ID   ASCL1_ORYSJ             Reviewed;         309 AA.
AC   Q6EUN0; Q0E030;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=ASC1-like protein 1;
DE   AltName: Full=Alternaria stem canker resistance-like protein 1;
GN   OrderedLocusNames=Os02g0581300, LOC_Os02g37080; ORFNames=OJ1115_A05.19;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
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; AP003999; BAD27639.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF09158.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS79426.1; -; Genomic_DNA.
DR   EMBL; AK071553; BAG92552.1; -; mRNA.
DR   RefSeq; XP_015627118.1; XM_015771632.1.
DR   AlphaFoldDB; Q6EUN0; -.
DR   STRING; 4530.OS02T0581300-01; -.
DR   PaxDb; Q6EUN0; -.
DR   PRIDE; Q6EUN0; -.
DR   EnsemblPlants; Os02t0581300-01; Os02t0581300-01; Os02g0581300.
DR   GeneID; 4329785; -.
DR   Gramene; Os02t0581300-01; Os02t0581300-01; Os02g0581300.
DR   KEGG; osa:4329785; -.
DR   eggNOG; KOG1607; Eukaryota.
DR   HOGENOM; CLU_028277_5_0_1; -.
DR   InParanoid; Q6EUN0; -.
DR   OMA; IAIEWIF; -.
DR   OrthoDB; 987268at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6EUN0; OS.
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..309
FT                   /note="ASC1-like protein 1"
FT                   /id="PRO_0000185523"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          75..289
FT                   /note="TLC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
SQ   SEQUENCE   309 AA;  36421 MW;  F2C81A6513727A70 CRC64;
     MGVAAAAGRL LAAVDWEREA YPAYRDFFAL PLFAVFFLVV RYLLDCFVFE WIGRKLIFGK
     EKVDYEKEET RKKIRKFKES AWKCVYFLSG EILSLSVTYN EPWFTNTKYF WVGPGDQVWP
     DQKIKWKLKA VYMYAAGFYT YSIFALMFWE TRRSDFGVSM SHHVATVALI VLSYVFRFAR
     VGSVVLAIHD ASDVFLEVGK MAKYSHCDLL ANVAFLLFVV SWVLLRLTYF PFWILRSTSY
     EVLLTLDKKK HNFDGPIYYY VFNSLLFSLL VLHIYWWVLI YRMLVRQIKT RNVGDDVRSD
     SEGEDEHED