PPI1_ARATH
ID PPI1_ARATH Reviewed; 612 AA.
AC O23144; B9DFB6; Q9SZS5;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Proton pump-interactor 1;
GN Name=PPI1; OrderedLocusNames=At4g27500; ORFNames=F27G19.100;
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, INTERACTION WITH AHA1, GENE FAMILY,
RP AND NOMENCLATURE.
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf, and Root;
RX PubMed=12182706; DOI=10.1046/j.1365-313x.2002.01373.x;
RA Morandini P., Valera M., Albumi C., Bonza M.C., Giacometti S., Ravera G.,
RA Murgia I., Soave C., De Michelis M.I.;
RT "A novel interaction partner for the C-terminus of Arabidopsis thaliana
RT plasma membrane H+-ATPase (AHA1 isoform): site and mechanism of action on
RT H+-ATPase activity differ from those of 14-3-3 proteins.";
RL Plant J. 31:487-497(2002).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-510.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, AND INTERACTION WITH AHA1.
RX PubMed=16279950; DOI=10.1111/j.1742-4658.2005.04985.x;
RA Viotti C., Luoni L., Morandini P., De Michelis M.I.;
RT "Characterization of the interaction between the plasma membrane H-ATPase
RT of Arabidopsis thaliana and a novel interactor (PPI1).";
RL FEBS J. 272:5864-5871(2005).
RN [7]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=18304198; DOI=10.1111/j.1438-8677.2007.00022.x;
RA Anzi C., Pelucchi P., Vazzola V., Murgia I., Gomarasca S., Piccoli M.B.,
RA Morandini P.;
RT "The proton pump interactor (Ppi) gene family of Arabidopsis thaliana:
RT expression pattern of Ppi1 and characterisation of knockout mutants for
RT Ppi1 and 2.";
RL Plant Biol. 10:237-249(2008).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=19796364; DOI=10.1111/j.1438-8677.2008.00181.x;
RA Bonza M.C., Fusca T., Homann U., Thiel G., De Michelis M.I.;
RT "Intracellular localisation of PPI1 (proton pump interactor, isoform 1), a
RT regulatory protein of the plasma membrane H(+)-ATPase of Arabidopsis
RT thaliana.";
RL Plant Biol. 11:869-877(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, 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: Promotes AHA1 plasma membrane ATPase activity by binding to a
CC site different from the 14-3-3 binding site.
CC {ECO:0000269|PubMed:12182706, ECO:0000269|PubMed:16279950}.
CC -!- SUBUNIT: Interacts with AHA1 via N-terminal region.
CC {ECO:0000269|PubMed:12182706, ECO:0000269|PubMed:16279950}.
CC -!- INTERACTION:
CC O23144; P20649: AHA1; NbExp=7; IntAct=EBI-2354477, EBI-2354448;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19796364};
CC Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000269|PubMed:19796364}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in root and shoot vascular
CC systems, particularly in meristematic and sink tissues. Also present in
CC pollen, stigmas and siliques, but not in developing embryos.
CC {ECO:0000269|PubMed:18304198}.
CC -!- SIMILARITY: Belongs to the plant Proton pump-interactor protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43882.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81400.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ002020; CAA05145.2; -; mRNA.
DR EMBL; AL078467; CAB43882.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161571; CAB81400.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85350.1; -; Genomic_DNA.
DR EMBL; AY050365; AAK91382.1; -; mRNA.
DR EMBL; AY143914; AAN28853.1; -; mRNA.
DR EMBL; AK316706; BAH19433.1; -; mRNA.
DR PIR; T08942; T08942.
DR RefSeq; NP_194480.2; NM_118885.4.
DR AlphaFoldDB; O23144; -.
DR SMR; O23144; -.
DR BioGRID; 14146; 9.
DR IntAct; O23144; 1.
DR STRING; 3702.AT4G27500.1; -.
DR iPTMnet; O23144; -.
DR PaxDb; O23144; -.
DR PRIDE; O23144; -.
DR ProMEX; O23144; -.
DR ProteomicsDB; 249345; -.
DR EnsemblPlants; AT4G27500.1; AT4G27500.1; AT4G27500.
DR GeneID; 828859; -.
DR Gramene; AT4G27500.1; AT4G27500.1; AT4G27500.
DR KEGG; ath:AT4G27500; -.
DR Araport; AT4G27500; -.
DR TAIR; locus:2124019; AT4G27500.
DR eggNOG; ENOG502QQX1; Eukaryota.
DR HOGENOM; CLU_018947_1_0_1; -.
DR InParanoid; O23144; -.
DR OMA; NVNMEAS; -.
DR OrthoDB; 661653at2759; -.
DR PhylomeDB; O23144; -.
DR PRO; PR:O23144; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23144; baseline and differential.
DR Genevisible; O23144; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0010155; P:regulation of proton transport; IDA:UniProtKB.
DR InterPro; IPR029669; PPI.
DR PANTHER; PTHR32219:SF17; PTHR32219:SF17; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Endoplasmic reticulum; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..612
FT /note="Proton pump-interactor 1"
FT /id="PRO_0000420212"
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 90..113
FT /evidence="ECO:0000255"
FT COILED 251..314
FT /evidence="ECO:0000255"
FT COILED 466..526
FT /evidence="ECO:0000255"
FT COMPBIAS 436..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 326
FT /note="D -> E (in Ref. 5; BAH19433)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 612 AA; 68879 MW; F0882E8AB50D089B CRC64;
MGVEVVNSGG FEVAPAPFEG KPEKNGKLDQ GKGDDAPINF GSVGELPKNA EENNNKVVNS
DAPKNAAEEW PVAKQIHSFY LVKYRSYADP KIKAKLDLAD KELEKLNKAR TGVLDKLRAK
RAERSELFDL LDPLKSERKG FNTMFDEKRK EMEPLQQALG KLRSNDGGSA RGPAICSSEE
ELNSMIYSYQ YRIQHESIPL TEEKQILKEI RLLEGTRDKV IANAAMRAKI KESMGQKDDI
QGQVKLMGAG LDGVKKERQA ISARINELSE KLKATKDEIT VLENELKTVS EKRDKAYSNI
HDLRRQRDET NSEYYQNRTV LNKARDLAAQ KNISELEALA NAEVEKFISL WCSKKNFRED
YEKRILQSLD SRQLSRDGRM RNPDEKPLIA PEAAPSKATP SETEVVPKAK AKPQPKEEPV
SAPKPDATVA QNTEKAKDAV KVKNVADDDD DEVYGLGKPQ KEEKPVDAAT AKEMRKQEEI
AKAKQAMERK KKLAEKAAAK AAIRAQKEAE KKEKKEQEKK AKKKTGGNTE TETEEVPEAS
EEEIEAPVQE EKPQKEKVFK EKPIRNRTRG RGPETIPRAI LKRKKSTNYW VYAAPAALVV
LLLLVLGYYY VL
