LTG12_ARATH
ID LTG12_ARATH Reviewed; 176 AA.
AC Q9ZVC7; Q8L963;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Non-specific lipid transfer protein GPI-anchored 12 {ECO:0000303|PubMed:23893219};
DE Short=AtLTPG-12 {ECO:0000303|PubMed:23893219};
DE Short=Protein LTP-GPI-ANCHORED 12 {ECO:0000303|PubMed:23893219};
DE AltName: Full=Xylogen-like protein 13 {ECO:0000303|PubMed:21558309};
DE Short=AtXYLP13 {ECO:0000303|PubMed:21558309};
DE Short=AtXYP11 {ECO:0000303|PubMed:21558309};
DE Flags: Precursor;
GN Name=LTPG12 {ECO:0000303|PubMed:23893219};
GN Synonyms=XYLP13 {ECO:0000303|PubMed:21558309},
GN XYP11 {ECO:0000303|PubMed:21558309};
GN OrderedLocusNames=At2g27130 {ECO:0000312|Araport:AT2G27130};
GN ORFNames=T20P8.18 {ECO:0000312|EMBL:AAC77871.2};
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, GENE FAMILY, AND
RP 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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 -!- TISSUE SPECIFICITY: Preferentially expressed in the endodermis of
CC hypocotyls and roots of seedlings, and in petals and anthers of
CC inflorescences (PubMed:21558309). May also be expressed in siliques,
CC carpels and pedicels (PubMed:21558309). {ECO:0000269|PubMed:21558309}.
CC -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
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DR EMBL; AB246330; BAE73267.1; -; mRNA.
DR EMBL; AC005623; AAC77871.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07941.1; -; Genomic_DNA.
DR EMBL; AY088619; AAM67343.1; -; mRNA.
DR EMBL; AK175860; BAD43623.1; -; mRNA.
DR EMBL; AK175855; BAD43618.1; -; mRNA.
DR EMBL; AK175830; BAD43593.1; -; mRNA.
DR PIR; B84669; B84669.
DR RefSeq; NP_565637.1; NM_128271.4.
DR AlphaFoldDB; Q9ZVC7; -.
DR STRING; 3702.AT2G27130.1; -.
DR PaxDb; Q9ZVC7; -.
DR PRIDE; Q9ZVC7; -.
DR ProteomicsDB; 242557; -.
DR EnsemblPlants; AT2G27130.1; AT2G27130.1; AT2G27130.
DR GeneID; 817255; -.
DR Gramene; AT2G27130.1; AT2G27130.1; AT2G27130.
DR KEGG; ath:AT2G27130; -.
DR Araport; AT2G27130; -.
DR TAIR; locus:2059242; AT2G27130.
DR eggNOG; ENOG502S59X; Eukaryota.
DR HOGENOM; CLU_089796_5_2_1; -.
DR InParanoid; Q9ZVC7; -.
DR OMA; EQLSTIC; -.
DR OrthoDB; 1573659at2759; -.
DR PhylomeDB; Q9ZVC7; -.
DR PRO; PR:Q9ZVC7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVC7; baseline and differential.
DR Genevisible; Q9ZVC7; AT.
DR GO; GO:0031225; C:anchored component of membrane; TAS:TAIR.
DR GO; GO:0046658; C:anchored component of plasma membrane; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
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 PANTHER; PTHR33044; PTHR33044; 1.
DR Pfam; PF14368; LTP_2; 1.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..149
FT /note="Non-specific lipid transfer protein GPI-anchored 12"
FT /id="PRO_0000259450"
FT PROPEP 150..176
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000259451"
FT LIPID 149
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 40..83
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 50..67
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 68..110
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT DISULFID 81..120
FT /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT CONFLICT 15
FT /note="L -> LV (in Ref. 4; AAM67343)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="V -> T (in Ref. 4; AAM67343)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="S -> T (in Ref. 4; AAM67343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 18089 MW; 0727AEA64F0BFE47 CRC64;
MLTTNTLAVL LLLFLSLCSG QSPPAPEPIA ADGPSSPVNC LVSMLNVSDC FSYVQVGSNE
IKPEAACCPE LAGMVQSSPE CVCNLYGGGA SPRFGVKLDK QRAEQLSTIC GVKAPSPSLC
SVLGFPTISP AGSEDSSSGS EGSDKDKKNG AMTTKYCGVA LNSLALLLLF TFLSLS
