PAP14_ARATH
ID PAP14_ARATH Reviewed; 670 AA.
AC Q9LV04; C0Z3D5; Q8VZ70;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Probable plastid-lipid-associated protein 14, chloroplastic;
DE Short=AtPap14;
DE AltName: Full=Fibrillin-11;
DE AltName: Full=OBP3-responsive protein 1;
DE Flags: Precursor;
GN Name=PAP14; Synonyms=FBN11, FIB11, ORG1; OrderedLocusNames=At5g53450;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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] (ISOFORMS 1 AND 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
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 [5]
RP FUNCTION, AND INDUCTION BY SALICYLIC ACID AND JASMONIC ACID.
RX PubMed=12887587; DOI=10.1046/j.1365-313x.2003.01812.x;
RA Kang H.-G., Foley R.C., Onate-Sanchez L., Lin C., Singh K.B.;
RT "Target genes for OBP3, a Dof transcription factor, include novel basic
RT helix-loop-helix domain proteins inducible by salicylic acid.";
RL Plant J. 35:362-372(2003).
RN [6]
RP LACK OF AUTOPHOSPHORYLATION.
RX PubMed=21477822; DOI=10.1016/j.phytochem.2011.02.029;
RA Nemoto K., Seto T., Takahashi H., Nozawa A., Seki M., Shinozaki K.,
RA Endo Y., Sawasaki T.;
RT "Autophosphorylation profiling of Arabidopsis protein kinases using the
RT cell-free system.";
RL Phytochemistry 72:1136-1144(2011).
RN [7]
RP GENE FAMILY, TISSUE SPECIFICITY, AND NOMENCLATURE.
RX PubMed=21571574; DOI=10.1016/j.tplants.2011.03.014;
RA Singh D.K., McNellis T.W.;
RT "Fibrillin protein function: the tip of the iceberg?";
RL Trends Plant Sci. 16:432-441(2011).
CC -!- FUNCTION: Directly regulated by DOF3.6/OBP3; unknown function.
CC {ECO:0000269|PubMed:12887587}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LV04-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LV04-2; Sequence=VSP_053357;
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:21571574}.
CC -!- INDUCTION: Up-regulated by salicylic acid and down-regulated by
CC jasmonic acid. {ECO:0000269|PubMed:12887587}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- PTM: Not autophosphorylated.
CC -!- SIMILARITY: Belongs to the PAP/fibrillin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH57214.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AB020754; BAA97322.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96355.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96356.1; -; Genomic_DNA.
DR EMBL; AY065207; AAL38683.1; -; mRNA.
DR EMBL; BT002001; AAN72012.1; -; mRNA.
DR EMBL; BT008410; AAP37769.1; -; mRNA.
DR EMBL; AK319099; BAH57214.1; ALT_SEQ; mRNA.
DR RefSeq; NP_200157.2; NM_124724.5. [Q9LV04-2]
DR RefSeq; NP_851182.1; NM_180851.2. [Q9LV04-1]
DR AlphaFoldDB; Q9LV04; -.
DR BioGRID; 20671; 6.
DR IntAct; Q9LV04; 7.
DR STRING; 3702.AT5G53450.1; -.
DR PaxDb; Q9LV04; -.
DR PRIDE; Q9LV04; -.
DR ProteomicsDB; 234946; -. [Q9LV04-1]
DR EnsemblPlants; AT5G53450.1; AT5G53450.1; AT5G53450. [Q9LV04-1]
DR EnsemblPlants; AT5G53450.2; AT5G53450.2; AT5G53450. [Q9LV04-2]
DR GeneID; 835426; -.
DR Gramene; AT5G53450.1; AT5G53450.1; AT5G53450. [Q9LV04-1]
DR Gramene; AT5G53450.2; AT5G53450.2; AT5G53450. [Q9LV04-2]
DR KEGG; ath:AT5G53450; -.
DR Araport; AT5G53450; -.
DR TAIR; locus:2178456; AT5G53450.
DR eggNOG; KOG0594; Eukaryota.
DR InParanoid; Q9LV04; -.
DR OMA; AFDMRCL; -.
DR PhylomeDB; Q9LV04; -.
DR PRO; PR:Q9LV04; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LV04; baseline and differential.
DR Genevisible; Q9LV04; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR006843; PAP/fibrillin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF04755; PAP_fibrillin; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..670
FT /note="Probable plastid-lipid-associated protein 14,
FT chloroplastic"
FT /id="PRO_0000424244"
FT DOMAIN 88..399
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..80
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172,
FT ECO:0000303|PubMed:19423640"
FT /id="VSP_053357"
SQ SEQUENCE 670 AA; 75766 MW; 52DDE0C2D4A4E45B CRC64;
MALCGVCSTP NLPNLQVFRS VRNSSIGYKR NHSLWQLRSS SFRAKSVIFH CSSSLRQSPS
NVEEIDDNPS VSLEDESAHV MQFKWSDFRI LDRVSIGHGG RADELVFEAI VQVPDSPLFN
QGVVLRKLNT TRAQRRGRRA IEVFKKLVRR RLLYHSYSMQ VHGYITNNLS DDQYSFTLVH
GCHGSFSIRH WLQQSDWIPT LEATLALDEE SFRRVGDDTT GGPAVSRQLR LIRTLMRDIL
IGVNYLHSHG LAHTELRLEN VHISPVDRHI KVGILGNAAD FNGDVPSTSN AYSTMDRRQM
MIAFDMRCVG FMMAKMVLQE LMDPLIFAKL KSFLAKGNDP SSLREFFVTT LNTNSESGNT
GVQILDRNWG AGWHLLSLLI ATRPSERISC LDALKHPFLC GPRWRVAPSM DIIRWGLGST
AVKISEEYIY RMPQRQRLAH FIGLMEMLNP YPKPNCWLEL LPGRWRLLYS TGKHIGLTLR
QPSTRALIGN VHLTITRASE SINNTSLSFT SDIRFTAITS KDWPHNKIGA AGKLQTLSQF
RLIAGKRLYL KEEKKNIGKF SMGEPDAEEG LAEKLETEKW KKVVPFKEFP SSLPVAKLVS
GEIEVTMNMN DHIDSPGSVI GEVRKQIPPE MFDLSKLVCG TYIDSRLLVL RCVNGSALLF
TRSSLDHKSM
