GRP19_ARATH
ID GRP19_ARATH Reviewed; 106 AA.
AC Q42574;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Tapetal oleosin GRP-19 {ECO:0000303|PubMed:11431566};
DE Short=T-oleosin GRP-19 {ECO:0000305|PubMed:26305561};
DE AltName: Full=Glycine-rich protein 19 {ECO:0000303|PubMed:11431566};
DE Short=AtGRP19 {ECO:0000303|PubMed:11431566};
DE AltName: Full=Oleopollenin GRP-19 {ECO:0000305|PubMed:14739246};
DE AltName: Full=Putative glycine-rich protein 1 {ECO:0000303|PubMed:11929861};
DE Short=PutG-1 {ECO:0000303|PubMed:11929861};
GN Name=GRP19 {ECO:0000303|PubMed:11431566};
GN Synonyms=PUTG1 {ECO:0000303|PubMed:11929861};
GN OrderedLocusNames=At5g07550 {ECO:0000312|Araport:AT5G07550};
GN ORFNames=T2I1.260 {ECO:0000312|EMBL:CAB87944.1};
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=8220457; DOI=10.1046/j.1365-313x.1993.03040495.x;
RA de Oliveira D.E., Franco L.O., Simoens C., Seurinck J., Coppieters J.,
RA Botterman J., Van Montagu M.;
RT "Inflorescence-specific genes from Arabidopsis thaliana encoding glycine-
RT rich proteins.";
RL Plant J. 3:495-507(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Kas-1, cv. Landsberg erecta, and cv. Wassilewskija-2;
RX PubMed=11431566; DOI=10.1126/science.1060972;
RA Mayfield J.A., Fiebig A., Johnstone S.E., Preuss D.;
RT "Gene families from the Arabidopsis thaliana pollen coat proteome.";
RL Science 292:2482-2485(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
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 [5]
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 [6]
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 [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11929861; DOI=10.1074/jbc.m109298200;
RA Kim H.U., Hsieh K., Ratnayake C., Huang A.H.C.;
RT "A novel group of oleosins is present inside the pollen of Arabidopsis.";
RL J. Biol. Chem. 277:22677-22684(2002).
RN [8]
RP TISSUE SPECIFICITY, AND GENE FAMILY.
RX PubMed=14739246; DOI=10.1093/molbev/msh059;
RA Schein M., Yang Z., Mitchell-Olds T., Schmid K.J.;
RT "Rapid evolution of a pollen-specific oleosin-like gene family from
RT Arabidopsis thaliana and closely related species.";
RL Mol. Biol. Evol. 21:659-669(2004).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND PROTEOLYTIC CLEAVAGE.
RC STRAIN=cv. Columbia;
RX PubMed=26305561; DOI=10.1111/nph.13611;
RA Levesque-Lemay M., Chabot D., Hubbard K., Chan J.K., Miller S.,
RA Robert L.S.;
RT "Tapetal oleosins play an essential role in tapetosome formation and
RT protein relocation to the pollen coat.";
RL New Phytol. 209:691-704(2016).
CC -!- FUNCTION: Lipid-binding oleosin involved in anther tapetum development,
CC especially for the physiology of tapetosomes (PubMed:26305561). Also
CC implicated in the formation of pollen coat (PubMed:26305561).
CC {ECO:0000269|PubMed:26305561}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, pollen coat {ECO:0000269|PubMed:11431566,
CC ECO:0000269|PubMed:26305561}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q9LY09}. Membrane {ECO:0000255}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Surface of oil bodies (By
CC similarity). Oleosins exist at a monolayer lipid/water interface (By
CC similarity). Associated with discrete organelles within the anther
CC tapetum called tapetosomes and with a network of structures previously
CC described as fibrils or 'strings of beads' (PubMed:26305561).
CC {ECO:0000250|UniProtKB:C3S7F0, ECO:0000269|PubMed:26305561}.
CC -!- TISSUE SPECIFICITY: Present in pollen (at protein level)
CC (PubMed:11431566, PubMed:26305561). Inflorescence-specific expression,
CC especially in flowers florets (PubMed:11929861, PubMed:14739246).
CC {ECO:0000269|PubMed:11431566, ECO:0000269|PubMed:11929861,
CC ECO:0000269|PubMed:14739246, ECO:0000269|PubMed:26305561}.
CC -!- DEVELOPMENTAL STAGE: In flowers, present in the anther tapetum early in
CC anther development and later in the pollen coat (PubMed:11929861,
CC PubMed:26305561). Upon tapetum degeneration, associated with
CC tapetosomal debris 'in transit' to the pollen cell wall in the anther
CC locule (PubMed:26305561). {ECO:0000269|PubMed:11929861,
CC ECO:0000269|PubMed:26305561}.
CC -!- PTM: Proteolytically cleaved following anther tapetal breakdown.
CC {ECO:0000269|PubMed:26305561}.
CC -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR EMBL; Z11858; CAA77884.1; -; Genomic_DNA.
DR EMBL; AF362474; AAK83827.1; -; Genomic_DNA.
DR EMBL; AF362478; AAK83840.1; -; Genomic_DNA.
DR EMBL; AF362479; AAK83841.1; -; Genomic_DNA.
DR EMBL; AL163912; CAB87944.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91175.1; -; Genomic_DNA.
DR EMBL; AY063954; AAL36310.1; -; mRNA.
DR EMBL; AY114071; AAM45119.1; -; mRNA.
DR EMBL; AY088559; AAM66091.1; -; mRNA.
DR PIR; S24835; S24835.
DR RefSeq; NP_196372.1; NM_120837.5.
DR AlphaFoldDB; Q42574; -.
DR STRING; 3702.AT5G07550.1; -.
DR PaxDb; Q42574; -.
DR PRIDE; Q42574; -.
DR ProteomicsDB; 175300; -.
DR EnsemblPlants; AT5G07550.1; AT5G07550.1; AT5G07550.
DR GeneID; 830648; -.
DR Gramene; AT5G07550.1; AT5G07550.1; AT5G07550.
DR Araport; AT5G07550; -.
DR TAIR; locus:2183414; AT5G07550.
DR HOGENOM; CLU_144388_1_0_1; -.
DR InParanoid; Q42574; -.
DR OMA; MWLFKKI; -.
DR OrthoDB; 1619644at2759; -.
DR PhylomeDB; Q42574; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q42574; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0012511; C:monolayer-surrounded lipid storage body; IEA:InterPro.
DR GO; GO:0070505; C:pollen coat; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; ISS:TAIR.
DR GO; GO:0048655; P:anther wall tapetum morphogenesis; IDA:UniProtKB.
DR GO; GO:0019915; P:lipid storage; IBA:GO_Central.
DR GO; GO:0019953; P:sexual reproduction; IBA:GO_Central.
DR InterPro; IPR000136; Oleosin.
DR PANTHER; PTHR33203; PTHR33203; 1.
DR Pfam; PF01277; Oleosin; 1.
DR PROSITE; PS00811; OLEOSINS; 1.
PE 1: Evidence at protein level;
KW Extracellular matrix; Lipid droplet; Membrane; Reference proteome;
KW Secreted; Transmembrane; Transmembrane helix.
FT CHAIN 1..106
FT /note="Tapetal oleosin GRP-19"
FT /id="PRO_0000454877"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 84..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 106 AA; 10683 MW; F52C47547FC9521E CRC64;
MFEIIQAVFS AGVALALLTF AGITLGGSVV ACIISTPLFV IFSPVLVPAT IATTLLASGF
TASGSFGATA FTILSWLYKK RTGRDLPKIP GLTPPAPASN PAGSGV
