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LTG33_ARATH
ID   LTG33_ARATH             Reviewed;         140 AA.
AC   O49645; Q9SUV7;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Non-specific lipid transfer protein GPI-anchored 33 {ECO:0000303|PubMed:23893219};
DE            Short=AtLTPG-33 {ECO:0000303|PubMed:23893219};
DE            Short=Protein LTP-GPI-ANCHORED 33 {ECO:0000303|PubMed:23893219};
DE   Flags: Precursor;
GN   Name=LTPG33 {ECO:0000303|PubMed:23893219};
GN   OrderedLocusNames=At4g22640 {ECO:0000312|Araport:AT4G22640};
GN   ORFNames=T12H17.30 {ECO:0000312|EMBL:CAA16549.1};
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O49645-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O49645-2; Sequence=VSP_060826;
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR   EMBL; AL021635; CAA16549.1; -; Genomic_DNA.
DR   EMBL; AL033545; CAA22169.1; -; Genomic_DNA.
DR   EMBL; AL161557; CAB79219.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84633.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM66157.1; -; Genomic_DNA.
DR   EMBL; BT010802; AAR24169.1; -; mRNA.
DR   EMBL; BT011284; AAR92320.1; -; mRNA.
DR   PIR; C85259; C85259.
DR   PIR; T04559; T04559.
DR   RefSeq; NP_001328070.1; NM_001341557.1. [O49645-1]
DR   RefSeq; NP_193995.1; NM_118390.3. [O49645-2]
DR   AlphaFoldDB; O49645; -.
DR   PRIDE; O49645; -.
DR   ProteomicsDB; 185213; -. [O49645-1]
DR   ProteomicsDB; 193665; -.
DR   EnsemblPlants; AT4G22640.1; AT4G22640.1; AT4G22640. [O49645-2]
DR   EnsemblPlants; AT4G22640.2; AT4G22640.2; AT4G22640. [O49645-1]
DR   GeneID; 828360; -.
DR   Gramene; AT4G22640.1; AT4G22640.1; AT4G22640. [O49645-2]
DR   Gramene; AT4G22640.2; AT4G22640.2; AT4G22640. [O49645-1]
DR   KEGG; ath:AT4G22640; -.
DR   Araport; AT4G22640; -.
DR   TAIR; locus:2127580; AT4G22640.
DR   HOGENOM; CLU_138794_0_0_1; -.
DR   OMA; VYHNDCG; -.
DR   OrthoDB; 1522870at2759; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O49645; 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   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   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   GPI-anchor; Lipoprotein; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..115
FT                   /note="Non-specific lipid transfer protein GPI-anchored 33"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5015096782"
FT   PROPEP          116..140
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000451662"
FT   LIPID           115
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        40..80
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        52..64
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        65..104
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        78..112
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   VAR_SEQ         115..139
FT                   /note="GDASGGSTNKIAASMVLLGLVASLF -> I (in isoform 2)"
FT                   /id="VSP_060826"
SQ   SEQUENCE   140 AA;  14753 MW;  9770BC193B41C234 CRC64;
     MAYTNKVTIS AAVATMMLFL AVTIVDAQSM PPMPKFNPVC ALADLPNIVQ LCYFNLDLTP
     SEECCNDLKS SSTIQVNCLC DNFIAHPSNG NISQARYDLV NSACGVADKF ACKGGDASGG
     STNKIAASMV LLGLVASLFF
 
 
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