ICT1_YEAST
ID ICT1_YEAST Reviewed; 394 AA.
AC Q12385; D6VY99; Q7LGX2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=1-acylglycerol-3-phosphate O-acyltransferase ICT1;
DE EC=2.3.1.51;
DE AltName: Full=Increased copper tolerance protein 1;
DE AltName: Full=Lysophosphatidic acid acyltransferase ICT1;
DE Short=LPAAT;
GN Name=ICT1; OrderedLocusNames=YLR099C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=9717239;
RX DOI=10.1002/(sici)1097-0061(199807)14:10<935::aid-yea289>3.0.co;2-9;
RA Launhardt H., Hinnen A., Munder T.;
RT "Drug-induced phenotypes provide a tool for the functional analysis of
RT yeast genes.";
RL Yeast 14:935-942(1998).
RN [4]
RP FUNCTION.
RX PubMed=10628851; DOI=10.1007/pl00013817;
RA Entian K.-D., Schuster T., Hegemann J.H., Becher D., Feldmann H.,
RA Gueldener U., Goetz R., Hansen M., Hollenberg C.P., Jansen G., Kramer W.,
RA Klein S., Koetter P., Kricke J., Launhardt H., Mannhaupt G., Maierl A.,
RA Meyer P., Mewes W., Munder T., Niedenthal R.K., Ramezani Rad M.,
RA Roehmer A., Roemer A., Rose M., Schaefer B., Siegler M.-L., Vetter J.,
RA Wilhelm N., Wolf K., Zimmermann F.K., Zollner A., Hinnen A.;
RT "Functional analysis of 150 deletion mutants in Saccharomyces cerevisiae by
RT a systematic approach.";
RL Mol. Gen. Genet. 262:683-702(1999).
RN [5]
RP FUNCTION.
RX PubMed=11055939; DOI=10.1128/aem.66.11.4883-4889.2000;
RA Miura S., Zou W., Ueda M., Tanaka A.;
RT "Screening of genes involved in isooctane tolerance in Saccharomyces
RT cerevisiae by using mRNA differential display.";
RL Appl. Environ. Microbiol. 66:4883-4889(2000).
RN [6]
RP FUNCTION, AND DOMAIN.
RX PubMed=18252723; DOI=10.1074/jbc.m708418200;
RA Ghosh A.K., Ramakrishnan G., Rajasekharan R.;
RT "YLR099C (ICT1) encodes a soluble Acyl-CoA-dependent lysophosphatidic acid
RT acyltransferase responsible for enhanced phospholipid synthesis on organic
RT solvent stress in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 283:9768-9775(2008).
CC -!- FUNCTION: Lysophosphatidic acid acyltransferase involved in membrane
CC remodeling leading to increased organic solvent tolerance. Involved in
CC resistance to azoles and copper. {ECO:0000269|PubMed:10628851,
CC ECO:0000269|PubMed:11055939, ECO:0000269|PubMed:18252723,
CC ECO:0000269|PubMed:9717239}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- MISCELLANEOUS: The isooctane tolerance of organic-solvent tolerant
CC strain KK-21 may result from the alteration of the expression of
CC several genes including ICT1, due to the loss of their proper
CC regulation.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z73271; CAA97663.1; -; Genomic_DNA.
DR EMBL; Z73272; CAA97666.1; -; Genomic_DNA.
DR EMBL; U53876; AAB67543.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09415.1; -; Genomic_DNA.
DR PIR; S64933; S64933.
DR RefSeq; NP_013200.1; NM_001181986.1.
DR AlphaFoldDB; Q12385; -.
DR SMR; Q12385; -.
DR BioGRID; 31372; 84.
DR DIP; DIP-5245N; -.
DR IntAct; Q12385; 2.
DR STRING; 4932.YLR099C; -.
DR ESTHER; yeast-ict1; CGI-58_ABHD5_ABHD4.
DR MEROPS; S33.A43; -.
DR PaxDb; Q12385; -.
DR PRIDE; Q12385; -.
DR EnsemblFungi; YLR099C_mRNA; YLR099C; YLR099C.
DR GeneID; 850788; -.
DR KEGG; sce:YLR099C; -.
DR SGD; S000004089; ICT1.
DR VEuPathDB; FungiDB:YLR099C; -.
DR eggNOG; KOG4409; Eukaryota.
DR GeneTree; ENSGT00940000170137; -.
DR HOGENOM; CLU_017361_1_1_1; -.
DR InParanoid; Q12385; -.
DR OMA; ARDPIMD; -.
DR BioCyc; YEAST:G3O-32249-MON; -.
DR Reactome; R-SCE-1482839; Acyl chain remodelling of PE.
DR PRO; PR:Q12385; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12385; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IDA:SGD.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IMP:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipid biosynthesis; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Stress response; Transferase.
FT CHAIN 1..394
FT /note="1-acylglycerol-3-phosphate O-acyltransferase ICT1"
FT /id="PRO_0000080854"
FT DOMAIN 74..381
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT MOTIF 374..379
FT /note="HXXXXD motif"
SQ SEQUENCE 394 AA; 45141 MW; 7B686E611E81C380 CRC64;
MWTNTFKWCS KTEKETTTAD AKVCASVQGL KALQQQIMDS TTVRGSVNNT MTPGGINQWH
FHNKRANKVC TPTVLIHGYA ASSMAFYRTF ENLSDNIKDL YAIDLPANGA SEAPALQVNK
TKKIKSLRFK HIEDDVVIPV IEKRPPAEDI KSHLEQYESY FVDRIEQWRK DNKLRKINVV
GHSFGGYISF KYALKYPDSI EKLCLISPLG VENSIHAITH KWEPNTTYPL TFTDPSSRYY
TRKLNVPRFI FENQLNVLKW MGPIGSKLCS NYISTAYVKV PDQIYKDYLL HSFVGKNQTV
QPQTIKVFTH LFERNLIARD PIINNVRFLN PATPVMFMYG EHDWMDKYAG YLTTESMLKN
KAKASYVEVP DAGHNLFLDN PQHFASSLVS FLSK
