LTPG4_ARATH
ID LTPG4_ARATH Reviewed; 208 AA.
AC Q2PE70; O22272;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 4 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-4 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 4 {ECO:0000303|PubMed:23893219};
DE AltName: Full=Xylogen like protein 3 {ECO:0000303|PubMed:21558309};
DE Short=AtXYLP3 {ECO:0000303|PubMed:21558309};
DE Short=AtXYP3 {ECO:0000303|PubMed:21558309};
DE Flags: Precursor;
GN Name=LTPG4 {ECO:0000303|PubMed:23893219};
GN Synonyms=XYLP3 {ECO:0000303|PubMed:21558309},
GN XYP3 {ECO:0000303|PubMed:21558309};
GN OrderedLocusNames=At4g08670 {ECO:0000312|Araport:AT4G08670};
GN ORFNames=T3F12.2 {ECO:0000312|EMBL:AAB81871.1};
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 [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE
RP FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=21558309; DOI=10.1093/pcp/pcr060;
RA Kobayashi Y., Motose H., Iwamoto K., Fukuda H.;
RT "Expression and genome-wide analysis of the xylogen-type gene family.";
RL Plant Cell Physiol. 52:1095-1106(2011).
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 TISSUE SPECIFICITY.
RX PubMed=14671020; DOI=10.1105/tpc.014407;
RA Lalanne E., Honys D., Johnson A., Borner G.H.H., Lilley K.S., Dupree P.,
RA Grossniklaus U., Twell D.;
RT "SETH1 and SETH2, two components of the glycosylphosphatidylinositol anchor
RT biosynthetic pathway, are required for pollen germination and tube growth
RT in Arabidopsis.";
RL Plant Cell 16:229-240(2004).
RN [5]
RP REVIEW.
RX PubMed=23505340; DOI=10.1199/tab.0161;
RA Li-Beisson Y., Shorrosh B., Beisson F., Andersson M.X., Arondel V.,
RA Bates P.D., Baud S., Bird D., Debono A., Durrett T.P., Franke R.B.,
RA Graham I.A., Katayama K., Kelly A.A., Larson T., Markham J.E., Miquel M.,
RA Molina I., Nishida I., Rowland O., Samuels L., Schmid K.M., Wada H.,
RA Welti R., Xu C., Zallot R., Ohlrogge J.;
RT "Acyl-lipid metabolism.";
RL Arabidopsis Book 11:E0161-E0161(2013).
RN [6]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=23893219; DOI=10.1007/s11103-013-0113-5;
RA Edstam M.M., Blomqvist K., Ekloef A., Wennergren U., Edqvist J.;
RT "Coexpression patterns indicate that GPI-anchored non-specific lipid
RT transfer proteins are involved in accumulation of cuticular wax, suberin
RT and sporopollenin.";
RL Plant Mol. Biol. 83:625-649(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=24460633; DOI=10.1111/ppl.12156;
RA Edstam M.M., Edqvist J.;
RT "Involvement of GPI-anchored lipid transfer proteins in the development of
RT seed coats and pollen in Arabidopsis thaliana.";
RL Physiol. Plantarum 152:32-42(2014).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=30102837; DOI=10.1111/mpp.12740;
RA Fahlberg P., Buhot N., Johansson O.N., Andersson M.X.;
RT "Involvement of lipid transfer proteins in resistance against a non-host
RT powdery mildew in Arabidopsis thaliana.";
RL Mol. Plant Pathol. 20:69-77(2019).
CC -!- FUNCTION: Lipid transfer protein involved in seed and ovule maturation
CC and development, probably by regulating the fatty acids homeostasis
CC during suberin and sporopollenin biosynthesis or deposition.
CC {ECO:0000269|PubMed:24460633}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Confined to the anthers and stamen of the
CC inflorescence, especially in pollen. {ECO:0000269|PubMed:14671020,
CC ECO:0000269|PubMed:21558309, ECO:0000269|PubMed:23893219}.
CC -!- DEVELOPMENTAL STAGE: In the anthers, specifically expressed in pollen,
CC with levels varying during the different developmental stages.
CC {ECO:0000269|PubMed:21558309}.
CC -!- DISRUPTION PHENOTYPE: Some early aborted shrunken and deformed seeds,
CC with abnormal hair-like outgrowths, and infertile ovules, and increased
CC salt permeability in seeds associated with an increase in unsubstituted
CC fatty acids but a decrease in omega-hydroxy fatty acids in seed coats.
CC {ECO:0000269|PubMed:24460633}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB81871.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB77992.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB246322; BAE73259.1; -; mRNA.
DR EMBL; AC002983; AAB81871.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161512; CAB77992.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82667.1; -; Genomic_DNA.
DR PIR; T00941; T00941.
DR RefSeq; NP_192607.2; NM_116936.3.
DR AlphaFoldDB; Q2PE70; -.
DR STRING; 3702.AT4G08670.1; -.
DR PaxDb; Q2PE70; -.
DR EnsemblPlants; AT4G08670.1; AT4G08670.1; AT4G08670.
DR GeneID; 826433; -.
DR Gramene; AT4G08670.1; AT4G08670.1; AT4G08670.
DR KEGG; ath:AT4G08670; -.
DR Araport; AT4G08670; -.
DR TAIR; locus:2138586; AT4G08670.
DR HOGENOM; CLU_095117_0_0_1; -.
DR InParanoid; Q2PE70; -.
DR OMA; TDSCCAG; -.
DR OrthoDB; 1478198at2759; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q2PE70; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR Gene3D; 1.10.110.10; -; 1.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR InterPro; IPR043325; LTSS.
DR InterPro; IPR000528; Plant_nsLTP.
DR PANTHER; PTHR33044; PTHR33044; 1.
DR Pfam; PF14368; LTP_2; 1.
DR PRINTS; PR00382; LIPIDTRNSFER.
DR SMART; SM00499; AAI; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..179
FT /note="Non-specific lipid transfer protein GPI-anchored 4"
FT /id="PRO_5014308757"
FT PROPEP 180..208
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451637"
FT REGION 136..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 179
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 48..91
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 58..75
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 76..116
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 89..125
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 208 AA; 20852 MW; 4017587C617D555F CRC64;
MKQSLLLSFV LLLLSSSSLV TPIHARNKSN PAKSPVGAPA PGPSSSDCST VIYSMMDCLG
YLGVGSNETK PEKSCCTGIE TVLQYNPQCI CAGLVSAGEM GIELNSTRAL ATPKACKLSI
APPHCGIITS GATTPGASPV SPSAGAPTTS PSAAKSPETS ATSPSSDETP SMTAPSPSSS
GTNILSVPAL TIVFVIVSSV AYISAFSN
