MDV1_ASHGO
ID MDV1_ASHGO Reviewed; 715 AA.
AC Q758R7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Mitochondrial division protein 1;
GN Name=MDV1; OrderedLocusNames=AEL314W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Involved in mitochondrial fission. Acts as an adapter protein
CC required to form mitochondrial fission complexes. Formation of these
CC complexes is required to promote constriction and fission of the
CC mitochondrial compartment at a late step in mitochondrial division (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat MDV1/CAF4 family. {ECO:0000305}.
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DR EMBL; AE016818; AAS52370.1; -; Genomic_DNA.
DR RefSeq; NP_984546.1; NM_209899.1.
DR AlphaFoldDB; Q758R7; -.
DR SMR; Q758R7; -.
DR STRING; 33169.AAS52370; -.
DR EnsemblFungi; AAS52370; AAS52370; AGOS_AEL314W.
DR GeneID; 4620718; -.
DR KEGG; ago:AGOS_AEL314W; -.
DR eggNOG; KOG4155; Eukaryota.
DR HOGENOM; CLU_012350_1_0_1; -.
DR InParanoid; Q758R7; -.
DR OMA; IVGVWTC; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
DR GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR GO; GO:0016559; P:peroxisome fission; IBA:GO_Central.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IEA:EnsemblFungi.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Coiled coil; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..715
FT /note="Mitochondrial division protein 1"
FT /id="PRO_0000330095"
FT REPEAT 409..449
FT /note="WD 1"
FT REPEAT 452..490
FT /note="WD 2"
FT REPEAT 503..542
FT /note="WD 3"
FT REPEAT 564..604
FT /note="WD 4"
FT REPEAT 605..644
FT /note="WD 5"
FT REPEAT 646..681
FT /note="WD 6"
FT REPEAT 685..715
FT /note="WD 7"
FT REGION 122..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 228..268
FT /evidence="ECO:0000255"
FT COMPBIAS 131..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 715 AA; 79870 MW; 29C9ED47E57B3465 CRC64;
MSSGTSGDQI SHFGKTLTTT ASLVFGSQSM EDTILSYSSP YKKILHDTIT SSGGTSSLMK
VERSGRMFTP FRTRNSAFQD IFHASSGRGY FKNGFSDTRT SFQVLSYLSD AMLADIPSSE
SAAATSGKLV TEKGEKGKKK RAETAHARGP SLYQGFEASL PTINQTITTH QKKQIMNRDI
KSIRESDATP EDVGQDVDIE KGEEETTHDE FTLPKGIKPE HLSNSYSIKN LKGAVQTITD
NLDLLEIQKN LAASEIRELD LKMEKLKLMR DLVFRRVAKI EQNELFLEKH LMNIRERIDM
IEEYNLDNDT DAEKAYEEAT SAPEDTKDQY SELPDANTAE SGETVVQEPQ VNLASAQKSL
KKRSKQTGYS HKNHEKKVQQ HEFRHLRKTY PTLQQYYEPG ANILSFDSAH EDNVTCLDFN
LPFGTLCSAG KLDPTIKVWN LSKNKHVASI TGHLATVSCM QMDQYNTLIT GGRDALLKMW
DIQKAIDNDS IPSDEVCIYT FDSHIDEITA LSFEANNLVS GSQDRTIRQW DLNNGKCVQT
LDINFATGGN LSRSMIGSGF LNTNNDHPII GAIQCYDAAL ATGTKDGIVR LWDLRSGRVV
RTLEGHSDAV TSLQFDSLNL VTGSLDNSIR IWDLRTGTLA DTFSYEHPVT CLQFDLNKIV
VANQEGTVKV YNRQEKKHWF CGGDEHSENA VEYVRYKDGY LVEGRANGDI NAWAI
