RST1_ARATH
ID RST1_ARATH Reviewed; 1841 AA.
AC Q7XZF5; F4IWL6; Q9LVX3;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein RST1 {ECO:0000305};
DE AltName: Full=Protein RESURRECTION 1 {ECO:0000303|PubMed:16183838};
GN Name=RST1 {ECO:0000303|PubMed:16183838}; OrderedLocusNames=At3g27670;
GN ORFNames=MGF10.8;
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], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. C24;
RX PubMed=16183838; DOI=10.1104/pp.105.066753;
RA Chen X., Goodwin S.M., Liu X., Chen X., Bressan R.A., Jenks M.A.;
RT "Mutation of the RESURRECTION1 locus of Arabidopsis reveals an association
RT of cuticular wax with embryo development.";
RL Plant Physiol. 139:909-919(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19625635; DOI=10.1104/pp.109.142158;
RA Mang H.G., Laluk K.A., Parsons E.P., Kosma D.K., Cooper B.R., Park H.C.,
RA AbuQamar S., Boccongelli C., Miyazaki S., Consiglio F., Chilosi G.,
RA Bohnert H.J., Bressan R.A., Mengiste T., Jenks M.A.;
RT "The Arabidopsis RESURRECTION1 gene regulates a novel antagonistic
RT interaction in plant defense to biotrophs and necrotrophs.";
RL Plant Physiol. 151:290-305(2009).
RN [5]
RP FUNCTION, INTERACTION WITH CER16/RIPR, AND SUBCELLULAR LOCATION.
RX PubMed=31455787; DOI=10.1038/s41467-019-11807-4;
RA Lange H., Ndecky S.Y.A., Gomez-Diaz C., Pflieger D., Butel N., Zumsteg J.,
RA Kuhn L., Piermaria C., Chicher J., Christie M., Karaaslan E.S.,
RA Lang P.L.M., Weigel D., Vaucheret H., Hammann P., Gagliardi D.;
RT "RST1 and RIPR connect the cytosolic RNA exosome to the Ski complex in
RT Arabidopsis.";
RL Nat. Commun. 10:3871-3871(2019).
RN [6]
RP FUNCTION.
RX PubMed=31076735; DOI=10.1038/s41477-019-0419-7;
RA Li T., Natran A., Chen Y., Vercruysse J., Wang K., Gonzalez N., Dubois M.,
RA Inze D.;
RT "A genetics screen highlights emerging roles for CPL3, RST1 and URT1 in RNA
RT metabolism and silencing.";
RL Nat. Plants 5:539-550(2019).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31221737; DOI=10.1105/tpc.19.00003;
RA Zhao Q., Shen J., Gao C., Cui Y., Wang Y., Cui J., Cheng L., Cao W.,
RA Zhu Y., Huang S., Zhou Q., Leong C.K., Leung K.P., Chen X., Jiang L.;
RT "RST1 is a FREE1 suppressor that negatively regulates vacuolar trafficking
RT in Arabidopsis.";
RL Plant Cell 31:2152-2168(2019).
CC -!- FUNCTION: Involved in cuticular wax formation (PubMed:16183838,
CC PubMed:19625635). Required for the synthesis of alkanes from wax
CC precursors (PubMed:16183838, PubMed:19625635). May play a role in acyl-
CC CoA reduction to aldehydes (PubMed:16183838). Is repressed by FREE1 and
CC functions downstream of FREE1 to negatively regulate multivesicular
CC body (MVB) biogenesis and vacuolar transport (PubMed:31221737).
CC Together with CER16/RIPR, acts as cofactor of the cytoplasmic exosome
CC and connects the cytosolic RNA exosome to the SKI complex
CC (PubMed:31455787). Acts as post-transcriptional gene silencing (PTGS)
CC suppressor (PubMed:31455787, PubMed:31076735). RST1 can, like
CC CER16/RIPR, suppress the production of small interfering RNAs (siRNAs)
CC from the CER3 locus, which is involved in cuticule membrane and wax
CC production, and in the typhine and sporopollenin biosynthesis of pollen
CC (PubMed:31455787). {ECO:0000269|PubMed:16183838,
CC ECO:0000269|PubMed:19625635, ECO:0000269|PubMed:31076735,
CC ECO:0000269|PubMed:31221737, ECO:0000269|PubMed:31455787}.
