MSBP1_ORYSJ
ID MSBP1_ORYSJ Reviewed; 232 AA.
AC Q9FVZ7; A3C684; Q337F5;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Membrane steroid-binding protein 1 {ECO:0000303|PubMed:25711711};
DE Short=OsMSBP1 {ECO:0000303|PubMed:25711711};
DE AltName: Full=OsMSBP2 {ECO:0000303|PubMed:17512025};
GN Name=MSBP1 {ECO:0000303|PubMed:25711711};
GN OrderedLocusNames=Os10g0502600 {ECO:0000312|EMBL:BAF26907.1},
GN LOC_Os10g35870 {ECO:0000312|EMBL:ABB47845.2};
GN ORFNames=OSJNBb0073N24.4 {ECO:0000312|EMBL:AAG13629.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17512025; DOI=10.1016/j.phytochem.2007.04.002;
RA Iino M., Nomura T., Tamaki Y., Yamada Y., Yoneyama K., Takeuchi Y.,
RA Mori M., Asami T., Nakano T., Yokota T.;
RT "Progesterone: its occurrence in plants and involvement in plant growth.";
RL Phytochemistry 68:1664-1673(2007).
RN [8]
RP FUNCTION, AND INTERACTION WITH SERL2.
RX PubMed=25711711; DOI=10.1093/jxb/erv058;
RA Xu C., Liu Y., Li Y., Xu X., Xu C., Li X., Xiao J., Zhang Q.;
RT "Differential expression of GS5 regulates grain size in rice.";
RL J. Exp. Bot. 66:2611-2623(2015).
CC -!- FUNCTION: Binds multiple steroid compounds (By similarity). May act as
CC a coreceptor with SERL2 and enhance its endocytosis (Probable).
CC {ECO:0000250|UniProtKB:Q9XFM6, ECO:0000305|PubMed:25711711}.
CC -!- SUBUNIT: Interacts with SERL2. {ECO:0000269|PubMed:25711711}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaf sheaths, leaf blades and
CC panicles. {ECO:0000269|PubMed:17512025}.
CC -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved iron-
CC binding His residues at positions 108 and 132. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC {ECO:0000305}.
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DR EMBL; AC078840; AAG13629.1; -; Genomic_DNA.
DR EMBL; DP000086; ABB47845.2; -; Genomic_DNA.
DR EMBL; AP008216; BAF26907.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT11541.1; -; Genomic_DNA.
DR EMBL; CM000147; EAZ16597.1; -; Genomic_DNA.
DR EMBL; AK069511; BAG91467.1; -; mRNA.
DR EMBL; AK105774; BAG97358.1; -; mRNA.
DR RefSeq; XP_015614354.1; XM_015758868.1.
DR AlphaFoldDB; Q9FVZ7; -.
DR SMR; Q9FVZ7; -.
DR STRING; 4530.OS10T0502600-01; -.
DR CarbonylDB; Q9FVZ7; -.
DR PaxDb; Q9FVZ7; -.
DR PRIDE; Q9FVZ7; -.
DR EnsemblPlants; Os10t0502600-01; Os10t0502600-01; Os10g0502600.
DR EnsemblPlants; Os10t0502600-03; Os10t0502600-03; Os10g0502600.
DR GeneID; 4349046; -.
DR Gramene; Os10t0502600-01; Os10t0502600-01; Os10g0502600.
DR Gramene; Os10t0502600-03; Os10t0502600-03; Os10g0502600.
DR KEGG; osa:4349046; -.
DR eggNOG; KOG1110; Eukaryota.
DR HOGENOM; CLU_042860_0_2_1; -.
DR InParanoid; Q9FVZ7; -.
DR OMA; DYPQPEP; -.
DR OrthoDB; 1331617at2759; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR ExpressionAtlas; Q9FVZ7; baseline and differential.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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: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; Reference proteome; Signal-anchor;
KW Steroid-binding; Transmembrane; Transmembrane helix.
FT CHAIN 1..232
FT /note="Membrane steroid-binding protein 1"
FT /id="PRO_0000441259"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 71..170
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT REGION 48..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..170
FT /note="Steroid-binding"
FT /evidence="ECO:0000250"
FT REGION 172..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 50..52
FT /note="PPP -> QEL (in Ref. 5; EAZ16597)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 24635 MW; D85E5F8B977AE5B9 CRC64;
MAAAVAELWE TLKQAIVAYT GLSPAAFFTA VAAAAALYHV VSGIFAGPPP PPPPRPRDEP
EAEPLPPPVQ LGEVSEEELR QYDGSDPKKP LLMAIKGQIY DVTQSRMFYG PGGPYALFAG
KDASRALAKM SFEPQDLTGD ISGLGPFELD ALQDWEYKFM GKYVKVGTVK KTVPVEDGAP
STSPETTETA AAAEPEKAPA TEEKPREVSS EEVKEKEDAV AAAAPDEGAK ES
