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MDV1_CANGA
ID   MDV1_CANGA              Reviewed;         711 AA.
AC   Q6FT96;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Mitochondrial division protein 1;
GN   Name=MDV1; OrderedLocusNames=CAGL0G04345g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Involved in mitochondrial fission. Has a partially redundant
CC       function to CAF4 in acting as an adapter protein required to form
CC       mitochondrial fission complexes. Formation of these complexes is
CC       required to promote constriction and fission of the mitochondrial
CC       compartment at a late step in mitochondrial division (By similarity).
CC       {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; CR380953; CAG59475.1; -; Genomic_DNA.
DR   RefSeq; XP_446548.1; XM_446548.1.
DR   AlphaFoldDB; Q6FT96; -.
DR   SMR; Q6FT96; -.
DR   STRING; 5478.XP_446548.1; -.
DR   EnsemblFungi; CAG59475; CAG59475; CAGL0G04345g.
DR   GeneID; 2888015; -.
DR   KEGG; cgr:CAGL0G04345g; -.
DR   CGD; CAL0130372; CAGL0G04345g.
DR   VEuPathDB; FungiDB:CAGL0G04345g; -.
DR   eggNOG; KOG4155; Eukaryota.
DR   HOGENOM; CLU_012350_1_0_1; -.
DR   InParanoid; Q6FT96; -.
DR   Proteomes; UP000002428; Chromosome G.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
DR   GO; GO:0000266; P:mitochondrial fission; IEA:EnsemblFungi.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IEA:EnsemblFungi.
DR   GO; GO:0016559; P:peroxisome fission; IEA:EnsemblFungi.
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; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
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..711
FT                   /note="Mitochondrial division protein 1"
FT                   /id="PRO_0000330101"
FT   REPEAT          402..442
FT                   /note="WD 1"
FT   REPEAT          445..484
FT                   /note="WD 2"
FT   REPEAT          497..536
FT                   /note="WD 3"
FT   REPEAT          560..601
FT                   /note="WD 4"
FT   REPEAT          602..639
FT                   /note="WD 5"
FT   REPEAT          641..680
FT                   /note="WD 6"
FT   REPEAT          682..711
FT                   /note="WD 7"
FT   REGION          116..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          224..281
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   711 AA;  80326 MW;  47AD6DC50F2E84C8 CRC64;
     MTDQISHLGK TLSTAASVLI GSQDIEKNVE NNLLSNSPRN PYRKTLQESL TAADFMNHET
     FDKLRKTRAI ASTLSEDSKG LYSQRSREKY FTNKVSDKKT TFKVLSHLSD DLLKDLPETA
     ESKSNTRDQG ETKLLKESDS TDASQERIFS LYQGFEASIP VINRSVEKEH LLLEQNNQES
     AAQILPQMGN KPRIRSGPWE DLLESKEDTY ISLDFNPERI SNIKSKKELE RINELANNNL
     VMLDIRKKLS ADEIDEIKKQ IQDLQLKQNL LVKKIAAIEE NELFLEDIIR LIGHRSADFS
     NDTQIEFDQA KSLSGLNNPE SMIDATRPTA LERKNSIDIV ETSLNEIRTS FDGSKQSIEG
     KDNHNALNGF FEDASNKKSR KAQPTVQKYY NSGKKLSTIP KAHDDAITCL DFDPHFSTLC
     TAGYMDHIVK LWDYTKKRQI GAMEGHVATI SCMQVDKNYN MVATGSKDAT VKLWNANDVI
     GRYEEGNNSE ALHTLDAHLD EVSSLYIDGA NLMTASQDKT IRRWDLYSGK CIQVFDVNFP
     SLSAYKSSFM KSNEDSMILK TVNTPIIGSI QSFDAALATG TKDGLIRLWD MRTGEVVRVL
     EGHMDAITSL KFDATTIISG SLDGTIRLWD LRSNNLTDII SYEKPISSLD FDAKHIVVAS
     NEHNTHIYDR NDGNKWDLQD EEQDTTSLFV KYKERYTMEG RSNGDIGIWI V
 
 
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