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LTG17_ARATH
ID   LTG17_ARATH             Reviewed;         116 AA.
AC   Q8GYS8; A0A1I9LT01; Q8LFZ3; Q9LJ89;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=Non-specific lipid transfer protein GPI-anchored 17 {ECO:0000303|PubMed:23893219};
DE            Short=AtLTPG-17 {ECO:0000303|PubMed:23893219};
DE            Short=Protein LTP-GPI-ANCHORED 17 {ECO:0000303|PubMed:23893219};
DE   Flags: Precursor;
GN   Name=LTPG17 {ECO:0000303|PubMed:23893219};
GN   OrderedLocusNames=At3g22570 {ECO:0000312|Araport:AT3G22570};
GN   ORFNames=F16J14.13 {ECO:0000312|EMBL:BAB01472.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
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].
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
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   [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).
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: Expressed in seedlings, preferentially in roots.
CC       {ECO:0000269|PubMed:23893219}.
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ANM65709.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAB01472.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP000731; BAB01472.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; ANM65709.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BT004995; AAO50528.1; -; mRNA.
DR   EMBL; AK117414; BAC42080.1; -; mRNA.
DR   EMBL; AY084552; AAM61119.1; -; mRNA.
DR   RefSeq; NP_001327657.1; NM_001338593.1.
DR   AlphaFoldDB; Q8GYS8; -.
DR   IntAct; Q8GYS8; 5.
DR   PaxDb; Q8GYS8; -.
DR   PeptideAtlas; Q8GYS8; -.
DR   ProteomicsDB; 195447; -.
DR   EnsemblPlants; AT3G22570.2; AT3G22570.2; AT3G22570.
DR   GeneID; 821829; -.
DR   Gramene; AT3G22570.2; AT3G22570.2; AT3G22570.
DR   KEGG; ath:AT3G22570; -.
DR   Araport; AT3G22570; -.
DR   TAIR; locus:2077056; AT3G22570.
DR   HOGENOM; CLU_2100246_0_0_1; -.
DR   PhylomeDB; Q8GYS8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8GYS8; 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   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   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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..107
FT                   /note="Non-specific lipid transfer protein GPI-anchored 17"
FT                   /id="PRO_5010847050"
FT   PROPEP          108..116
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000451648"
FT   LIPID           107
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        31..74
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        42..58
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        59..99
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   CONFLICT        15
FT                   /note="V -> A (in Ref. 5; AAM61119)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   116 AA;  12580 MW;  C7AC4CE694D205C1 CRC64;
     MKIGVVLVLL TVFVVVMSST SVSAQSDEDE CLKETGQMQL NCFPYLTDNR IHTPSFACCS
     EVYTVGKTYV DCFCQFINNG GPSFGIVVSQ KLLDLPELCG VYGACGNGKN FKNTSL
 
 
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