. 2; AAD34616 and 6; AAM63860)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="G -> E (in Ref. 2; AAD34616 and 6; AAM63860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 220 AA; 24405 MW; 6374B26784579FB8 CRC64;
MALELWQTLK EAIHAYTGLS PVVFFTALAL AFAIYQVISG WFASPFDDVN RHQRARSLAQ
EEEPPIPQPV QVGEITEEEL KQYDGSDPQK PLLMAIKHQI YDVTQSRMFY GPGGPYALFA
GKDASRALAK MSFEEKDLTW DVSGLGPFEL DALQDWEYKF MSKYAKVGTV KVAGSEPETA
SVSEPTENVE QDAHVTTTPG KTVVDKSDDA PAETVLKKEE
