ORP3B_ARATH
ID ORP3B_ARATH Reviewed; 458 AA.
AC Q9SR33;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Oxysterol-binding protein-related protein 3B;
DE AltName: Full=OSBP-related protein 3B;
GN Name=ORP3B; OrderedLocusNames=At3g09300; ORFNames=F3L24.17;
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=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 [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 TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16897474; DOI=10.1007/s11103-006-0030-y;
RA Skirpan A.L., Dowd P.E., Sijacic P., Jaworski C.J., Gilroy S., Kao T.H.;
RT "Identification and characterization of PiORP1, a Petunia oxysterol-
RT binding-protein related protein involved in receptor-kinase mediated
RT signaling in pollen, and analysis of the ORP gene family in Arabidopsis.";
RL Plant Mol. Biol. 61:553-565(2006).
CC -!- FUNCTION: May be involved in the transport of sterols. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:16897474}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
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DR EMBL; AC011436; AAF14027.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74748.1; -; Genomic_DNA.
DR EMBL; AY062703; AAL32781.1; -; mRNA.
DR EMBL; AY093373; AAM13372.1; -; mRNA.
DR RefSeq; NP_187541.1; NM_111764.4.
DR AlphaFoldDB; Q9SR33; -.
DR SMR; Q9SR33; -.
DR STRING; 3702.AT3G09300.1; -.
DR iPTMnet; Q9SR33; -.
DR PaxDb; Q9SR33; -.
DR PRIDE; Q9SR33; -.
DR ProteomicsDB; 248646; -.
DR EnsemblPlants; AT3G09300.1; AT3G09300.1; AT3G09300.
DR GeneID; 820086; -.
DR Gramene; AT3G09300.1; AT3G09300.1; AT3G09300.
DR KEGG; ath:AT3G09300; -.
DR Araport; AT3G09300; -.
DR TAIR; locus:2083594; AT3G09300.
DR eggNOG; KOG1737; Eukaryota.
DR HOGENOM; CLU_007105_6_0_1; -.
DR InParanoid; Q9SR33; -.
DR OMA; FRIICEQ; -.
DR OrthoDB; 863978at2759; -.
DR PhylomeDB; Q9SR33; -.
DR PRO; PR:Q9SR33; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SR33; baseline and differential.
DR Genevisible; Q9SR33; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR PROSITE; PS01013; OSBP; 1.
PE 2: Evidence at transcript level;
KW Lipid transport; Lipid-binding; Reference proteome; Transport.
FT CHAIN 1..458
FT /note="Oxysterol-binding protein-related protein 3B"
FT /id="PRO_0000402163"
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 51956 MW; 2BED9BBFA6522F33 CRC64;
MAPNDPKKAV GGGGSGFFAS LASSISNLGS AMTKSVNGLV PYEGLEVINP EGSTDDAEEE
ASRGRWKQED RDGYWKMMQK YIGSDVTSMV TLPVIIFEPM TMLQKMAELM EYSHLLDMAD
KTEDPYLRMV YASSWAISVY YAFQRTWKPF NPILGETYEM ANYNGVNFIS EQVSHHPPMS
AGHAENEHFT YDCTSKLKTK FLGNSIDVYP VGRTRVTLKR DGVVLDLVPP LTKVHNLIFG
RTWVDSPGEM IMTNQTTGDK VVLYFQPCGW FGSGRYEVDG YVYNASEEPK ILMTGKWNES
MSYQPCDGEG EPLPGTELKE VWKLADVPKD DKYQYTHFAH KINSFDTAPK KLLPSDSRLR
PDRYALEMGD MSKSGYEKSS MEERQRAEKR TREEKGQAFT PKWFDVTEEV TATPWGDLEV
YQFNGKYSEH RAAADNSEDN TDPKSIQFNP WQFQDLST