CC -!- SUBUNIT: Interacts with CER16/RIPR. {ECO:0000269|PubMed:31455787}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19625635};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:31221737, ECO:0000269|PubMed:31455787}.
CC -!- TISSUE SPECIFICITY: Expressed in the vasculature of leaves, petioles
CC and hypocotyls, anthers of mature flowers and siliques
CC (PubMed:19625635). Expressed at low levels in roots and stems
CC (PubMed:16183838). {ECO:0000269|PubMed:16183838,
CC ECO:0000269|PubMed:19625635}.
CC -!- DISRUPTION PHENOTYPE: Shrunken non viable seeds due to arrested embryo
CC development when homozygous (PubMed:16183838). Alteration in cuticular
CC waxes with elevated amounts of cutin monomers in leaves
CC (PubMed:16183838, PubMed:19625635). Susceptibility to the obligate
CC biotrophic fungus E.cichoracearum and increased resistance to the
CC necrotrophic fungi B.cinerea and A.brassicicola (PubMed:19625635).
CC {ECO:0000269|PubMed:16183838, ECO:0000269|PubMed:19625635}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02691.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY307371; AAP74222.1; -; mRNA.
DR EMBL; AB018114; BAB02691.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77350.1; -; Genomic_DNA.
DR RefSeq; NP_189404.2; NM_113683.3.
DR AlphaFoldDB; Q7XZF5; -.
DR BioGRID; 7719; 1.
DR STRING; 3702.AT3G27670.1; -.
DR iPTMnet; Q7XZF5; -.
DR PaxDb; Q7XZF5; -.
DR PRIDE; Q7XZF5; -.
DR ProteomicsDB; 228052; -.
DR EnsemblPlants; AT3G27670.1; AT3G27670.1; AT3G27670.
DR GeneID; 822389; -.
DR Gramene; AT3G27670.1; AT3G27670.1; AT3G27670.
DR KEGG; ath:AT3G27670; -.
DR Araport; AT3G27670; -.
DR TAIR; locus:2089114; AT3G27670.
DR eggNOG; ENOG502S0XX; Eukaryota.
DR HOGENOM; CLU_243099_0_0_1; -.
DR OMA; SMYISRN; -.
DR OrthoDB; 38538at2759; -.
DR PRO; PR:Q7XZF5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q7XZF5; baseline and differential.
DR Genevisible; Q7XZF5; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043447; P:alkane biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006723; P:cuticle hydrocarbon biosynthetic process; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:1900369; P:negative regulation of post-transcriptional gene silencing by RNA; IGI:TAIR.
DR GO; GO:0048316; P:seed development; IMP:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR022542; FOCAD/RST1_DUF3730.
DR InterPro; IPR045163; Focadhesin/RST1.
DR PANTHER; PTHR16212; PTHR16212; 1.
