GRP17_ARATH
ID GRP17_ARATH Reviewed; 543 AA.
AC Q9LY09; B3H5N1; Q43302;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Tapetal oleosin GRP-17 {ECO:0000303|PubMed:11431566};
DE Short=T-oleosin GRP-17 {ECO:0000305|PubMed:26305561};
DE AltName: Full=Glycine rich protein 17 {ECO:0000303|PubMed:11431566};
DE Short=AtGRP-17 {ECO:0000303|PubMed:11431566};
DE AltName: Full=Glycine rich protein 7 {ECO:0000303|PubMed:8220457};
DE Short=AtGRP-7 {ECO:0000303|PubMed:8220457};
DE AltName: Full=Oleopollenin GRP-17 {ECO:0000305|PubMed:14739246};
GN Name=GRP17 {ECO:0000303|PubMed:11431566};
GN Synonyms=GRP7 {ECO:0000303|PubMed:8220457};
GN OrderedLocusNames=At5g07530 {ECO:0000312|Araport:AT5G07530};
GN ORFNames=T2I1.240 {ECO:0000312|EMBL:CAB87942.1};
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 / MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Stamen;
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 [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 [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] (ISOFORM 1).
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 171-189 AND 511-528, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Wassilewskija-2;
RX PubMed=10655594; DOI=10.1038/35000084;
RA Mayfield J.A., Preuss D.;
RT "Rapid initiation of Arabidopsis pollination requires the oleosin-domain
RT protein GRP17.";
RL Nat. Cell Biol. 2:128-130(2000).
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, AND DISRUPTION PHENOTYPE.
RX PubMed=20033440; DOI=10.1007/s00497-009-0104-5;
RA Updegraff E.P., Zhao F., Preuss D.;
RT "The extracellular lipase EXL4 is required for efficient hydration of
RT Arabidopsis pollen.";
RL Sex. Plant Reprod. 22:197-204(2009).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RC STRAIN=cv. Columbia, cv. Wassilewskija, and cv. Wassilewskija-2;
RX PubMed=23602096; DOI=10.1016/j.plantsci.2013.02.008;
RA Suzuki T., Tsunekawa S., Koizuka C., Yamamoto K., Imamura J., Nakamura K.,
RA Ishiguro S.;
RT "Development and disintegration of tapetum-specific lipid-accumulating
RT organelles, elaioplasts and tapetosomes, in Arabidopsis thaliana and
RT Brassica napus.";
RL Plant Sci. 207:25-36(2013).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, 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 pollen coat protein required to mediate
CC pollen recognition by stigma cells and subsequent pollen hydration
CC (PubMed:10655594, PubMed:20033440, PubMed:26305561). Involved in anther
CC tapetum development, especially for the physiology of tapetosomes
CC (PubMed:26305561). Also implicated in the formation of pollen coat
CC (PubMed:26305561). {ECO:0000269|PubMed:10655594,
CC ECO:0000269|PubMed:20033440, ECO:0000269|PubMed:26305561}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, pollen coat {ECO:0000269|PubMed:10655594,
CC ECO:0000269|PubMed:11431566, ECO:0000269|PubMed:26305561}. Lipid
CC droplet {ECO:0000250|UniProtKB:C3S7F0}. Membrane {ECO:0000255}; Multi-
CC pass 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 (e.g. granules of 1-5
CC um in diameter) within the anther tapetum called tapetosomes and with a
CC network of structures previously described as fibrils or 'strings of
CC beads' (PubMed:26305561, PubMed:23602096).
CC {ECO:0000250|UniProtKB:C3S7F0, ECO:0000269|PubMed:23602096,
CC ECO:0000269|PubMed:26305561}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LY09-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LY09-2; Sequence=VSP_044417, VSP_044418;
CC -!- TISSUE SPECIFICITY: Flower specific, especially in anther tapetum,
CC pollen (at protein level) and flowers florets.
