ID   CCHL_MOUSE              Reviewed;         272 AA.
AC   P53702; Q6P5G5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Holocytochrome c-type synthase {ECO:0000250|UniProtKB:P53701};
DE            EC=4.4.1.17 {ECO:0000250|UniProtKB:P53701};
DE   AltName: Full=Cytochrome c-type heme lyase {ECO:0000250|UniProtKB:P53701};
DE            Short=CCHL {ECO:0000250|UniProtKB:P53701};
GN   Name=Hccs {ECO:0000312|MGI:MGI:106911}; Synonyms=Cchl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8661044; DOI=10.1006/geno.1996.0261;
RA   Schaefer L., Ballabio A., Zoghbi H.Y.;
RT   "Cloning and characterization of a putative human holocytochrome c-type
RT   synthetase gene (HCCS) isolated from the critical region for microphthalmia
RT   with linear skin defects (MLS).";
RL   Genomics 34:166-172(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Lyase that catalyzes the covalent linking of the heme group
CC       to the cytochrome C apoprotein to produce the mature functional
CC       cytochrome. {ECO:0000250|UniProtKB:P53701}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[cytochrome c] = apo-[cytochrome c] + heme b;
CC         Xref=Rhea:RHEA:22648, Rhea:RHEA-COMP:10725, Rhea:RHEA-COMP:10726,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:60344, ChEBI:CHEBI:83739; EC=4.4.1.17;
CC         Evidence={ECO:0000250|UniProtKB:P53701};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22650;
CC         Evidence={ECO:0000250|UniProtKB:P53701};
CC   -!- INTERACTION:
CC       P53702; P51906: Slc1a1; NbExp=5; IntAct=EBI-8579982, EBI-8580001;
CC       P53702; Q60989: Xiap; NbExp=5; IntAct=EBI-8579982, EBI-517478;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P53701}. Membrane
CC       {ECO:0000250|UniProtKB:P53701}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P53701}.
CC   -!- SIMILARITY: Belongs to the cytochrome c-type heme lyase family.
CC       {ECO:0000305}.
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DR   EMBL; U36788; AAB19008.1; -; mRNA.
DR   EMBL; AL805974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL831750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC061466; AAH61466.1; -; mRNA.
DR   EMBL; BC062905; AAH62905.1; -; mRNA.
DR   CCDS; CCDS30535.1; -.
DR   RefSeq; NP_001317978.1; NM_001331049.1.
DR   RefSeq; NP_001317979.1; NM_001331050.1.
DR   RefSeq; NP_032248.3; NM_008222.5.
DR   RefSeq; XP_006528768.1; XM_006528705.1.
DR   AlphaFoldDB; P53702; -.
DR   BioGRID; 200246; 3.
DR   IntAct; P53702; 4.
DR   MINT; P53702; -.
DR   STRING; 10090.ENSMUSP00000107743; -.
DR   GlyGen; P53702; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P53702; -.
DR   PhosphoSitePlus; P53702; -.
DR   SwissPalm; P53702; -.
DR   EPD; P53702; -.
DR   PaxDb; 10090-ENSMUSP00000033717; -.
DR   PeptideAtlas; P53702; -.
DR   ProteomicsDB; 281423; -.
DR   Pumba; P53702; -.
DR   Antibodypedia; 479; 346 antibodies from 32 providers.
DR   DNASU; 15159; -.
DR   Ensembl; ENSMUST00000033717.9; ENSMUSP00000033717.3; ENSMUSG00000031352.11.
DR   Ensembl; ENSMUST00000112115.2; ENSMUSP00000107743.2; ENSMUSG00000031352.11.
DR   GeneID; 15159; -.
DR   KEGG; mmu:15159; -.
DR   UCSC; uc009uxx.2; mouse.
DR   AGR; MGI:106911; -.
DR   CTD; 3052; -.
DR   MGI; MGI:106911; Hccs.
DR   VEuPathDB; HostDB:ENSMUSG00000031352; -.
DR   eggNOG; KOG3996; Eukaryota.
DR   GeneTree; ENSGT00390000004175; -.
DR   HOGENOM; CLU_048602_2_1_1; -.
DR   InParanoid; P53702; -.
DR   OMA; KARFWLF; -.
DR   OrthoDB; 36084at2759; -.
DR   PhylomeDB; P53702; -.
DR   TreeFam; TF105185; -.
DR   BRENDA; 4.4.1.17; 3474.
DR   BioGRID-ORCS; 15159; 24 hits in 80 CRISPR screens.
DR   PRO; PR:P53702; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; P53702; Protein.
DR   Bgee; ENSMUSG00000031352; Expressed in heart right ventricle and 255 other cell types or tissues.
DR   ExpressionAtlas; P53702; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0020037; F:heme binding; ISO:MGI.
DR   GO; GO:0004408; F:holocytochrome-c synthase activity; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000511; Holocyt_c/c1_synthase.
DR   PANTHER; PTHR12743; CYTOCHROME C1 HEME LYASE; 1.
DR   PANTHER; PTHR12743:SF0; HOLOCYTOCHROME C-TYPE SYNTHASE; 1.
DR   Pfam; PF01265; Cyto_heme_lyase; 1.
DR   PROSITE; PS00821; CYTO_HEME_LYASE_1; 1.
DR   PROSITE; PS00822; CYTO_HEME_LYASE_2; 1.
DR   Genevisible; P53702; MM.
PE   1: Evidence at protein level;
KW   Heme; Iron; Lipoprotein; Lyase; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Myristate; Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P53701"
FT   CHAIN           2..272
FT                   /note="Holocytochrome c-type synthase"
FT                   /id="PRO_0000121713"
FT   REPEAT          28..33
FT                   /note="HRM 1"
FT   REPEAT          38..43
FT                   /note="HRM 2"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P53701"
FT   CONFLICT        12
FT                   /note="V -> E (in Ref. 1; AAB19008)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   272 AA;  30978 MW;  AAAD63DBB3F81E47 CRC64;
     MGASASSPAT AVNASNASDG QPASPPSGCP MHKGQRKGCP VTAATSDLTS ESKAHTVPAH
     QDRAYDYVEC PVTGARAKDK ESLDPSNLMP PPNQTPSPDQ PFTLSTSREE SSIPRADSEK
     KWVYPSEQMF WNAMLRKGWK WKDDDISQKD MYNIIRIHNQ NNEQAWKEIL KWEALHAHEC
     PCGPSLVRFG GKAREYSPRA RIRSWMGYEL PFDRHDWIIN RCGTEVRYVI DYYDGGEVNK
     EYQFTILDVR PAFDSFSAVW DRMKVAWWRW TS
//