ID   MDV1_YEAS7              Reviewed;         714 AA.
AC   A6ZQL5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Mitochondrial division protein 1;
DE   AltName: Full=Mitochondria fission 2 protein;
GN   Name=MDV1; Synonyms=FIS2, GAG3, NET2; ORFNames=SCY_3176;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Involved in mitochondrial fission. Has a partially redundant
CC       function to CAF4 in acting as an adapter protein, binding to FIS1 on
CC       the mitochondrial outer membrane and recruiting the dynamin-like GTPase
CC       DNM1 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   -!- SUBUNIT: Interacts with CAF4, DNM1 and FIS1, components of the
CC       mitochondrial fission machinery. Interacts via its N-terminal, coiled-
CC       coil extension (NTE) with FIS1, and via its WD repeats with DNM1 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Note=Uniformly distributed on the cytoplasmic face of
CC       the mitochondrial outer membrane. This localization is dependent on
CC       FIS1. Reorganizes to punctate structures on mitochondria, corresponding
CC       to mitochondrial constriction sites, at a late step in mitochondrial
CC       division. This relocalization is dependent on DNM1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat MDV1/CAF4 family. {ECO:0000305}.
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DR   EMBL; AAFW02000044; EDN63267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZQL5; -.
DR   SMR; A6ZQL5; -.
DR   PRIDE; A6ZQL5; -.
DR   EnsemblFungi; EDN63267; EDN63267; SCY_3176.
DR   HOGENOM; CLU_012350_1_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR021061; Mt_division_protein_1.
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; PF11542; Mdv1; 1.
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; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Phosphoprotein; Repeat; WD repeat.
FT   CHAIN           1..714
FT                   /note="Mitochondrial division protein 1"
FT                   /id="PRO_0000330115"
FT   REPEAT          396..436
FT                   /note="WD 1"
FT   REPEAT          439..478
FT                   /note="WD 2"
FT   REPEAT          500..539
FT                   /note="WD 3"
FT   REPEAT          561..603
FT                   /note="WD 4"
FT   REPEAT          604..642
FT                   /note="WD 5"
FT   REPEAT          644..681
FT                   /note="WD 6"
FT   REPEAT          685..714
FT                   /note="WD 7"
FT   REGION          323..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          240..298
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        330..347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         376
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P47025"
SQ   SEQUENCE   714 AA;  80058 MW;  D0D58271AAC032BC CRC64;
     MSVNDQITHI GKTLSTTASA FLNYQKSNSN TQDVLTNNGP YKNLLSNTVN NASSTSYFYK
     RTEHGRFVKN ASNTFEDIYS KTRRGDVFRN KFTDNKTCFR MLTYISDDLL NEIPTKEGLK
     SDADGKLLTE GGENENLRKN ASKKETSLFQ GFKSYLPIAE LAIENTERLN YDTNGTSGTV
     GAKDVMSKTN ERDEIHTELP NFQDSFLIPP GVETKKISSS YSPSALKSFS QTLVNSLEFL
     NIQKNSTLSE IRDIEVEVEN LRQKKEKLLG KIANIEQNQL LLEDNLKQID DRLDFLEEYG
     LEVIEANSDE NAEDDGMSER KALKNDAIRN EGVTTESISS EASNLPPRRR QQLRDDNSLN
     RLGAFYSKSK KRHRKSFPTF QQLYEPGTKI GSIMSTHDDF LTCLDFDAPF GTLCTAGYLD
     HTVKIWDLSK QNKIGELAGH LATINCMQIN RDYGTLVTGG RDAALKLWNL NLAQQLYQET
     QNLTSPTNHI DSPCVYTFEA HTDEVTALSL DPSFLVSGSQ DRTIRQWDLR SGKCLQTIDL
     SFANVLTTST NVDLSKSTLL TQRNERPSIG ALQSFDAALA TGTKDGVVRL WDLRSGKVIR
     TLKGHTDAIT SLKFDSACLV TGSYDRTVRI WDLRTGLLNK FHAYSAPVLS LDLFQENAAV
     VVADEPSVQI YDSEKDESWS CVEQGNETSV STVKYKENYM VEGRENGDVN IWAV