MDV1_YEAST
ID MDV1_YEAST Reviewed; 714 AA.
AC P47025; D6VW72;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Mitochondrial division protein 1;
DE AltName: Full=Mitochondria fission 2 protein;
GN Name=MDV1; Synonyms=FIS2, GAG3, NET2; OrderedLocusNames=YJL112W;
GN ORFNames=J0802;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8948101;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1471::aid-yea30>3.0.co;2-4;
RA Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.;
RT "Sequencing analysis of a 40.2 kb fragment of yeast chromosome X reveals 19
RT open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14,
RT RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta
RT elements and a Ty4 transposon.";
RL Yeast 12:1471-1474(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 596-714.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7483851; DOI=10.1002/yea.320110909;
RA Rasmussen S.W.;
RT "A 37.5 kb region of yeast chromosome X includes the SME1, MEF2, GSH1 and
RT CSD3 genes, a TCP-1-related gene, an open reading frame similar to the
RT DAL80 gene, and a tRNA(Arg).";
RL Yeast 11:873-883(1995).
RN [5]
RP FUNCTION, INTERACTION WITH DNM1, AND SUBCELLULAR LOCATION.
RX PubMed=11038182; DOI=10.1083/jcb.151.2.353;
RA Tieu Q., Nunnari J.;
RT "Mdv1p is a WD repeat protein that interacts with the dynamin-related
RT GTPase, Dnm1p, to trigger mitochondrial division.";
RL J. Cell Biol. 151:353-366(2000).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11038180; DOI=10.1083/jcb.151.2.333;
RA Fekkes P., Shepard K.A., Yaffe M.P.;
RT "Gag3p, an outer membrane protein required for fission of mitochondrial
RT tubules.";
RL J. Cell Biol. 151:333-340(2000).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11038183; DOI=10.1083/jcb.151.2.367;
RA Mozdy A.D., McCaffery J.M., Shaw J.M.;
RT "Dnm1p GTPase-mediated mitochondrial fission is a multi-step process
RT requiring the novel integral membrane component Fis1p.";
RL J. Cell Biol. 151:367-380(2000).
RN [8]
RP FUNCTION, AND INTERACTION WITH FIS1.
RX PubMed=12163467; DOI=10.1083/jcb.200205031;
RA Tieu Q., Okreglak V., Naylor K., Nunnari J.;
RT "The WD repeat protein, Mdv1p, functions as a molecular adaptor by
RT interacting with Dnm1p and Fis1p during mitochondrial fission.";
RL J. Cell Biol. 158:445-452(2002).
RN [9]
RP INTERACTION WITH DNM1 AND FIS1, AND MUTAGENESIS OF PHE-400; ARG-461;
RP ASP-664 AND SER-689.
RX PubMed=14517324; DOI=10.1091/mbc.e03-02-0092;
RA Cerveny K.L., Jensen R.E.;
RT "The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate division
RT of mitochondria.";
RL Mol. Biol. Cell 14:4126-4139(2003).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP INTERACTION WITH FIS1.
RX PubMed=15809300; DOI=10.1074/jbc.m414092200;
RA Suzuki M., Neutzner A., Tjandra N., Youle R.J.;
RT "Novel structure of the N terminus in yeast Fis1 correlates with a
RT specialized function in mitochondrial fission.";
RL J. Biol. Chem. 280:21444-21452(2005).
RN [13]
RP INTERACTION WITH CAF4, AND SUBCELLULAR LOCATION.
RX PubMed=16009724; DOI=10.1083/jcb.200503148;
RA Griffin E.E., Graumann J., Chan D.C.;
RT "The WD40 protein Caf4p is a component of the mitochondrial fission
RT machinery and recruits Dnm1p to mitochondria.";
RL J. Cell Biol. 170:237-248(2005).
RN [14]
RP FUNCTION, INTERACTION WITH FIS1, AND MUTAGENESIS OF GLU-250.
RX PubMed=16247028; DOI=10.1083/jcb.200506158;
RA Karren M.A., Coonrod E.M., Anderson T.K., Shaw J.M.;
RT "The role of Fis1p-Mdv1p interactions in mitochondrial fission complex
RT assembly.";
RL J. Cell Biol. 171:291-301(2005).
RN [15]
RP FUNCTION, INTERACTION WITH DNM1 AND FIS1, AND MUTAGENESIS OF LEU-148;
RP HIS-440; ASN-544 AND HIS-605.
RX PubMed=16272155; DOI=10.1074/jbc.m507943200;
RA Naylor K., Ingerman E., Okreglak V., Marino M., Hinshaw J.E., Nunnari J.;
RT "Mdv1 interacts with assembled Dnm1 to promote mitochondrial division.";
RL J. Biol. Chem. 281:2177-2183(2006).
RN [16]
RP FUNCTION, AND INTERACTION WITH DNM1.
