MDV1_KLULA
ID MDV1_KLULA Reviewed; 705 AA.
AC Q6CJ50;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Mitochondrial division protein 1;
GN Name=MDV1; OrderedLocusNames=KLLA0F21406g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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. 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; CR382126; CAG98747.1; -; Genomic_DNA.
DR RefSeq; XP_456039.1; XM_456039.1.
DR AlphaFoldDB; Q6CJ50; -.
DR SMR; Q6CJ50; -.
DR STRING; 28985.XP_456039.1; -.
DR EnsemblFungi; CAG98747; CAG98747; KLLA0_F21406g.
DR GeneID; 2895446; -.
DR KEGG; kla:KLLA0_F21406g; -.
DR eggNOG; KOG4155; Eukaryota.
DR HOGENOM; CLU_012350_1_0_1; -.
DR InParanoid; Q6CJ50; -.
DR OMA; IVGVWTC; -.
DR Proteomes; UP000000598; Chromosome F.
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; 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..705
FT /note="Mitochondrial division protein 1"
FT /id="PRO_0000330106"
FT REPEAT 395..435
FT /note="WD 1"
FT REPEAT 438..476
FT /note="WD 2"
FT REPEAT 492..529
FT /note="WD 3"
FT REPEAT 547..594
FT /note="WD 4"
FT REPEAT 595..632
FT /note="WD 5"
FT REPEAT 634..671
FT /note="WD 6"
FT REPEAT 676..705
FT /note="WD 7"
FT REGION 110..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 216..250
FT /evidence="ECO:0000255"
FT COMPBIAS 295..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 79490 MW; F474DBAAA82A1D09 CRC64;
MSSNTGDQFA NLGKALSTTA SVLFSSQPME DTILSYSSPY KKLLHETITN AGGGSSLVKV
RHDVKLSKGK NTGFQDIYSN SKEFFKNSYS DPKTTFKVLS YLSDDLLEDA PRDTIPQNKN
MITENGEKRS AKSKKQEPTL FQGFEASLPV INETIELQQK LIMNSDMKPL TDSESIPVYA
EEEEQEEEFS LPDHLKADKL LHSYSASFLK DASRSITDNL DLLEIQKNLA ASEIRELDIK
LEKLKMMREL VFKRVAKIEQ HELFLEKHLN NVKDRIDMII EYNMDKEYSS EDEENINGLS
ELSPKTGETN ETYETAATTP LENKEEEHSP LLSKSIYQQL QDHEKKSDIS ERKKHSTSKK
IKDVGVSHRN RRRKTYPTLQ QFYDSGSKIT SLPKAHDEDI TCLDFDMPFG TMCSAGSLDH
SVKVWDLSKK KQIATLHGHL ASISCMQIDQ YSTLITGGRD AVLKLWDIDK AMADEASNSS
EDNDACLYTF DSHVDEITAI SFDGDNLVSG SQDRTVRQWD LNSGKCTQTI DISFATGPMR
SQRNIPLRNS VLLTKEPPAI GALQCFDAAL ATGTKDGIVR LWDLRSGKVV RMLEGHTDAI
TSLQFDSVNL VTGAMDRSIR IWDLRTGILS DVFAYEQPIT SLHFDLDKIV ISNNEPTVKI
YNRKDGNHWF CGEDDPEQGN VDFVRYKHGY LVEGRSNGDI NTWAI
