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LTG22_ARATH
ID   LTG22_ARATH             Reviewed;         177 AA.
AC   Q9M2G1; A0A178VAD0; Q8LC73;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Non-specific lipid transfer protein GPI-anchored 22 {ECO:0000303|PubMed:23893219};
DE            Short=AtLTPG-22 {ECO:0000303|PubMed:23893219};
DE            Short=Protein LTP-GPI-ANCHORED 22 {ECO:0000303|PubMed:23893219};
DE   Flags: Precursor;
GN   Name=LTPG22 {ECO:0000303|PubMed:23893219};
GN   OrderedLocusNames=At3g58550 {ECO:0000312|Araport:AT3G58550};
GN   ORFNames=F14P22.140 {ECO:0000312|EMBL:CAB68193.1};
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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
CC       hypocotyls and roots (PubMed:23893219). Also observed in siliques
CC       (PubMed:23893219). {ECO:0000269|PubMed:23893219}.
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM63806.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL137082; CAB68193.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79798.1; -; Genomic_DNA.
DR   EMBL; AK119080; BAC43656.1; -; mRNA.
DR   EMBL; BT003738; AAO39966.1; -; mRNA.
DR   EMBL; AY086755; AAM63806.1; ALT_INIT; mRNA.
DR   PIR; T45675; T45675.
DR   RefSeq; NP_191414.1; NM_115717.3.
DR   AlphaFoldDB; Q9M2G1; -.
DR   STRING; 3702.AT3G58550.1; -.
DR   PaxDb; Q9M2G1; -.
DR   PRIDE; Q9M2G1; -.
DR   ProteomicsDB; 189354; -.
DR   EnsemblPlants; AT3G58550.1; AT3G58550.1; AT3G58550.
DR   GeneID; 825024; -.
DR   Gramene; AT3G58550.1; AT3G58550.1; AT3G58550.
DR   KEGG; ath:AT3G58550; -.
DR   Araport; AT3G58550; -.
DR   TAIR; locus:2076406; AT3G58550.
DR   eggNOG; ENOG502RZD2; Eukaryota.
DR   HOGENOM; CLU_089796_1_1_1; -.
DR   InParanoid; Q9M2G1; -.
DR   OMA; ITQCPEL; -.
DR   OrthoDB; 1546514at2759; -.
DR   PhylomeDB; Q9M2G1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M2G1; 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..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..152
FT                   /note="Non-specific lipid transfer protein GPI-anchored 22"
FT                   /id="PRO_5015099898"
FT   PROPEP          153..177
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000451653"
FT   LIPID           152
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        38..81
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        48..63
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        64..108
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        79..117
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
SQ   SEQUENCE   177 AA;  19291 MW;  63C620EE9231DD42 CRC64;
     MARFMAYNQN PQMLALCITV AVMFLGVRSE LSQDIKGCQD AMSDLYSCLP FVTNKAKAPD
     STCCSTLKVK IDKGQTRKCL CTLVKDRDDP GLGFKVDANR AMSLPSACHV PANISQCPDL
     LHLLPDSPAS QIFKQFTESS SQTVGHKAVS TSSSIKGRDN KQFGLMMAGA LSIWYIM
 
 
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