CC {ECO:0000269|PubMed:10655594, ECO:0000269|PubMed:11431566,
CC ECO:0000269|PubMed:11929861, ECO:0000269|PubMed:14739246,
CC ECO:0000269|PubMed:23602096, ECO:0000269|PubMed:26305561,
CC ECO:0000269|PubMed:8220457}.
CC -!- DEVELOPMENTAL STAGE: Mostly expressed in anthers at the later stage of
CC flower development until tapetum degeneration (PubMed:8220457,
CC PubMed:23602096). 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, PubMed:23602096). Translocates from the pollen
CC coat at exine cavities to the site of contact between the pollen grain
CC and a papillar cell, called 'foot', 10 minutes after pollen landing;
CC the pollen tube elongation initiates later (about 20 minutes after
CC pollination) at the foot (PubMed:26305561).
CC {ECO:0000269|PubMed:11929861, ECO:0000269|PubMed:23602096,
CC ECO:0000269|PubMed:26305561, ECO:0000269|PubMed:8220457}.
CC -!- PTM: Proteolytically cleaved following anther tapetal breakdown.
CC {ECO:0000269|PubMed:23602096, ECO:0000269|PubMed:26305561}.
CC -!- DISRUPTION PHENOTYPE: Delayed pollen hydration and impaired competitive
CC ability due to a failure to interact with the stigma (PubMed:10655594,
CC PubMed:20033440). Abnormal anther tapetum development
CC (PubMed:26305561). {ECO:0000269|PubMed:10655594,
CC ECO:0000269|PubMed:20033440, ECO:0000269|PubMed:26305561}.
CC -!- SIMILARITY: Belongs to the oleosin family. {ECO:0000305}.
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DR EMBL; Z11858; CAA77882.1; -; Genomic_DNA.
DR EMBL; Z11868; CAA77894.1; -; mRNA.
DR EMBL; AL163912; CAB87942.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91171.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91172.1; -; Genomic_DNA.
DR EMBL; AK229852; BAF01681.1; -; mRNA.
DR PIR; S19933; S19933.
DR PIR; T49892; T49892.
DR RefSeq; NP_001119185.1; NM_001125713.1. [Q9LY09-2]
DR RefSeq; NP_196370.1; NM_120835.3. [Q9LY09-1]
DR AlphaFoldDB; Q9LY09; -.
DR BioGRID; 15925; 3.
DR STRING; 3702.AT5G07530.1; -.
DR iPTMnet; Q9LY09; -.
DR PaxDb; Q9LY09; -.
DR PRIDE; Q9LY09; -.
DR ProteomicsDB; 222299; -. [Q9LY09-1]
DR EnsemblPlants; AT5G07530.1; AT5G07530.1; AT5G07530. [Q9LY09-1]
DR EnsemblPlants; AT5G07530.2; AT5G07530.2; AT5G07530. [Q9LY09-2]
DR GeneID; 830646; -.
DR Gramene; AT5G07530.1; AT5G07530.1; AT5G07530. [Q9LY09-1]
DR Gramene; AT5G07530.2; AT5G07530.2; AT5G07530. [Q9LY09-2]
DR KEGG; ath:AT5G07530; -.
DR Araport; AT5G07530; -.
DR TAIR; locus:2183384; AT5G07530.
DR HOGENOM; CLU_532500_0_0_1; -.
DR OMA; EFHYRGQ; -.
DR OrthoDB; 1573729at2759; -.
DR PRO; PR:Q9LY09; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LY09; baseline and differential.
DR Genevisible; Q9LY09; AT.
DR GO; GO:0031012; C:extracellular matrix; IDA:TAIR.
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:0009859; P:pollen hydration; IMP:UniProtKB.
DR GO; GO:0048544; P:recognition of pollen; IMP:UniProtKB.
DR GO; GO:0019953; P:sexual reproduction; IBA:GO_Central.
DR InterPro; IPR000136; Oleosin.
DR PANTHER; PTHR33203; PTHR33203; 5.
DR Pfam; PF01277; Oleosin; 1.
