PAP85_ARATH
ID PAP85_ARATH Reviewed; 486 AA.
AC Q9LUJ7; Q42160; Q42174; Q42222; Q42326; Q56WF0;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Vicilin-like seed storage protein At3g22640;
DE AltName: Full=Globulin At3g22640;
DE Flags: Precursor;
GN Name=PAP85 {ECO:0000303|PubMed:7827492};
GN OrderedLocusNames=At3g22640 {ECO:0000312|Araport:AT3G22640};
GN ORFNames=MWI23.1 {ECO:0000312|EMBL:BAB01239.1};
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=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 [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].
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 [MRNA] OF 1-136; 179-261; 269-383 AND 397-486.
RC STRAIN=cv. Columbia; TISSUE=Dry seed;
RA Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 222-486.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7827492; DOI=10.2307/3869944;
RA Parcy F., Valon C., Raynal M., Gaubier-Comella P., Delseny M., Giraudat J.;
RT "Regulation of gene expression programs during Arabidopsis seed
RT development: roles of the ABI3 locus and of endogenous abscisic acid.";
RL Plant Cell 6:1567-1582(1994).
RN [7]
RP GENE FAMILY.
RX PubMed=12417707; DOI=10.1105/tpc.005009;
RA Gruis D.F., Selinger D.A., Curran J.M., Jung R.;
RT "Redundant proteolytic mechanisms process seed storage proteins in the
RT absence of seed-type members of the vacuolar processing enzyme family of
RT cysteine proteases.";
RL Plant Cell 14:2863-2882(2002).
RN [8]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=19014699; DOI=10.1186/1472-6750-8-88;
RA Rozwadowski K., Yang W., Kagale S.;
RT "Homologous recombination-mediated cloning and manipulation of genomic DNA
RT regions using Gateway and recombineering systems.";
RL BMC Biotechnol. 8:88-88(2008).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), DISRUPTION PHENOTYPE (MICROBIAL INFECTION),
RP AND INDUCTION BY TOBACCO MOSAIC VIRUS (MICROBIAL INFECTION).
RX PubMed=23576511; DOI=10.1128/jvi.00268-13;
RA Chen C.-E., Yeh K.-C., Wu S.-H., Wang H.-I., Yeh H.-H.;
RT "A vicilin-like seed storage protein, PAP85, is involved in tobacco mosaic
RT virus replication.";
RL J. Virol. 87:6888-6900(2013).
CC -!- FUNCTION: Seed storage protein. {ECO:0000305}.
CC -!- FUNCTION: (Microbial infection) Involved in tobacco mosaic virus (TMV)
CC replication. Required for endoplasmic reticulum (ER) aggregations
CC mediated by TMV main replicase (P126) upon viral infection.
CC {ECO:0000269|PubMed:23576511}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the embryo and endosperm
CC of developing seeds (PubMed:7827492, PubMed:19014699). Also present in
CC seedlings (PubMed:19014699). {ECO:0000269|PubMed:19014699,
CC ECO:0000269|PubMed:7827492}.
CC -!- DEVELOPMENTAL STAGE: First observed at 5 days post anthesis (DPA).
CC Accumulates throughout subsequent stages of embryo development, in
CC embryonic tissues such as cotyledons and embryo axis as well as in the
CC endosperm. In young seedlings, strictly confined to the cotyledons,
CC hypocotyl and root tip, 3-4 days after germination. Also detected in
CC the trichomes of new leaves. {ECO:0000269|PubMed:19014699}.
CC -!- INDUCTION: (Microbial infection) Accumulates after 0.5 to 6 h of
CC tobacco mosaic virus (TMV) infection. {ECO:0000269|PubMed:23576511}.
CC -!- DISRUPTION PHENOTYPE: (Microbial infection) Reduced tobacco mosaic
CC virus (TMV) accumulation associated with altered endoplasmic reticulum
CC (ER) transition in TMV-infected cells. {ECO:0000269|PubMed:23576511}.
CC -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC {ECO:0000305}.
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DR EMBL; AB022223; BAB01239.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76660.1; -; Genomic_DNA.
