PIRL4_ARATH
ID PIRL4_ARATH Reviewed; 549 AA.
AC Q9SVW8;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Plant intracellular Ras-group-related LRR protein 4;
GN Name=PIRL4; OrderedLocusNames=At4g35470; ORFNames=F15J1.40;
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], GENE FAMILY, MOTIF GVYW, AND TISSUE
RP SPECIFICITY.
RX PubMed=15809230; DOI=10.1093/pcp/pci097;
RA Forsthoefel N.R., Cutler K., Port M.D., Yamamoto T., Vernon D.M.;
RT "PIRLs: a novel class of plant intracellular leucine-rich repeat
RT proteins.";
RL Plant Cell Physiol. 46:913-922(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Leucine-rich repeat protein that likely mediates protein
CC interactions, possibly in the context of signal transduction.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15809230}.
CC -!- SIMILARITY: Belongs to the SHOC2 family. {ECO:0000305}.
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DR EMBL; AY849574; AAW57413.1; -; mRNA.
DR EMBL; AL117188; CAB54875.1; -; Genomic_DNA.
DR EMBL; AL161587; CAB80263.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86519.1; -; Genomic_DNA.
DR EMBL; AY072324; AAL61931.1; -; mRNA.
DR EMBL; AY128730; AAM91130.1; -; mRNA.
DR PIR; T41744; T41744.
DR RefSeq; NP_195272.1; NM_119712.6.
DR AlphaFoldDB; Q9SVW8; -.
DR SMR; Q9SVW8; -.
DR BioGRID; 14981; 6.
DR IntAct; Q9SVW8; 3.
DR STRING; 3702.AT4G35470.1; -.
DR iPTMnet; Q9SVW8; -.
DR SwissPalm; Q9SVW8; -.
DR PaxDb; Q9SVW8; -.
DR PRIDE; Q9SVW8; -.
DR ProteomicsDB; 234759; -.
DR EnsemblPlants; AT4G35470.1; AT4G35470.1; AT4G35470.
DR GeneID; 829699; -.
DR Gramene; AT4G35470.1; AT4G35470.1; AT4G35470.
DR KEGG; ath:AT4G35470; -.
DR Araport; AT4G35470; -.
DR TAIR; locus:2117617; AT4G35470.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_038753_0_0_1; -.
DR InParanoid; Q9SVW8; -.
DR OrthoDB; 607914at2759; -.
DR PhylomeDB; Q9SVW8; -.
DR PRO; PR:Q9SVW8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SVW8; baseline and differential.
DR Genevisible; Q9SVW8; AT.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR PROSITE; PS51450; LRR; 9.
PE 1: Evidence at protein level;
KW Leucine-rich repeat; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..549
FT /note="Plant intracellular Ras-group-related LRR protein 4"
FT /id="PRO_0000423604"
FT REPEAT 245..268
FT /note="LRR 1"
FT REPEAT 269..291
FT /note="LRR 2"
FT REPEAT 293..313
FT /note="LRR 3"
FT REPEAT 314..337
FT /note="LRR 4"
FT REPEAT 339..360
FT /note="LRR 5"
FT REPEAT 362..383
FT /note="LRR 6"
FT REPEAT 384..406
FT /note="LRR 7"
FT REPEAT 407..430
FT /note="LRR 8"
FT REPEAT 432..454
FT /note="LRR 9"
FT REPEAT 455..476
FT /note="LRR 10"
FT REPEAT 478..500
FT /note="LRR 11"
FT REGION 119..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 501..508
FT /note="GVYW; degenerate"
FT COMPBIAS 119..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 549 AA; 60995 MW; CBA29184696C5635 CRC64;
MDLMQMDKRL DSTEQVVEEI MRIHRSLPAR PGIDEVEAAK GLIDNVEKED QACLEAIARQ
RKSSEVPGEL FMVLQEMKKG YVQFRSKEQI REALKLLDLE SVHSLFDDFI QRASNCIASP
SSNGSVSSRP PLPPATTTAA RSDSQSSLNF SERAPVRPKD MVSRDDSFVT KSKPSSLYSD
GFAAPPRRPQ ILDSTLTTGN DGEKLSLIKL ASLIEVSAKK ATQEINLQNK LTEQLEWLPD
SLGKLSSLTS LDLSENHIVV LPNTIGGLSS LTKLDLHSNR IGQLPESIGE LLNLVYLNLG
SNQLSSLPSA FSRLVRLEEL DLSCNNLPIL PESIGSLVSL KKLDVETNDI EEIPYSIGGC
SSLIELRADY NKLKALPEAI GKITTLEILS VRYNNIRQLP TTMSSLASLK ELDVSFNELE
SVPESLCFAT TLVKLNIGNN FADMVSLPRS IGNLEMLEEL DISNNQIRVL PDSFKMLTKL
RVFRAQENPL HIPPRDIAEK GPQAVVQYMN DLVETRNAKS LMVKPKKSWV QMCFFSKSNK
RKQSSMEIV
