ID   ASCL_SOLLC              Reviewed;         303 AA.
AC   Q8W4Y5;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=ASC1-like protein;
DE   AltName: Full=Alternaria stem canker resistance-like protein;
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 [MRNA].
RC   TISSUE=Leaf;
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).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
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DR   EMBL; AJ416474; CAC95155.1; -; mRNA.
DR   RefSeq; NP_001233968.2; NM_001247039.2.
DR   AlphaFoldDB; Q8W4Y5; -.
DR   STRING; 4081.Solyc05g010280.2.1; -.
DR   PaxDb; Q8W4Y5; -.
DR   GeneID; 543781; -.
DR   KEGG; sly:543781; -.
DR   eggNOG; KOG1607; Eukaryota.
DR   OrthoDB; 987268at2759; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; Q8W4Y5; baseline and differential.
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..303
FT                   /note="ASC1-like protein"
FT                   /id="PRO_0000185522"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          72..284
FT                   /note="TLC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
SQ   SEQUENCE   303 AA;  36023 MW;  2799C9378E3F6947 CRC64;
     MGLLEGTFLD WEYESYPSYE DFAVLPLFAL FFPSVRFLLD RFVFEKVARR LIFGKGQEVV
     ENETDDRRRR IRKFKESAWK CIYFLSAEVF ALVVTYNEPW FTNTRYFWVG PGDQVWPDQM
     YKSKLKALYM YTGGFYTYSI FALIFWETRR SDFGVSMSHH VATAILIVLS YNIRFARVGS
     VVLAIHDASD IFLEIGKMSK YSGAEALASF RYLCLSWIIL RLIYYPFWVL WSTSYEVLQT
     LDKEKHKVDG PIYYYIFNSL LFCLLVLHIY WWVLIYRMLV KQIQARGQLS DDVRSDSEDE
     HED