DR PROSITE; PS00811; OLEOSINS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Extracellular matrix;
KW Lipid droplet; Membrane; Reference proteome; Repeat; Secreted;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..543
FT /note="Tapetal oleosin GRP-17"
FT /id="PRO_0000420171"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 220..223
FT /note="1"
FT REPEAT 227..230
FT /note="2"
FT REPEAT 234..237
FT /note="3"
FT REPEAT 259..262
FT /note="4"
FT REPEAT 269..272
FT /note="5"
FT REPEAT 276..279
FT /note="6"
FT REPEAT 301..304
FT /note="7"
FT REPEAT 305..308
FT /note="8"
FT REPEAT 312..315
FT /note="9"
FT REPEAT 319..322
FT /note="10"
FT REPEAT 344..347
FT /note="11"
FT REPEAT 348..351
FT /note="12"
FT REPEAT 355..358
FT /note="13"
FT REPEAT 362..365
FT /note="14"
FT REPEAT 387..390
FT /note="15"
FT REPEAT 391..394
FT /note="16"
FT REPEAT 398..401
FT /note="17"
FT REPEAT 405..408
FT /note="18"
FT REPEAT 410..413
FT /note="19"
FT REPEAT 414..417
FT /note="20"
FT REPEAT 438..441
FT /note="21"
FT REPEAT 445..448
FT /note="22"
FT REPEAT 458..461
FT /note="23"
FT REPEAT 464..467
FT /note="24"
FT REPEAT 468..471
FT /note="25"
FT REPEAT 492..495
FT /note="26"
FT REPEAT 499..502
FT /note="27"
FT REPEAT 506..509
FT /note="28"
FT REPEAT 511..514
FT /note="29"
FT REGION 1..67
FT /note="Polar"
FT /evidence="ECO:0000250"
FT REGION 68..162
FT /note="Hydrophobic"
FT /evidence="ECO:0000250"
FT REGION 148..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..514
FT /note="29 X 4 AA approximate tandem repeats of G-M-S-G"
FT COMPBIAS 314..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 468..512
FT /note="GSGSKHKIGGGKHGGLRGKFGKKRGMSGSEGGMSGSEGGMSESGM -> VEG
FT VNTKSEEVNTNLEEVNTEVEVATWRSKEQWSSCSNIKQIIVH (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044417"
FT VAR_SEQ 513..543
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044418"
FT CONFLICT 344
FT /note="S -> G (in Ref. 1; CAA77882/CAA77894)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="N -> K (in Ref. 1; CAA77882/CAA77894)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="R -> G (in Ref. 1; CAA77882/CAA77894)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 543 AA; 53193 MW; 08E7A0488EB4BDB8 CRC64;
MSEELSQKPS SAQSLSLREG RNRFPFLSLS QREGRFFPSL SLSERDGRKF SFLSMFSFLM
PLLEVIKIII ASVASVIFVG FACVTLAGSA AALVVSTPVF IIFSPVLVPA TIATVVLATG
FTAGGSFGAT ALGLIMWLVK RRMGVKPKDN PPPAGLPPNS GAGAGGAQSL IKKSKAKSKG
GLKAWCKKML KSKFGGKKGK SGGGKSKFGG KGGKSEGEEG MSSGDEGMSG SEGGMSGGEG
GKSKSGKGKL KAKLEKKKGM SGGSESEEGM SGSEGGMSGG GGSKSKSKKS KLKAKLGKKK
GMSGGMSGSE EGMSGSEGGM SSGGGSKSKS KKSKLKAKLG KKKSMSGGMS GSEEGMSGSE
GGMSGGGGGK SKSRKSKLKA NLGKKKCMSG GMSGSEGGMS RSEGGISGGG MSGGSGSKHK
IGGGKHGGLG GKFGKKRGMS GSGGGMSGSE GGVSGSEGSM SGGGMSGGSG SKHKIGGGKH
GGLRGKFGKK RGMSGSEGGM SGSEGGMSES GMSGSGGGKH KIGGGKHKFG GGKHGGGGGH
MAE
