PIP2_ARATH
ID PIP2_ARATH Reviewed; 84 AA.
AC F4JRC5; O23158; Q8L9Y5;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=PAMP-induced secreted peptide 2 {ECO:0000303|PubMed:25188390};
DE Flags: Precursor;
GN Name=PIP2 {ECO:0000303|PubMed:25188390};
GN OrderedLocusNames=At4g37290 {ECO:0000312|Araport:AT4G37290};
GN ORFNames=C7A10.70 {ECO:0000312|EMBL:CAB16755.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND HYDROXYLATION AT PRO-77 AND PRO-79.
RX PubMed=25188390; DOI=10.1371/journal.ppat.1004331;
RA Hou S., Wang X., Chen D., Yang X., Wang M., Turra D., Di Pietro A.,
RA Zhang W.;
RT "The secreted peptide PIP1 amplifies immunity through receptor-like kinase
RT 7.";
RL PLoS Pathog. 10:E1004331-E1004331(2014).
CC -!- FUNCTION: Endogenous secreted peptide that acts as elicitor of immune
CC response and positive regulator of defense response. Amplifies the
CC immune response triggered by flg22, the active epitope of bacterial
CC flagellin. Acts as negative regulator of root growth.
CC {ECO:0000269|PubMed:25188390}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250|UniProtKB:Q1PE40}.
CC -!- PTM: Contains 4-hydroxyproline; hydroxylated on Pro-77 and Pro-79.
CC {ECO:0000305|PubMed:25188390}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM65691.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB16755.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB80395.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z99707; CAB16755.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161591; CAB80395.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE86777.1; -; Genomic_DNA.
DR EMBL; AY088146; AAM65691.1; ALT_INIT; mRNA.
DR PIR; F85440; F85440.
DR RefSeq; NP_568022.1; NM_119892.2.
DR AlphaFoldDB; F4JRC5; -.
DR STRING; 3702.AT4G37290.1; -.
DR PaxDb; F4JRC5; -.
DR PRIDE; F4JRC5; -.
DR EnsemblPlants; AT4G37290.1; AT4G37290.1; AT4G37290.
DR GeneID; 829883; -.
DR Gramene; AT4G37290.1; AT4G37290.1; AT4G37290.
DR KEGG; ath:AT4G37290; -.
DR Araport; AT4G37290; -.
DR TAIR; locus:2115159; AT4G37290.
DR eggNOG; ENOG502RRHB; Eukaryota.
DR HOGENOM; CLU_2515718_0_0_1; -.
DR InParanoid; F4JRC5; -.
DR OMA; MMMINKA; -.
DR OrthoDB; 1565384at2759; -.
DR PRO; PR:F4JRC5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JRC5; baseline and differential.
DR GO; GO:0048046; C:apoplast; IDA:TAIR.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR InterPro; IPR044700; PIP2/PIPL1.
DR PANTHER; PTHR34663; PTHR34663; 1.
PE 1: Evidence at protein level;
KW Apoplast; Hydroxylation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..84
FT /note="PAMP-induced secreted peptide 2"
FT /evidence="ECO:0000255"
FT /id="PRO_5009954975"
FT REGION 50..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305|PubMed:25188390"
FT MOD_RES 79
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000305|PubMed:25188390"
SQ SEQUENCE 84 AA; 9032 MW; 06D16D86C7688185 CRC64;
MMMNKNVLSS ILFFMLIGSV LVESRPLGLT KTEEKFVASL FDGLSLGSIK DSGPSPGEGH
KVVDRKDTFR FVKHSGPSPS GPGH
