CYC2_YEAST
ID CYC2_YEAST Reviewed; 366 AA.
AC P38909; D6W2A4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cytochrome c mitochondrial import factor CYC2;
DE EC=1.-.-.-;
DE AltName: Full=Cytochrome c assembly flavoprotein CYC2;
DE Flags: Precursor;
GN Name=CYC2; OrderedLocusNames=YOR037W; ORFNames=OR26.30;
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] OF 128-366, AND SUBCELLULAR LOCATION.
RX PubMed=8413243; DOI=10.1128/mcb.13.10.6442-6451.1993;
RA Dumont M.E., Schlichter J.B., Cardillo T.S., Hayes M.K., Bethlendy G.,
RA Sherman F.;
RT "CYC2 encodes a factor involved in mitochondrial import of yeast cytochrome
RT c.";
RL Mol. Cell. Biol. 13:6442-6451(1993).
RN [4]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, FAD-BINDING, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=16207709; DOI=10.1074/jbc.m508574200;
RA Bernard D.G., Quevillon-Cheruel S., Merchant S., Guiard B., Hamel P.P.;
RT "Cyc2p, a membrane-bound flavoprotein involved in the maturation of
RT mitochondrial c-type cytochromes.";
RL J. Biol. Chem. 280:39852-39859(2005).
CC -!- FUNCTION: Redox component that participates in c-type cytochrome
CC biogenesis in the mitochondrial intermembrane space. May play a role in
CC the reduction of heme prior to its ligation to apocytochrome c by
CC cytochrome c heme lyase. Has oxidoreductase activity in vitro.
CC {ECO:0000269|PubMed:16207709}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:16207709};
CC Note=Binds 1 FAD per monomer. {ECO:0000269|PubMed:16207709};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for NADPH {ECO:0000269|PubMed:16207709};
CC KM=30 mM for NADH {ECO:0000269|PubMed:16207709};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:16207709, ECO:0000269|PubMed:8413243}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16207709,
CC ECO:0000269|PubMed:8413243}; Intermembrane side
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:16207709, ECO:0000269|PubMed:8413243}.
CC -!- MISCELLANEOUS: Present with 2730 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA72429.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA60756.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA99227.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X87331; CAA60756.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74945; CAA99227.1; ALT_INIT; Genomic_DNA.
DR EMBL; L28428; AAA72429.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006948; DAA10820.1; -; Genomic_DNA.
DR PIR; S62176; S62176.
DR RefSeq; NP_014680.2; NM_001183456.1.
DR AlphaFoldDB; P38909; -.
DR SMR; P38909; -.
DR BioGRID; 34439; 178.
DR DIP; DIP-3836N; -.
DR STRING; 4932.YOR037W; -.
DR MaxQB; P38909; -.
DR PaxDb; P38909; -.
DR PRIDE; P38909; -.
DR EnsemblFungi; YOR037W_mRNA; YOR037W; YOR037W.
DR GeneID; 854202; -.
DR KEGG; sce:YOR037W; -.
DR SGD; S000005563; CYC2.
DR VEuPathDB; FungiDB:YOR037W; -.
DR eggNOG; KOG0534; Eukaryota.
DR HOGENOM; CLU_003827_6_2_1; -.
DR InParanoid; P38909; -.
DR OMA; VKQPEIM; -.
DR BioCyc; YEAST:G3O-33583-MON; -.
DR SABIO-RK; P38909; -.
DR PRO; PR:P38909; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P38909; protein.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:SGD.
DR GO; GO:0018063; P:cytochrome c-heme linkage; IGI:SGD.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IBA:GO_Central.
DR GO; GO:0007006; P:mitochondrial membrane organization; IMP:SGD.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; PTHR19370; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW NADP; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 51..366
FT /note="Cytochrome c mitochondrial import factor CYC2"
FT /id="PRO_0000079749"
FT DOMAIN 63..184
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
SQ SEQUENCE 366 AA; 42368 MW; AE7ADA43C51824D7 CRC64;
MLWKNYVLSS SRITRRLHKS PRKSSFSKNF FITGCLLTVG AVSSYLTYRY TSERENKHEL
SPSYFVKYKI SHKRDIDSSH FLLEVTPLFK QKVNIWSLMT AENLWSVEIK QPEVMVVRNY
TPLPLKFNPA SKEIEILKDG DNADGKLSFY IKKYENGEVA RWLHHLPKGH IIEIRGPFID
YEFPHLPNEL KRSRDCLYMD NRNERGNNVR ENSQFIYQPY DIMMFTAGTG IVTALQLLLT
ESPFRGTIKL FHTDKNIKQL GPLYPILLRL QASNRVQLKI FETDRQTKQD VLKSIQKSIT
KPYPYKGLLP FSNVNNKNIM PVLALVCGPE SYISSISGRK YDLNQGPVGG LLSKEGWNSD
NVYKLS
