MIC19_BOVIN
ID MIC19_BOVIN Reviewed; 227 AA.
AC Q5E9D3; Q3T0L4;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=MICOS complex subunit MIC19;
DE AltName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 3;
GN Name=CHCHD3; Synonyms=MIC19;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the MICOS complex, a large protein complex of
CC the mitochondrial inner membrane that plays crucial roles in the
CC maintenance of crista junctions, inner membrane architecture, and
CC formation of contact sites to the outer membrane. Has also been shown
CC to function as a transcription factor which binds to the BAG1 promoter
CC and represses BAG1 transcription. Plays an important role in the
CC maintenance of the MICOS complex stability and the mitochondrial
CC cristae morphology. {ECO:0000250|UniProtKB:Q9NX63}.
CC -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC organizing system (MICOS) complex, composed of at least MICOS10/MIC10,
CC CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26
CC and MICOS13/MIC13. This complex was also known under the names MINOS or
CC MitOS complex. The MICOS complex associates with mitochondrial outer
CC membrane proteins SAMM50, MTX1 and MTX2 (together described as
CC components of the mitochondrial outer membrane sorting assembly
CC machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane
CC protein TMEM11 and with HSPA9. The MICOS and SAM complexes together
CC with DNAJC11 are part of a large protein complex spanning both
CC membranes termed the mitochondrial intermembrane space bridging (MIB)
CC complex. Interacts with HSPA1A/HSPA1B and OPA1, preferentially with the
CC soluble OPA1 form. Interacts with IMMT/MIC60.
CC {ECO:0000250|UniProtKB:Q9CRB9, ECO:0000250|UniProtKB:Q9NX63}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q9CRB9}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9CRB9}; Intermembrane side
CC {ECO:0000250|UniProtKB:Q9CRB9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9NX63}. Nucleus {ECO:0000250|UniProtKB:Q9NX63}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q9NX63}.
CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic19 family. Metazoan
CC Mic19 subfamily. {ECO:0000305}.
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DR EMBL; BT020987; AAX09004.1; -; mRNA.
DR EMBL; BC102347; AAI02348.1; -; mRNA.
DR RefSeq; NP_001030552.1; NM_001035475.1.
DR AlphaFoldDB; Q5E9D3; -.
DR SMR; Q5E9D3; -.
DR STRING; 9913.ENSBTAP00000034331; -.
DR PaxDb; Q5E9D3; -.
DR PeptideAtlas; Q5E9D3; -.
DR PRIDE; Q5E9D3; -.
DR Ensembl; ENSBTAT00000034438; ENSBTAP00000034331; ENSBTAG00000024723.
DR GeneID; 616477; -.
DR KEGG; bta:616477; -.
DR CTD; 54927; -.
DR VEuPathDB; HostDB:ENSBTAG00000024723; -.
DR VGNC; VGNC:27272; CHCHD3.
DR eggNOG; KOG4083; Eukaryota.
DR GeneTree; ENSGT00390000000903; -.
DR HOGENOM; CLU_049040_2_1_1; -.
DR InParanoid; Q5E9D3; -.
DR OMA; QCYQQNP; -.
DR OrthoDB; 1509756at2759; -.
DR TreeFam; TF326279; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000024723; Expressed in corpus luteum and 105 other tissues.
DR GO; GO:0061617; C:MICOS complex; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR GO; GO:0042407; P:cristae formation; IEA:Ensembl.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IBA:GO_Central.
DR GO; GO:0008053; P:mitochondrial fusion; IEA:Ensembl.
DR InterPro; IPR007964; MIC19/MIC25.
DR Pfam; PF05300; MIC19_MIC25; 1.
DR PROSITE; PS51808; CHCH; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Disulfide bond; Lipoprotein; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Myristate; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NX63"
FT CHAIN 2..227
FT /note="MICOS complex subunit MIC19"
FT /id="PRO_0000129162"
FT DOMAIN 180..222
FT /note="CHCH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT REGION 34..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 183..193
FT /note="Cx9C motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT MOTIF 204..214
FT /note="Cx9C motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT COMPBIAS 40..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX63"
FT MOD_RES 49
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX63"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX63"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CRB9"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX63"
FT MOD_RES 142
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX63"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:Q9CRB9"
FT DISULFID 183..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT DISULFID 193..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ SEQUENCE 227 AA; 26100 MW; 192164E1B3C88E6C CRC64;
MGGTASTRRV TFEADENENI TVVKGIRLSE NVIDRMKETS PSGPKSQRYS GTYGASVSDE
ELKRRVAEEL ALEQAKKESE NQKRLKQSKE LDAEKAFANE QLTRAILRER ISNEEERAKA
KHLAKQLEEK DRVIKKQDAF YKEQLARLEE RSSEFYKVTT EQYQKAAEEV EAKFKRYEYH
PVCADLQAQI LQCYRQNTQQ TLSCSALASQ YMRCVNQAKQ STLEKGG