DR Pfam; PF12530; DUF3730; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Lipid metabolism; Membrane; Plant defense;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1841
FT /note="Protein RST1"
FT /id="PRO_0000429124"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..566
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 943..963
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 982..1002
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1123..1143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1175..1195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1229..1249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1277..1297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1719..1739
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1374..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 608
FT /note="Q -> K (in Ref. 1; AAP74222)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="H -> R (in Ref. 1; AAP74222)"
FT /evidence="ECO:0000305"
FT CONFLICT 719
FT /note="N -> S (in Ref. 1; AAP74222)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="F -> G (in Ref. 1; AAP74222)"
FT /evidence="ECO:0000305"
FT CONFLICT 898
FT /note="M -> L (in Ref. 1; AAP74222)"
FT /evidence="ECO:0000305"
FT CONFLICT 925
FT /note="T -> A (in Ref. 1; AAP74222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1841 AA; 203747 MW; 9361053BE597CFD3 CRC64;
MASYATLLEK TRVPQPSIQR FAVISVFSKL RSAPEQFGSE AEAGREAISF CLTSESITVV
DQSVHELCRL VSDSVLDLSR GLLELQSALE GCDSKLVSLF VKGLGFLIRI GYERNNGNWK
FNSTENHPFV RIQSSRVETQ TELLHQVSLF VMHNRRLGMV GVCEFLEPFL NFTILRIPLS
DSSSSLFARE LISSMASLCC SSRHEALPIF RLLMRCLKYI PGNNLEVIVK ILVDAYTVVV
RDLVGTGLEV TEVHLLGVQL VDGVLFLCAS PHVQTTEQES VIESLKHLLA VQKDLGLAYS
HDLSLVVLSL VFMLAKSTVE HEQLCILKFL LFLLKWKTES ENLSVKDAAG SSVESLLLFP
ITALMSSPSK SIKVAASKVL SIVENFLVTV SNAPKIEVHT SKGDSPLSRV GSVVFRFMQQ
LWHQNDYTPS TSSFLRVAYT NGSEKQETYL GPVTWNSLLR EHAERFWDKK KLSASFCLSQ
EIPILLGAVA GVMVMHPSLG ADAIGSLTII GGIDSKMSVP LLLAVLYFSN LLSRTNVPCQ
SLLSKLLGLL PSLAAQQVMI PLVVQTITPM LRKDAKGLLY ATAIRLLCQT WVVNDRAFSS
LQEVLRPQGF IEYISERHIC ISMAASIHDV CKRHPDRGVD LILSVQACIE SQNCPVRALG
FQSLSHLCEA DVIDFYTAWD VIKKHAQHIK LDPLLAYSVC HLLKWGAMDA EAYPEDAENV
LNILWEIGSS MQKPHDSQWT KARVSAIVAL GQYEVSFMEN KFSDFNKNCT YLLFSETNAE
ILNALEDLSI KIMIHEHSVR RRYVREKKVP GSKIEKLLDV IPQVIFPAGK EIKTGELPGA
ALLCLSYNPR DVKFGSSRSF HDVHFQYEEA FRVVVKSLQL SRNISLALIS LQSLKAFMRR
WMRANILSID ATTKELSSDK TSKATNNIMK SLVHMAEEAL PRCAENIALA LGALCAALPA
ASHNIKASAS KFLLSWLLEH EHEHRQWTAG ISLGLISSSL HVTDHKQKFQ NISGLLEVLC
SSKSTLVKGA CGVGLGFSCQ DLLTRTEASA SSDIDSDSYR NQEERLLGRI VRLLSSILHG
FLHTPCDILE SLSALFPPGE EDNVIGLPQL LDESSDDFDD DTWGIAGLII GLGMSVGAIY
RAGKKDAVVK IKNLIVSWIP YADSLKQTSG SNSKVSVRLF SVGSCLALPI VITFCQKVEL
FDAHEVDDII GCFKDLISEL LIVRKSGALR KRLLMASCIG AGDLLGSVLN EGIHPVKIES
VKELLELFKK CYSGLYPPVA HFGGMLGVVN VLGAGAGNLV YSHPRPRAPP ASSEENEISY
VSGPLLSNAY FTQQLTPVVQ EIFLIAQNTK DRQLQHYAAW AISILRTYMR SGESSSLSNE
NQSDDSDRNS ISHNVPEHTM VMKLAQGLTN PSFPLAGSPL NIGTMASALR CLSHAPRLPN
LDWGATIRRL MKQETQTDVT QSGDVPKEIT LREECFKFSL AHASEFDELL AFLDELSELS
RFKALEESLQ SCLLCHLGGL MRIFSGSRMN KLFDDVSCFV VSLSSDQTYS CDQKSSLRVS
CWKGLSQCLE ETSLESSEYV TKIEKCIELL FAVLPVASQS PRADQMGSVK EWSEAVTCLQ
KSHRDWLYKF LQVSNLEPGN EKTNFQGDLK KIQAKAKLAK LGSVPFSELG KLKAIILNCE
ESDIWDVLIE IVAALHHAEG GIKRQWLIDA VEISCVSSHP STAIIFVGLL SSICCEYMPF
LNLDRSTVLS DMSVTVTSLL SDPSYEVVTE PFISFLWTSL ERVYSFATES DANARLSSQQ
IAQSERDKAP MLVKVMHYIC VAFRDHLPLE KQLRLASMDM S