DR EMBL; AY058085; AAL24193.1; -; mRNA.
DR EMBL; AY090307; AAL90968.1; -; mRNA.
DR EMBL; Z27025; CAA81568.1; -; mRNA.
DR EMBL; Z27252; CAA81765.1; -; mRNA.
DR EMBL; Z29841; CAA82813.1; -; mRNA.
DR EMBL; Z46695; CAA86672.1; -; mRNA.
DR EMBL; AK222092; BAD94983.1; -; mRNA.
DR RefSeq; NP_566714.1; NM_113163.4.
DR AlphaFoldDB; Q9LUJ7; -.
DR SMR; Q9LUJ7; -.
DR STRING; 3702.AT3G22640.1; -.
DR PaxDb; Q9LUJ7; -.
DR PRIDE; Q9LUJ7; -.
DR ProMEX; Q9LUJ7; -.
DR ProteomicsDB; 236834; -.
DR EnsemblPlants; AT3G22640.1; AT3G22640.1; AT3G22640.
DR GeneID; 821835; -.
DR Gramene; AT3G22640.1; AT3G22640.1; AT3G22640.
DR KEGG; ath:AT3G22640; -.
DR Araport; AT3G22640; -.
DR TAIR; locus:2094404; AT3G22640.
DR eggNOG; ENOG502QQEP; Eukaryota.
DR HOGENOM; CLU_018703_1_1_1; -.
DR InParanoid; Q9LUJ7; -.
DR OMA; ELTGDEC; -.
DR OrthoDB; 1072107at2759; -.
DR PhylomeDB; Q9LUJ7; -.
DR PRO; PR:Q9LUJ7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUJ7; baseline and differential.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 2.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..486
FT /note="Vicilin-like seed storage protein At3g22640"
FT /evidence="ECO:0000255"
FT /id="PRO_5004329289"
FT DOMAIN 64..223
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 278..448
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 34..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 117..119
FT /note="PHH -> STP (in Ref. 4; CAA81765)"
FT /evidence="ECO:0000305"
FT CONFLICT 135..136
FT /note="IE -> MR (in Ref. 4; CAA81765)"
FT /evidence="ECO:0000305"
FT CONFLICT 179..180
FT /note="TV -> HR (in Ref. 4; CAA82813)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="N -> D (in Ref. 4; CAA82813)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="E -> G (in Ref. 5; BAD94983)"
FT /evidence="ECO:0000305"
FT CONFLICT 366..374
FT /note="EEEDMSENV -> GGGRYELKTL (in Ref. 4; CAA81568)"
FT /evidence="ECO:0000305"
FT CONFLICT 381..382
FT /note="VC -> SV (in Ref. 4; CAA81568)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="Q -> L (in Ref. 4; CAA86672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 55063 MW; 325ECF68D9A6345B CRC64;
MAITNKLIIT LLLLISIAVV HCLSFRVEID EFEPPQQGEQ EGPRRRPGGG SGEGWEEEST
NHPYHFRKRS FSDWFQSKEG FVRVLPKFTK HAPALFRGIE NYRFSLVEME PTTFFVPHHL
DADAVFIVLQ GKGVIEFVTD KTKESFHITK GDVVRIPSGV TNFITNTNQT VPLRLAQITV
PVNNPGNYKD YFPAASQFQQ SYFNGFTKEV LSTSFNVPEE LLGRLVTRSK EIGQGIIRRI
SPDQIKELAE HATSPSNKHK AKKEKEEDKD LRTLWTPFNL FAIDPIYSND FGHFHEAHPK
NYNQLQDLHI AAAWANMTQG SLFLPHFNSK TTFVTFVENG CARFEMATPY KFQRGQQQWP
GQGQEEEEDM SENVHKVVSR VCKGEVFIVP AGHPFTILSQ DQDFIAVGFG IYATNSKRTF
LAGEENLLSN LNPAATRVTF GVGSKVAEKL FTSQNYSYFA PTSRSQQQIP EKHKPSFQSI
LDFAGF
