IMMT2_CAEEL
ID IMMT2_CAEEL Reviewed; 654 AA.
AC Q9XXN2;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=MICOS complex subunit MIC60-2 {ECO:0000305};
DE AltName: Full=Inner mitochondrial membrane protein 2 {ECO:0000303|PubMed:20578245};
DE AltName: Full=Mitofilin homolog 2 {ECO:0000305|PubMed:20578245};
DE Flags: Precursor;
GN Name=immt-2 {ECO:0000312|WormBase:W06H3.1};
GN ORFNames=W06H3.1 {ECO:0000312|WormBase:W06H3.1};
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 23% of
CC mutants, reduced brood size and increased resistance to oxidative
CC stress inducer paraquat (PubMed:20578245, PubMed:21248201). Abnormal
CC mitochondrial morphology with mitochondria appearing larger, thinner
CC and connected with large pores in the outer mitochondrial membrane
CC (PubMed:21248201). Mitochondria also have elongated and curved cristae
CC that are stacked with a reduced number of junctions (PubMed:21248201).
CC Double knockout with immt-1 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). {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; BX284605; CAA16516.2; -; Genomic_DNA.
DR PIR; T26251; T26251.
DR RefSeq; NP_507241.2; NM_074840.6.
DR AlphaFoldDB; Q9XXN2; -.
DR SMR; Q9XXN2; -.
DR STRING; 6239.W06H3.1; -.
DR EPD; Q9XXN2; -.
DR PaxDb; Q9XXN2; -.
DR PeptideAtlas; Q9XXN2; -.
DR PRIDE; Q9XXN2; -.
DR EnsemblMetazoa; W06H3.1.1; W06H3.1.1; WBGene00012315.
DR GeneID; 180122; -.
DR KEGG; cel:CELE_W06H3.1; -.
DR UCSC; W06H3.1; c. elegans.
DR CTD; 180122; -.
DR WormBase; W06H3.1; CE36215; WBGene00012315; immt-2.
DR eggNOG; KOG1854; Eukaryota.
DR GeneTree; ENSGT00390000002313; -.
DR HOGENOM; CLU_021851_2_0_1; -.
DR InParanoid; Q9XXN2; -.
DR OMA; MDIQNRK; -.
DR OrthoDB; 1073064at2759; -.
DR PhylomeDB; Q9XXN2; -.
DR PRO; PR:Q9XXN2; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00012315; Expressed in germ line (C elegans) 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..12
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 13..654
FT /note="MICOS complex subunit MIC60-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438530"
FT TOPO_DOM 13..20
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..654
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT REGION 115..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 72623 MW; 5B6F8FA081083367 CRC64;
MRGSRNLLTQ RLASSRATGS SGGLKFVGAT VGAVTAGAAG VAGYASYDNE FRKKLEGVIP
GSRTILNYTI GEEEPPAPRL KDLRPLQYSA DPKVPPKPFE PKPVKKELIG VKENLKETTE
PKKIEKKPEN PYIGAKTPLN PQERNEKLTE SLKNHLTQAE KATKVATSAK LETIRAIEHH
VQTIREAIEA GKDGDWDSVT VAHLKAKRLA EKDEKAEKLA RNAVADLVTE ANLGGQGETT
QLNPLVPISK ATAEKLSNEL DEMISNVKHV DSERIFVHDY SDRVAESRRK FQMELKAVHP
NLNYEDGMKI KKADLHTILA HAHLRIDQLS QKLIDSKLNE EKRIQSIIAK KKEDLLEKLR
LETNAKQAAV IPEFDKKKLD AELARATAEI QKKYDEKLKE VVRTQKQLYD IEHAKDVDEA
VLKERNLHSS AVGKALAQLA GIEKALSGHL QMDIENRKSK QMWLATQNLK GTVIFGNRAS
CCMEGRRAPL GDQMKTLLSC CGGGNSDEFV KTINTAMSKT SKVRGEYTEQ DLNTRFNKVC
RIGRRVAYVN EGGALAHLYS WLKSSLTIEL VPKKGANESL TPAVENNFTL LTRAEQLWKS
GKKSDAIRVL QLTDGATRRV AADFIADARR QHEALLLSRL LLAHAALTSI RSTY
