CCHL_MOUSE
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 03-AUG-2022, entry version 134.
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, Spleen, and
RC 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.ENSMUSP00000033717; -.
DR iPTMnet; P53702; -.
DR PhosphoSitePlus; P53702; -.
DR SwissPalm; P53702; -.
DR EPD; P53702; -.
DR PaxDb; P53702; -.
DR PeptideAtlas; P53702; -.
DR PRIDE; P53702; -.
DR ProteomicsDB; 281423; -.
DR Antibodypedia; 479; 316 antibodies from 32 providers.
DR DNASU; 15159; -.
DR Ensembl; ENSMUST00000033717; ENSMUSP00000033717; ENSMUSG00000031352.
DR Ensembl; ENSMUST00000112115; ENSMUSP00000107743; ENSMUSG00000031352.
DR GeneID; 15159; -.
DR KEGG; mmu:15159; -.
DR UCSC; uc009uxx.2; mouse.
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; EGAWDEI; -.
DR OrthoDB; 1282808at2759; -.
DR PhylomeDB; P53702; -.
DR TreeFam; TF105185; -.
DR BRENDA; 4.4.1.17; 3474.
DR BioGRID-ORCS; 15159; 24 hits in 75 CRISPR screens.
DR PRO; PR:P53702; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P53702; protein.
DR Bgee; ENSMUSG00000031352; Expressed in heart right ventricle and 251 other tissues.
DR ExpressionAtlas; P53702; baseline and differential.
DR Genevisible; P53702; MM.
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 GO; GO:0018063; P:cytochrome c-heme linkage; ISO:MGI.
DR InterPro; IPR000511; Holocyt_c/c1_synthase.
DR PANTHER; PTHR12743; PTHR12743; 1.
DR Pfam; PF01265; Cyto_heme_lyase; 1.
DR PROSITE; PS00821; CYTO_HEME_LYASE_1; 1.
DR PROSITE; PS00822; CYTO_HEME_LYASE_2; 1.
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
