ORP3A_ARATH
ID ORP3A_ARATH Reviewed; 453 AA.
AC Q9LZM1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Oxysterol-binding protein-related protein 3A;
DE AltName: Full=OSBP-related protein 3A;
DE AltName: Full=Protein UNFERTILIZED EMBRYO SAC 18;
GN Name=ORP3A; Synonyms=UNE18; OrderedLocusNames=At5g02100;
GN ORFNames=T7H20.150;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
RN [5]
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).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PVA12, AND MUTAGENESIS OF
RP 172-PRO-PRO-173 AND 398-TRP--GLU-403.
RX PubMed=19207211; DOI=10.1111/j.1365-313x.2009.03815.x;
RA Saravanan R.S., Slabaugh E., Singh V.R., Lapidus L.J., Haas T.,
RA Brandizzi F.;
RT "The targeting of the oxysterol-binding protein ORP3a to the endoplasmic
RT reticulum relies on the plant VAP33 homolog PVA12.";
RL Plant J. 58:817-830(2009).
CC -!- FUNCTION: Oxysterol-binding protein that may be involved in the
CC transport of sterols between the ER and the Golgi. Binds beta-
CC sitosterol. Required for ovule fertilization.
CC {ECO:0000269|PubMed:15634699, ECO:0000269|PubMed:19207211}.
CC -!- SUBUNIT: Interacts with PVA12. {ECO:0000269|PubMed:19207211}.
CC -!- INTERACTION:
CC Q9LZM1; Q9SHC8: PVA12; NbExp=3; IntAct=EBI-2292648, EBI-2292633;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:19207211}. Golgi apparatus
CC {ECO:0000269|PubMed:19207211}. Note=Interaction with PVA12 is necessary
CC for targeting to the ER. Located in the Golgi in the absence of
CC interaction with PVA12.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC pollen. {ECO:0000269|PubMed:16897474}.
CC -!- DISRUPTION PHENOTYPE: Unfertilized ovules, but normal pollen tube
CC attraction. {ECO:0000269|PubMed:15634699}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
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DR EMBL; AY050839; AAK92774.1; -; mRNA.
DR EMBL; AY091166; AAM14105.1; -; mRNA.
DR EMBL; AL162508; CAB82983.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90431.1; -; Genomic_DNA.
DR PIR; T48231; T48231.
DR RefSeq; NP_195830.1; NM_120288.3.
DR AlphaFoldDB; Q9LZM1; -.
DR SMR; Q9LZM1; -.
DR BioGRID; 17117; 1.
DR IntAct; Q9LZM1; 1.
DR STRING; 3702.AT5G02100.1; -.
DR iPTMnet; Q9LZM1; -.
DR PaxDb; Q9LZM1; -.
DR PRIDE; Q9LZM1; -.
DR EnsemblPlants; AT5G02100.1; AT5G02100.1; AT5G02100.
DR GeneID; 831841; -.
DR Gramene; AT5G02100.1; AT5G02100.1; AT5G02100.
DR KEGG; ath:AT5G02100; -.
DR Araport; AT5G02100; -.
DR TAIR; locus:2185163; AT5G02100.
DR eggNOG; KOG1737; Eukaryota.
DR HOGENOM; CLU_007105_6_0_1; -.
DR InParanoid; Q9LZM1; -.
DR OrthoDB; 863978at2759; -.
DR PhylomeDB; Q9LZM1; -.
DR PRO; PR:Q9LZM1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZM1; baseline and differential.
DR Genevisible; Q9LZM1; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0032934; F:sterol binding; IDA:TAIR.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IMP:TAIR.
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 1: Evidence at protein level;
KW Endoplasmic reticulum; Fertilization; Golgi apparatus; Lipid transport;
KW Lipid-binding; Reference proteome; Steroid-binding; Transport.
FT CHAIN 1..453
FT /note="Oxysterol-binding protein-related protein 3A"
FT /id="PRO_0000402162"
FT REGION 166..175
FT /note="Required for oxysterol binding"
FT REGION 370..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..403
FT /note="Required for binding to PVA12 and location in the
FT ER"
FT COMPBIAS 371..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 172..173
FT /note="PP->AA: Unable to bind beta-sitosterol."
FT /evidence="ECO:0000269|PubMed:19207211"
FT MUTAGEN 398..403
FT /note="WFDETE->KV: Unable to bind PVA12 and to locate in
FT the ER."
FT /evidence="ECO:0000269|PubMed:19207211"
SQ SEQUENCE 453 AA; 51545 MW; 83646151C2F24B0A CRC64;
MASNDPKNGG GFFASLASSI TNFGSAMSKS VNGLMGYEGL EVINPEGSTD DAEEEAGRGR
WKQEERDGYW KMMQKYIGSD VTSMVTLPVI IFEPMTMLQK MAELMEYSYL LDMADKTEDP
YMRMVYASSW AISVYYAYQR TWKPFNPILG ETYEMTNHNG INFIAEQVCH HPPMSAGHAE
NEHFAYDCTS KLKTKFLGNS IDVYPVGRTR VTLKRDGVVL DLVPPLTKVH NLIFGRTWVD
SPGEMVMTNL TTGDKVVLYF QPCGWFGSGR YEVDGYVYNS AEEPKMLMTG KWNESLSYQP
CDAEGEPLPG TELKEVWKVA EAPKNDKYQY THFAHKINSF DTAPKKLLSS DSRLRPDRYA
LEMGDMSKSG FEKSSLEDRQ RAEKKSREEK GQKFAPKWFD ETEEVTPTPW GDLEVYQFNG
KYSVHRATAE NSEDTTDVKL TQFNPWQFQD LSA
