ID E2A3N4_CAMFO Unreviewed; 747 AA.
AC E2A3N4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 03-MAY-2023, entry version 51.
DE RecName: Full=MICOS complex subunit {ECO:0000256|RuleBase:RU363021};
GN ORFNames=EAG_03931 {ECO:0000313|EMBL:EFN71926.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN71926.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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.
CC {ECO:0000256|RuleBase:RU363021}.
CC -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC organizing system (MICOS) complex. {ECO:0000256|RuleBase:RU363021}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU363021}.
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DR EMBL; GL436457; EFN71926.1; -; Genomic_DNA.
DR AlphaFoldDB; E2A3N4; -.
DR STRING; 104421.E2A3N4; -.
DR InParanoid; E2A3N4; -.
DR OMA; VRTNESP; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
DR GO; GO:0061617; C:MICOS complex; IEA:UniProtKB-UniRule.
DR GO; GO:0042407; P:cristae formation; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd04450; DEP_RGS7-like; 1.
DR CDD; cd00068; GGL; 1.
DR CDD; cd08705; RGS_R7-like; 1.
DR Gene3D; 1.10.1240.60; -; 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR Gene3D; 4.10.260.10; Transducin (heterotrimeric G protein), gamma chain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR015898; G-protein_gamma-like_dom.
DR InterPro; IPR036284; GGL_sf.
DR InterPro; IPR019166; MIC26/MIC27.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR047016; RGS6/7/9/11.
DR InterPro; IPR047017; RGS6/7/9/11_DHEX_sf.
DR InterPro; IPR040759; RGS_DHEX.
DR InterPro; IPR034483; RGS_Egl-10.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45746; LP21163P; 1.
DR PANTHER; PTHR45746:SF6; LP21163P; 1.
DR Pfam; PF09769; ApoO; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00631; G-gamma; 1.
DR Pfam; PF00615; RGS; 1.
DR Pfam; PF18148; RGS_DHEX; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00049; DEP; 1.
DR SMART; SM01224; G_gamma; 1.
DR SMART; SM00224; GGL; 1.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR SUPFAM; SSF48670; Transducin (heterotrimeric G protein), gamma chain; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
DR PROSITE; PS50132; RGS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|RuleBase:RU363021};
KW Mitochondrion {ECO:0000256|RuleBase:RU363021};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU363021};
KW Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW Signal transduction inhibitor {ECO:0000256|ARBA:ARBA00022700}.
FT DOMAIN 312..386
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 522..582
FT /note="G protein gamma"
FT /evidence="ECO:0000259|PROSITE:PS50058"
FT DOMAIN 605..720
FT /note="RGS"
FT /evidence="ECO:0000259|PROSITE:PS50132"
FT REGION 231..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 519..546
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 253..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 85392 MW; A4495AF0154D67B3 CRC64;
MSPYSNESGV KKLIRPSELP IYPFEDDYSK QIPCTECSPS ALERNISKIR KSVQAVMSEY
QHYTGVISDT IDTGVEHSKS LLDYLREESN VMPRMGAIAI GGLAGLVLGL RGRTFKRVVY
SSTGALATAA VCYPKKAEEG LDTAKHYINV GYNFVYGVKP GDDRQLKITI PELPKLKIPT
SFSEFVDLTI VIGSTVTTTV GSFAQNIYTS LSDNKEGRCI SRRVDMVTMN SEKSACRRKP
VEKSSSSSSS GKKTSEHVEE ADKKNDDVRT NESPDLSPNT PTYNVTASCA EDTPNYLVYK
KMESIVEKML DEFTGVPVKT VKTFMTKTPS VFTGADLIVW MMKNMDIDDQ EALHVAHLMA
SHGYFFPIDD HCLTVKNDNT FYRFQTPYFW PSNCWEPENT DYAVYLCKRT MQNKTRLELA
DYEAENLARL QKMFSRKWEF IFMQAEAQSK VDKKRDKLER KVLDSQERAF WDVHRPMPGC
VNTTELDIKK ACRSYKSVIQ PSKHLQLGVA GGKISPSPES NATSSIEFLQ KQIETLKDRL
DRTVIKVSKV AEALIGYFEQ YMEYDPFLTQ PELTNPWVSD SPEMWEQEKL AKEISTRRVK
RWAFSLQELL QDPVGREQFI RFLDKEFSGE NLKFWETVQE LKTLPQKDVQ TKVEEIWREF
LDTDASCPIN VDSRSYEITK KNLEKPDQWC FDVAAAHVYH LMKSDSYSRY LRSEMYKDFL
NGSKKKTSVK GIRSIVSFTG RRDTTVS
//
