ASC1_SOLLC
ID ASC1_SOLLC Reviewed; 308 AA.
AC Q9M6A3; A0A3Q7GG99; Q9M6A4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 3.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Alternaria stem canker resistance protein 1 {ECO:0000303|PubMed:10781105};
DE Short=Protein ASC1 {ECO:0000303|PubMed:10781105};
GN Name=Asc-1 {ECO:0000303|PubMed:10781105};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASC-1, AND FUNCTION.
RC STRAIN=cv. VFNT Cherry;
RX PubMed=10781105; DOI=10.1073/pnas.97.9.4961;
RA Brandwagt B.F., Mesbah L.A., Takken F.L.W., Laurent P.L., Kneppers T.J.A.,
RA Hille J., Nijkamp H.J.J.;
RT "A longevity assurance gene homolog of tomato mediates resistance to
RT Alternaria alternata f. sp. lycopersici toxins and fumonisin B1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4961-4966(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=12445127; DOI=10.1046/j.1365-313x.2002.01444.x;
RA Spassieva S.D., Markham J.E., Hille J.;
RT "The plant disease resistance gene Asc-1 prevents disruption of
RT sphingolipid metabolism during AAL-toxin-induced programmed cell death.";
RL Plant J. 32:561-572(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
CC -!- FUNCTION: Mediates resistance to sphinganine-analog mycotoxins (SAMs)
CC by restoring the sphingolipid biosynthesis. Could salvage the transport
CC of GPI-anchored proteins from the endoplasmic reticulum to the Golgi
CC apparatus in ceramides-depleted cells after SAM exposure.
CC {ECO:0000269|PubMed:10781105, ECO:0000269|PubMed:12445127}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8C172}; Multi-pass membrane protein
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF198177; AAF67518.1; -; Genomic_DNA.
DR EMBL; AF198178; AAF67519.1; -; Genomic_DNA.
DR EMBL; AJ312131; CAC85301.1; -; mRNA.
DR RefSeq; NP_001234320.1; NM_001247391.2.
DR AlphaFoldDB; Q9M6A3; -.
DR STRING; 4081.Solyc03g114600.2.1; -.
DR PaxDb; Q9M6A3; -.
DR EnsemblPlants; Solyc03g114600.3.1; Solyc03g114600.3.1; Solyc03g114600.3.
DR GeneID; 778364; -.
DR Gramene; Solyc03g114600.3.1; Solyc03g114600.3.1; Solyc03g114600.3.
DR KEGG; sly:778364; -.
DR eggNOG; KOG1607; Eukaryota.
DR InParanoid; Q9M6A3; -.
DR OMA; ATLYWET; -.
DR OrthoDB; 987268at2759; -.
DR BioCyc; MetaCyc:MON-15535; -.
DR Proteomes; UP000004994; Chromosome 3.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0050291; F:sphingosine N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; IBA:GO_Central.
DR InterPro; IPR016439; Lag1/Lac1-like.
DR InterPro; IPR006634; TLC-dom.
DR PANTHER; PTHR12560; PTHR12560; 1.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR PIRSF; PIRSF005225; LAG1_LAC1; 1.
DR SMART; SM00724; TLC; 1.
DR PROSITE; PS50922; TLC; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..308
FT /note="Alternaria stem canker resistance protein 1"
FT /id="PRO_0000185521"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 73..287
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT VARIANT 69..87
FT /note="RKKINKFKESAWKFVYFLS -> EEDQQIQRVSMEICIFSIC (in
FT allele asc-1)"
FT VARIANT 88..306
FT /note="Missing (in allele asc-1)"
FT CONFLICT 88
FT /note="T -> A (in Ref. 1; AAF67518/AAF67519 and 2;
FT CAC85301)"
SQ SEQUENCE 308 AA; 36332 MW; 1C194B2B2A17F7A2 CRC64;
MKNLDHIAAS VDWEKESLPE YQDLIFLLFF ALFFPVLRFI LDRFVFEALA KRMIFGKKTV
VNINGREERK KINKFKESAW KFVYFLSTEL LALSVTCNEP WFTDSRYFWA GPGDVVWPNL
KMKLKLKLLY MYAGGFYFYS IFATLYWETR RYDFAAQIIH HVTTVSLIVL SYVYGFARIG
SVVLALHDGS DVFMEIAKMS KYSGFDLIAD IFFSLFALVF TSLRIICYPF WIIRSTCYEL
LYVLDIQKER TTGIILYFVF NALLICLLVL HLFWFKIILR MVKNQILSRG HITDDVREDS
ESDDDHKD
