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LTPG8_ARATH
ID   LTPG8_ARATH             Reviewed;         152 AA.
AC   B3H587; Q9C6B5; Q9FX47;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Non-specific lipid transfer protein GPI-anchored 8 {ECO:0000303|PubMed:23893219};
DE            Short=AtLTPG-8 {ECO:0000303|PubMed:23893219};
DE            Short=Protein LTP-GPI-ANCHORED 8 {ECO:0000303|PubMed:23893219};
DE   Flags: Precursor;
GN   Name=LTPG8 {ECO:0000303|PubMed:23893219};
GN   OrderedLocusNames=At1g73550 {ECO:0000312|EMBL:AEE35474.1};
GN   ORFNames=F6D5.6 {ECO:0000312|EMBL:AAG51811.1},
GN   T9L24.29 {ECO:0000312|EMBL:AAG30973.1};
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;
RA   Kim C.J., Bautista V.R., Chen H., De Los Reyes C., Wu S.Y., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=B3H587-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B3H587-2; Sequence=VSP_060822, VSP_060823;
CC   -!- SIMILARITY: Belongs to the plant LTP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG51811.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC012396; AAG30973.1; -; Genomic_DNA.
DR   EMBL; AC079676; AAG51811.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE35474.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35475.1; -; Genomic_DNA.
DR   EMBL; BT030072; ABN04810.1; -; mRNA.
DR   PIR; C96762; C96762.
DR   RefSeq; NP_001117596.1; NM_001124124.2. [B3H587-2]
DR   RefSeq; NP_177496.3; NM_106013.5. [B3H587-1]
DR   AlphaFoldDB; B3H587; -.
DR   PaxDb; B3H587; -.
DR   EnsemblPlants; AT1G73550.1; AT1G73550.1; AT1G73550. [B3H587-1]
DR   EnsemblPlants; AT1G73550.2; AT1G73550.2; AT1G73550. [B3H587-2]
DR   GeneID; 843689; -.
DR   Gramene; AT1G73550.1; AT1G73550.1; AT1G73550. [B3H587-1]
DR   Gramene; AT1G73550.2; AT1G73550.2; AT1G73550. [B3H587-2]
DR   KEGG; ath:AT1G73550; -.
DR   Araport; AT1G73550; -.
DR   TAIR; locus:2035057; AT1G73550.
DR   HOGENOM; CLU_116928_3_1_1; -.
DR   InParanoid; B3H587; -.
DR   OMA; PYIHSEL; -.
DR   OrthoDB; 1525005at2759; -.
DR   PhylomeDB; B3H587; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; B3H587; 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   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; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..124
FT                   /note="Non-specific lipid transfer protein GPI-anchored 8"
FT                   /id="PRO_5002788141"
FT   PROPEP          125..152
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000451642"
FT   LIPID           124
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        42..56
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        57..98
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   DISULFID        70..107
FT                   /evidence="ECO:0000250|UniProtKB:A0A0B4JDK1"
FT   VAR_SEQ         126..134
FT                   /note="NSFSTKKNT -> MHLPTPYQN (in isoform 2)"
FT                   /id="VSP_060822"
FT   VAR_SEQ         135..152
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_060823"
SQ   SEQUENCE   152 AA;  16510 MW;  738D4D61BB5C4A9A CRC64;
     MNITRILGVV TTVVILYSVQ VTAQFFGDVQ QAMRCVAKLM PCQPYIHLSI PPPPLCCNPM
     KQIAEKDVSC LCTAFKHPDL LRFLALTKEN AIKILDSCGI NHDPSVCNKT NPSSPAALPE
     AATSGNSFST KKNTALAITF FGFSFVFLGM II
 
 
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