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LTG29_ARATH
ID   LTG29_ARATH             Reviewed;         158 AA.
AC   Q9FY78; Q8LD67;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 143.
DE   RecName: Full=Non-specific lipid transfer protein GPI-anchored 29 {ECO:0000303|PubMed:23893219};
DE            Short=AtLTPG-29 {ECO:0000303|PubMed:23893219};
DE            Short=Protein LTP-GPI-ANCHORED 29 {ECO:0000303|PubMed:23893219};
DE   AltName: Full=Xylogen like protein 4 {ECO:0000312|EMBL:BAE73260.1};
DE            Short=AtXYLP4 {ECO:0000303|PubMed:21558309};
DE            Short=AtXYP4 {ECO:0000303|PubMed:21558309};
DE   Flags: Precursor;
GN   Name=LTPG29 {ECO:0000303|PubMed:23893219};
GN   Synonyms=XYLP4 {ECO:0000303|PubMed:21558309},
GN   XYP4 {ECO:0000303|PubMed:21558309};
GN   OrderedLocusNames=At5g09370 {ECO:0000312|Araport:AT5G09370};
GN   ORFNames=T5E8.170 {ECO:0000312|EMBL:CAC05463.1};
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] (ISOFORM 1), TISSUE SPECIFICITY, GENE FAMILY,
RP   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=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;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=16299181; DOI=10.1104/pp.105.067314;
RA   Yu H.-J., Hogan P., Sundaresan V.;
RT   "Analysis of the female gametophyte transcriptome of Arabidopsis by
RT   comparative expression profiling.";
RL   Plant Physiol. 139:1853-1869(2005).
RN   [7]
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: [Isoform 2]: Secreted {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000255}; Lipid-
CC       anchor, GPI-anchor {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9FY78-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9FY78-2; Sequence=VSP_060824, VSP_060825;
CC   -!- TISSUE SPECIFICITY: Confined to the ovaries of the inflorescence.
CC       {ECO:0000269|PubMed:16299181, ECO:0000269|PubMed:21558309}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Has no GPI-anchor. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR   EMBL; AB246323; BAE73260.1; -; mRNA.
DR   EMBL; AL391712; CAC05463.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91382.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91383.1; -; Genomic_DNA.
DR   EMBL; AK118479; BAC43083.1; -; mRNA.
DR   EMBL; AY086176; AAM63379.1; -; mRNA.
DR   RefSeq; NP_568210.1; NM_120973.5. [Q9FY78-2]
DR   RefSeq; NP_850800.1; NM_180469.4. [Q9FY78-1]
DR   AlphaFoldDB; Q9FY78; -.
DR   SMR; Q9FY78; -.
DR   STRING; 3702.AT5G09370.1; -.
DR   PaxDb; Q9FY78; -.
DR   EnsemblPlants; AT5G09370.1; AT5G09370.1; AT5G09370. [Q9FY78-1]
DR   EnsemblPlants; AT5G09370.2; AT5G09370.2; AT5G09370. [Q9FY78-2]
DR   GeneID; 830796; -.
DR   Gramene; AT5G09370.1; AT5G09370.1; AT5G09370. [Q9FY78-1]
DR   Gramene; AT5G09370.2; AT5G09370.2; AT5G09370. [Q9FY78-2]
DR   KEGG; ath:AT5G09370; -.
DR   Araport; AT5G09370; -.
DR   TAIR; locus:2184817; AT5G09370.
DR   HOGENOM; CLU_089796_5_2_1; -.
DR   InParanoid; Q9FY78; -.
DR   OMA; ECSAMIM; -.
DR   OrthoDB; 1492100at2759; -.
DR   PhylomeDB; Q9FY78; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FY78; baseline and differential.
DR   GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   GPI-anchor; Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..134
FT                   /note="Non-specific lipid transfer protein GPI-anchored 29"
FT                   /id="PRO_5014312872"
FT   PROPEP          135..158
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000451661"
FT   LIPID           134
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        28..71
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        38..55
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        56..95
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        69..105
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   VAR_SEQ         120..129
FT                   /note="APVWGSGWAP -> GKWNLFGLFA (in isoform 2)"
FT                   /id="VSP_060824"
FT   VAR_SEQ         130..158
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_060825"
SQ   SEQUENCE   158 AA;  16164 MW;  C19AB682BE9F28D6 CRC64;
     MAYFSTATSL LLLVLSVSSP YVHGASDCDT LVITLFPCLP FISIGGTADT PTASCCSSLK
     NILDTKPICL CEGLKKAPLG IKLNVTKSAT LPVACKLNAP PVSACDSLPP ASPPTANGQA
     PVWGSGWAPA PSPSKGNSLI PISGFSFVIV TALAMFRI
 
 
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