DCI1_YEAST
ID DCI1_YEAST Reviewed; 271 AA.
AC Q08558; D6W2N6;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase;
DE EC=5.3.3.-;
GN Name=DCI1; Synonyms=ECI2, EHD2; OrderedLocusNames=YOR180C;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP INDUCTION.
RX PubMed=9774671; DOI=10.1128/mcb.18.11.6560;
RA Karpichev I.V., Small G.M.;
RT "Global regulatory functions of Oaf1p and Pip2p (Oaf2p), transcription
RT factors that regulate genes encoding peroxisomal proteins in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 18:6560-6570(1998).
RN [5]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH ECI1.
RX PubMed=10381339; DOI=10.1006/bbrc.1999.0860;
RA Geisbrecht B.V., Schulz K., Nau K., Geraghty M.T., Schulz H., Erdmann R.,
RA Gould S.J.;
RT "Preliminary characterization of Yor180Cp: identification of a novel
RT peroxisomal protein of Saccharomyces cerevisiae involved in fatty acid
RT metabolism.";
RL Biochem. Biophys. Res. Commun. 260:28-34(1999).
RN [6]
RP INDUCTION, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10455114; DOI=10.1074/jbc.274.35.24514;
RA Gurvitz A., Mursula A.M., Yagi A.I., Hartig A., Ruis H., Rottensteiner H.,
RA Hiltunen J.K.;
RT "Alternatives to the isomerase-dependent pathway for the beta-oxidation of
RT oleic acid are dispensable in Saccharomyces cerevisiae. Identification of
RT YOR180c/DCI1 encoding peroxisomal delta(3,5)-delta(2,4)-dienoyl-CoA
RT isomerase.";
RL J. Biol. Chem. 274:24514-24521(1999).
RN [7]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10639339; DOI=10.1242/jcs.113.3.533;
RA Karpichev I.V., Small G.M.;
RT "Evidence for a novel pathway for the targeting of a Saccharomyces
RT cerevisiae peroxisomal protein belonging to the isomerase/hydratase
RT family.";
RL J. Cell Sci. 113:533-544(2000).
RN [8]
RP FUNCTION.
RX PubMed=11302517; DOI=10.1078/0171-9335-00144;
RA Yang X., Purdue P.E., Lazarow P.B.;
RT "Eci1p uses a PTS1 to enter peroxisomes: either its own or that of a
RT partner, Dci1p.";
RL Eur. J. Cell Biol. 80:126-138(2001).
RN [9]
RP INDUCTION.
RX PubMed=12429834; DOI=10.1091/mbc.e01-12-0149;
RA Palkova Z., Devaux F., Icicova M., Minarikova L., Le Crom S., Jacq C.;
RT "Ammonia pulses and metabolic oscillations guide yeast colony
RT development.";
RL Mol. Biol. Cell 13:3901-3914(2002).
CC -!- FUNCTION: Converts 3,5-dienoyl-CoAs to the corresponding 2,4-dienoyl-
CC CoAs. Involved in fatty acid metabolism. Required for ECI1 to be
CC peroxisomal located. {ECO:0000269|PubMed:10381339,
CC ECO:0000269|PubMed:10455114, ECO:0000269|PubMed:11302517}.
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC -!- SUBUNIT: Interacts with ECI1. {ECO:0000269|PubMed:10381339}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10381339,
CC ECO:0000269|PubMed:10455114, ECO:0000269|PubMed:10639339}.
CC -!- INDUCTION: By oleate, through the binding of the OAF1-PIP2
CC transcriptional activator complex to its promoter ORE element.
CC Expression is also induced during ammonia pulses in yeast colonies, at
CC the beginning of detectable ammonia production.
CC {ECO:0000269|PubMed:10455114, ECO:0000269|PubMed:10639339,
CC ECO:0000269|PubMed:12429834, ECO:0000269|PubMed:9774671}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; Z75088; CAA99389.1; -; Genomic_DNA.
DR EMBL; AY558432; AAS56758.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10952.1; -; Genomic_DNA.
DR PIR; S67072; S67072.
DR RefSeq; NP_014823.3; NM_001183599.3.
DR AlphaFoldDB; Q08558; -.
DR SMR; Q08558; -.
DR BioGRID; 34575; 69.
DR DIP; DIP-4132N; -.
DR IntAct; Q08558; 2.
DR MINT; Q08558; -.
DR STRING; 4932.YOR180C; -.
DR PaxDb; Q08558; -.
DR EnsemblFungi; YOR180C_mRNA; YOR180C; YOR180C.
DR GeneID; 854352; -.
DR KEGG; sce:YOR180C; -.
DR SGD; S000005706; DCI1.
DR VEuPathDB; FungiDB:YOR180C; -.
DR eggNOG; KOG0016; Eukaryota.
DR GeneTree; ENSGT00940000173631; -.
DR HOGENOM; CLU_009834_6_2_1; -.
DR InParanoid; Q08558; -.
DR OMA; MARCRIP; -.
DR BioCyc; MetaCyc:YOR180C-MON; -.
DR BioCyc; YEAST:YOR180C-MON; -.
DR UniPathway; UPA00659; -.
DR PRO; PR:Q08558; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08558; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:SGD.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IDA:SGD.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:SGD.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
PE 1: Evidence at protein level;
KW Fatty acid metabolism; Isomerase; Lipid metabolism; Peroxisome;
KW Reference proteome.
FT CHAIN 1..271
FT /note="Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase"
FT /id="PRO_0000232996"
FT MOTIF 269..271
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 152
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q05871"
FT BINDING 62..66
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q05871"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q05871"
SQ SEQUENCE 271 AA; 30058 MW; 0AA0BF3A981F733F CRC64;
MSSRVCYHIN GPFFIIKLID PKHLNSLTFE DFVYIALLLH KANDIDSVLF TVLQSSGKYF
SSGGKFSAVN KLNDGDVTSE VEKVSKLVSA ISSPNIFVAN AFAIHKKVLV CCLNGPAIGL
SASLVALCDI VYSQNDSVFL LFPFSNLGFV AEVGTSVTLT QKLGINSANE HMIFSTPVLF
KELIGTIITK NYQLTNTETF NEKVLQDIKQ NLEGLYPKSV LGMKELLHSE MKQKLIKAQA
METNGTLPFW ASGEPFKRFK QLQEGNRRHK L
