IMMT1_CAEEL
ID IMMT1_CAEEL Reviewed; 679 AA.
AC Q22505;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=MICOS complex subunit MIC60-1 {ECO:0000305};
DE AltName: Full=Inner mitochondrial membrane protein 1 {ECO:0000303|PubMed:20578245};
DE AltName: Full=Mitofilin homolog 1 {ECO:0000305|PubMed:20578245};
DE Flags: Precursor;
GN Name=immt-1 {ECO:0000312|WormBase:T14G11.3};
GN ORFNames=T14G11.3 {ECO:0000312|WormBase:T14G11.3};
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=20578245; DOI=10.1002/jcp.22177;
RA Mun J.Y., Lee T.H., Kim J.H., Yoo B.H., Bahk Y.Y., Koo H.S., Han S.S.;
RT "Caenorhabditis elegans mitofilin homologs control the morphology of
RT mitochondrial cristae and influence reproduction and physiology.";
RL J. Cell. Physiol. 224:748-756(2010).
RN [3] {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: Sustains mitochondrial morphology probably through
CC maintaining cristae morphology (PubMed:20578245, PubMed:21248201). May
CC act as a component of the MICOS complex, a large protein complex of the
CC mitochondria (By similarity). {ECO:0000250|UniProtKB:Q16891,
CC ECO:0000269|PubMed:20578245, ECO:0000269|PubMed:21248201}.
CC -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC organizing system (MICOS) complex. {ECO:0000250|UniProtKB:Q16891}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:20578245}; Single-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:20578245}. Note=Localized
CC to cytoplasmic foci in embryos and gonads. Evenly distributed between
CC the periphery and the cristae regions of the mitochondrion inner
CC membrane. {ECO:0000269|PubMed:20578245}.
CC -!- TISSUE SPECIFICITY: Expressed in the gonads and muscle cells.
CC {ECO:0000269|PubMed:20578245}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos.
CC {ECO:0000269|PubMed:20578245}.
CC -!- DISRUPTION PHENOTYPE: Egg-laying defects, defective oogenesis in 30% of
CC mutants, reduced brood size and increased resistance to oxidative
CC stress inducer paraquat (PubMed:20578245). Abnormal mitochondrial
CC morphology with mitochondria appearing larger and as localized
CC swellings and tubular extensions (PubMed:20578245, PubMed:21248201).
CC Mitochondria also have elongated and curved cristae that are stacked
CC with a reduced number of junctions (PubMed:20578245, PubMed:21248201).
CC Double knockout with immt-2 results in a more reduced brood size and
CC enhanced resistance to paraquat-induced oxidative stress as compared to
CC the single mutant, and in addition, mutants are slower swimmers, have
CC increased hydrogen peroxide-induced reactive oxygen species (ROS), and
CC reduced mitochondrial mass accompanied by reduced superoxide anion
CC oxidation (PubMed:20578245). Double knockout with chch-3 RNAi results
CC in reduced or no brood, poor growth and withered gonads
CC (PubMed:21248201). {ECO:0000269|PubMed:20578245,
CC ECO:0000269|PubMed:21248201}.
CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic60 family.
CC {ECO:0000255, ECO:0000255|RuleBase:RU363000}.
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DR EMBL; BX284606; CCD63791.1; -; Genomic_DNA.
DR PIR; T29795; T29795.
DR RefSeq; NP_508475.2; NM_076074.5.
DR AlphaFoldDB; Q22505; -.
DR SMR; Q22505; -.
DR IntAct; Q22505; 1.
DR STRING; 6239.T14G11.3; -.
DR EPD; Q22505; -.
DR PaxDb; Q22505; -.
DR PeptideAtlas; Q22505; -.
DR EnsemblMetazoa; T14G11.3.1; T14G11.3.1; WBGene00020511.
DR GeneID; 180566; -.
DR KEGG; cel:CELE_T14G11.3; -.
DR UCSC; T14G11.3; c. elegans.
DR CTD; 180566; -.
DR WormBase; T14G11.3; CE33696; WBGene00020511; immt-1.
DR eggNOG; KOG1854; Eukaryota.
DR GeneTree; ENSGT00390000002313; -.
DR HOGENOM; CLU_021851_2_0_1; -.
DR InParanoid; Q22505; -.
DR OMA; STYEAFS; -.
DR OrthoDB; 1073064at2759; -.
DR PhylomeDB; Q22505; -.
DR PRO; PR:Q22505; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00020511; Expressed in larva and 4 other tissues.
DR GO; GO:0061617; C:MICOS complex; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:WormBase.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:WormBase.
DR GO; GO:0042407; P:cristae formation; IMP:WormBase.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:WormBase.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:WormBase.
DR InterPro; IPR019133; Mt-IM_prot_Mitofilin.
DR PANTHER; PTHR15415; PTHR15415; 1.
DR Pfam; PF09731; Mitofilin; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..679
FT /note="MICOS complex subunit MIC60-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438529"
FT TOPO_DOM 18..42
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..679
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 679 AA; 75997 MW; 197F7EC397627E73 CRC64;
MFRIASKRSV SQTLKRARQQ SNQAAAPPKP PVQPPKKSGG GKGLALVGAT VVGAGGVVGY
AYVDPEFRHK VESTVPPVKQ VFDAVLGESS LQKTKQQIGD LKDAVVNAVP KKKEVLPPLE
LAPLPPVLPR EPTHVDPVDV RKDVTPMIPK PSPDVVFAKN QQLEEKLKIA IHSAEGKVRL
ATEAKLKTIN AINEHASILK QTVDDAKHAN WENVTSALQR AEAEARVDSG QEVDGRNYID
NLRKIVNDGK RDSTTATNPL LLNAQETANK LSHQLDEINA LVNKSRQESA VLNQYKDLIE
KSRQQFALEM KSILPNVDIH AKDKNLNEDE LNALIAHAHL KVDQLRCQLS DQQVREELHI
SKALEEQRLA DERIASEKLS IEMSRVGRQN ELEIERALVE SRSSWEGELE NQLKRTASAH
SEHLEQVIRT QRQLFEIEQN QKVEEAVLQE RNLHSKQVGA ALSRLEGIEE ALGSRVALDN
ENRRAKQFWI ACHNLIDTLK HGNKAGNNID ERRLPLNESL NLLKEVNPED EFVNAIIDSF
PKQATTVGTY TEQDLKNRFE QLYKIGRKTA SIDENGGTLG AYFWSYVKSL FLVDMPQQYG
NLDAIDVNNT DNYEILSRAK QYVHNGDLDK AIRVVQLLKG QPAHLARDWI VDTRSYLESR
LLAQLLVAHA AVSSIRSTY
