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 27-MAR-2024, entry version 67.
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 HOGENOM; CLU_012350_1_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 6.10.280.220; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19846:SF0; SFM DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR19846; WD40 REPEAT PROTEIN; 1.
DR Pfam; PF11542; Mdv1; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 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
//
