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LTG21_ARATH
ID   LTG21_ARATH             Reviewed;         205 AA.
AC   Q1G2Y5; A0MFR9; Q9LR49;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Non-specific lipid transfer protein GPI-anchored 21 {ECO:0000303|PubMed:23893219};
DE            Short=AtLTPG-21 {ECO:0000303|PubMed:23893219};
DE            Short=Protein LTP-GPI-ANCHORED 21 {ECO:0000303|PubMed:23893219};
DE   Flags: Precursor;
GN   Name=LTPG21 {ECO:0000303|PubMed:23893219};
GN   OrderedLocusNames=At1g05450 {ECO:0000312|Araport:AT1G05450};
GN   ORFNames=T25N20.10 {ECO:0000312|EMBL:AAF79724.1};
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
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   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF79724.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=ABK28778.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC005106; AAF79724.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE27841.1; -; Genomic_DNA.
DR   EMBL; DQ492243; ABF59172.1; -; mRNA.
DR   EMBL; DQ653396; ABK28778.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_973763.1; NM_202034.3.
DR   AlphaFoldDB; Q1G2Y5; -.
DR   STRING; 3702.AT1G05450.2; -.
DR   PaxDb; Q1G2Y5; -.
DR   PRIDE; Q1G2Y5; -.
DR   ProteomicsDB; 185439; -.
DR   EnsemblPlants; AT1G05450.2; AT1G05450.2; AT1G05450.
DR   GeneID; 837046; -.
DR   Gramene; AT1G05450.2; AT1G05450.2; AT1G05450.
DR   KEGG; ath:AT1G05450; -.
DR   Araport; AT1G05450; -.
DR   TAIR; locus:2201046; AT1G05450.
DR   eggNOG; ENOG502RZXE; Eukaryota.
DR   HOGENOM; CLU_085549_3_0_1; -.
DR   InParanoid; Q1G2Y5; -.
DR   OMA; MDPDGMP; -.
DR   OrthoDB; 1573578at2759; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q1G2Y5; 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   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..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..179
FT                   /note="Non-specific lipid transfer protein GPI-anchored 21"
FT                   /id="PRO_5014308292"
FT   PROPEP          180..205
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000451652"
FT   REGION          116..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           179
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        33..75
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        44..59
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        60..100
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        73..109
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ   SEQUENCE   205 AA;  20621 MW;  CD049B3FE271B27F CRC64;
     MNSNSFLISA ALIFSLLSSN SPTSILAQIN TPCSPSMLSS VTGCTSFLTG GGSFPTSDCC
     GALKSLTGTG MDCLCLIVTA GVPISIPINR TLAISLPRAC GIPGVPVQCK ASAAPLPTPG
     PASFGPTTSP TDSQTSDPEG SASFRPPTSP TTSQTPNDKD LSGSGNGGDP MGFAPPPPSS
     SPSSSHSLKL SYLLFAFAFT IIKFI
 
 
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