LTG34_ARATH
ID LTG34_ARATH Reviewed; 142 AA.
AC Q9SUV6; O49646;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 34 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-34 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 34 {ECO:0000303|PubMed:23893219};
DE Flags: Precursor;
GN Name=LTPG34 {ECO:0000303|PubMed:23893219};
GN OrderedLocusNames=At4g22650 {ECO:0000312|Araport:AT4G22650};
GN ORFNames=T12H17.40 {ECO:0000312|EMBL:CAA16550.1};
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=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 [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 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).
CC -!- FUNCTION: Probable lipid transfer protein.
CC {ECO:0000250|UniProtKB:Q9C7F7}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE84634.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA16550.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA22170.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79220.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021635; CAA16550.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL033545; CAA22170.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161557; CAB79220.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84634.1; ALT_SEQ; Genomic_DNA.
DR PIR; D85259; D85259.
DR PIR; T04560; T04560.
DR RefSeq; NP_193996.1; NM_118391.1.
DR AlphaFoldDB; Q9SUV6; -.
DR PaxDb; Q9SUV6; -.
DR PRIDE; Q9SUV6; -.
DR GeneID; 828361; -.
DR KEGG; ath:AT4G22650; -.
DR Araport; AT4G22650; -.
DR TAIR; locus:2127590; AT4G22650.
DR HOGENOM; CLU_1689128_0_0_1; -.
DR OrthoDB; 1860095at2759; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUV6; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR036312; Bifun_inhib/LTP/seed_sf.
DR InterPro; IPR016140; Bifunc_inhib/LTP/seed_store.
DR Pfam; PF14368; LTP_2; 1.
DR SUPFAM; SSF47699; SSF47699; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..120
FT /note="Non-specific lipid transfer protein GPI-anchored 34"
FT /id="PRO_5014313322"
FT PROPEP 121..142
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451663"
FT REGION 21..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 120
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..85
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 57..69
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 70..106
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 83..114
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ SEQUENCE 142 AA; 15077 MW; 5DCEBE713FEB484C CRC64;
MAVAVTAVLF LAVVIAPQWT ETKKPPRPSD TSDTSGTSGR DRRTMCPLSI PGIVQNCYAT
LNAFPSKECC KDLKTASKRE VTCLCNNVIA HPDPLYTNTN QVNKACGVLD KYACDAGNSN
GGATKKIVAS MGLFGVVASL FF
