ID   CHCH3_CAEEL             Reviewed;         169 AA.
AC   Q21551;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=MICOS complex subunit MIC19 {ECO:0000250|UniProtKB:Q9NX63};
DE   AltName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 3 {ECO:0000250|UniProtKB:Q9NX63};
GN   Name=chch-3 {ECO:0000303|PubMed:21248201, ECO:0000312|WormBase:M176.3};
GN   ORFNames=M176.3 {ECO:0000312|WormBase:M176.3};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21248201; DOI=10.1091/mbc.e10-07-0600;
RA   Head B.P., Zulaika M., Ryazantsev S., van der Bliek A.M.;
RT   "A novel mitochondrial outer membrane protein, MOMA-1, that affects cristae
RT   morphology in Caenorhabditis elegans.";
RL   Mol. Biol. Cell 22:831-841(2011).
CC   -!- FUNCTION: Plays a role in maintaining mitochondrial morphology
CC       (PubMed:21248201). May act as a component of the MICOS complex, a large
CC       protein complex of the mitochondria (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NX63, ECO:0000269|PubMed:21248201}.
CC   -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC       organizing system (MICOS) complex. {ECO:0000250|UniProtKB:Q9NX63}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q9NX63}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q9NX63}; Intermembrane side
CC       {ECO:0000250|UniProtKB:Q9NX63}.
CC   -!- DISRUPTION PHENOTYPE: Abnormal mitochondrial morphology with localized
CC       swellings and tubular extensions. Double knockout with moma-1 or immt-1
CC       results in reduced or no brood, poor growth and withered gonads.
CC       Furthermore, in double knockouts with moma-1, the gonads contain fewer
CC       mitochondria. {ECO:0000269|PubMed:21248201}.
CC   -!- SIMILARITY: Belongs to the MICOS complex subunit Mic19 family. Metazoan
CC       Mic19 subfamily. {ECO:0000305}.
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DR   EMBL; BX284602; CAB01650.1; -; Genomic_DNA.
DR   PIR; T23786; T23786.
DR   RefSeq; NP_496012.1; NM_063611.6.
DR   AlphaFoldDB; Q21551; -.
DR   SMR; Q21551; -.
DR   STRING; 6239.M176.3; -.
DR   World-2DPAGE; 0011:Q21551; -.
DR   EPD; Q21551; -.
DR   PaxDb; Q21551; -.
DR   EnsemblMetazoa; M176.3.1; M176.3.1; WBGene00010942.
DR   GeneID; 174494; -.
DR   KEGG; cel:CELE_M176.3; -.
DR   UCSC; M176.3.1; c. elegans.
DR   CTD; 174494; -.
DR   WormBase; M176.3; CE12464; WBGene00010942; chch-3.
DR   eggNOG; KOG4083; Eukaryota.
DR   GeneTree; ENSGT00390000000903; -.
DR   HOGENOM; CLU_1549035_0_0_1; -.
DR   InParanoid; Q21551; -.
DR   OMA; HRENVCQ; -.
DR   OrthoDB; 1412627at2759; -.
DR   PRO; PR:Q21551; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00010942; Expressed in embryo and 4 other tissues.
DR   GO; GO:0061617; C:MICOS complex; IBA:GO_Central.
DR   GO; GO:0007007; P:inner mitochondrial membrane organization; IBA:GO_Central.
DR   PROSITE; PS51808; CHCH; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Lipoprotein; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Myristate; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..169
FT                   /note="MICOS complex subunit MIC19"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000438528"
FT   DOMAIN          123..165
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           126..136
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           147..157
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        126..157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        136..147
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   169 AA;  19193 MW;  9D9E084ADCAA56AC CRC64;
     MGASQSAEQE ARPEVVRIDR NEIPEEYKTV GVSSDVVSRV NATRVAGNDG ESDRLRQELA
     REREEKARLR EDMAKLSQLQ QRKTAGISAA PVSISGNDLE ERKKIFDDTV ERVQKQFFAY
     HRENVCQDNE NEIVRCLQEN PGRVLKCAPL TEAFEKCVGE FRQQVLKGN