RX PubMed=16601120; DOI=10.1074/jbc.m513530200;
RA Bhar D., Karren M.A., Babst M., Shaw J.M.;
RT "Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be
RT stimulated to assemble into fission complexes containing Mdv1 and Fis1.";
RL J. Biol. Chem. 281:17312-17320(2006).
RN [17]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [18]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT accumulation of a subclass of preproteins.";
RL Mol. Biol. Cell 17:1436-1450(2006).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [21]
RP FUNCTION.
RX PubMed=23530241; DOI=10.1073/pnas.1300855110;
RA Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.;
RT "Interchangeable adaptors regulate mitochondrial dynamin assembly for
RT membrane scission.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013).
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.
CC {ECO:0000269|PubMed:11038180, ECO:0000269|PubMed:11038182,
CC ECO:0000269|PubMed:11038183, ECO:0000269|PubMed:12163467,
CC ECO:0000269|PubMed:16247028, ECO:0000269|PubMed:16272155,
CC ECO:0000269|PubMed:16601120, ECO:0000269|PubMed:23530241}.
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.
CC {ECO:0000269|PubMed:11038182, ECO:0000269|PubMed:12163467,
CC ECO:0000269|PubMed:14517324, ECO:0000269|PubMed:15809300,
CC ECO:0000269|PubMed:16009724, ECO:0000269|PubMed:16247028,
CC ECO:0000269|PubMed:16272155, ECO:0000269|PubMed:16601120}.
CC -!- INTERACTION:
CC P47025; P40515: FIS1; NbExp=5; IntAct=EBI-26032, EBI-25059;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:11038180, ECO:0000269|PubMed:11038182,
CC ECO:0000269|PubMed:11038183, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16009724, ECO:0000269|PubMed:16407407,
CC ECO:0000269|PubMed:16823961}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11038180, ECO:0000269|PubMed:11038182,
CC ECO:0000269|PubMed:11038183, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16009724, ECO:0000269|PubMed:16407407,
CC ECO:0000269|PubMed:16823961}; Cytoplasmic side
CC {ECO:0000269|PubMed:11038180, ECO:0000269|PubMed:11038182,
CC ECO:0000269|PubMed:11038183, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16009724, ECO:0000269|PubMed:16407407,
CC ECO:0000269|PubMed:16823961}. Note=Uniformly distributed on the
CC cytoplasmic face of the mitochondrial outer membrane. This localization
CC is dependent on FIS1. Reorganizes to punctate structures on
CC mitochondria, corresponding to mitochondrial constriction sites, at a
CC late step in mitochondrial division. This relocalization is dependent
CC on DNM1.
CC -!- MISCELLANEOUS: Present with 3730 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat MDV1/CAF4 family. {ECO:0000305}.
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DR EMBL; Z49387; CAA89407.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08688.1; -; Genomic_DNA.
DR PIR; S56893; S56893.
DR RefSeq; NP_012423.1; NM_001181545.2.
DR PDB; 2PQN; X-ray; 2.15 A; B=122-171.
DR PDB; 2XU6; X-ray; 2.70 A; A/B=231-300.
DR PDB; 3UUX; X-ray; 3.90 A; B/D=94-314.
DR PDB; 5JST; X-ray; 2.20 A; A/B=230-300.
DR PDBsum; 2PQN; -.
DR PDBsum; 2XU6; -.
DR PDBsum; 3UUX; -.
DR PDBsum; 5JST; -.
DR AlphaFoldDB; P47025; -.
DR SMR; P47025; -.
DR BioGRID; 33644; 120.
DR DIP; DIP-1907N; -.
DR IntAct; P47025; 13.
DR MINT; P47025; -.
DR STRING; 4932.YJL112W; -.
DR iPTMnet; P47025; -.
DR MaxQB; P47025; -.
DR PaxDb; P47025; -.
DR PRIDE; P47025; -.
DR EnsemblFungi; YJL112W_mRNA; YJL112W; YJL112W.
DR GeneID; 853332; -.
DR KEGG; sce:YJL112W; -.
DR SGD; S000003648; MDV1.
DR VEuPathDB; FungiDB:YJL112W; -.
DR eggNOG; KOG4155; Eukaryota.
DR GeneTree; ENSGT00940000176613; -.
DR HOGENOM; CLU_012350_1_0_1; -.
DR InParanoid; P47025; -.
DR OMA; IVGVWTC; -.
DR BioCyc; YEAST:G3O-31566-MON; -.
DR EvolutionaryTrace; P47025; -.
DR PRO; PR:P47025; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47025; protein.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0000266; P:mitochondrial fission; IMP:SGD.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:SGD.
DR GO; GO:0016559; P:peroxisome fission; IGI:SGD.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..714
FT /note="Mitochondrial division protein 1"
FT /id="PRO_0000051477"
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:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 148
FT /note="L->P: Abolishes interaction with FIS1."
FT /evidence="ECO:0000269|PubMed:16272155"
FT MUTAGEN 250
FT /note="E->G: Suppresses the mitochondrial fission defect of
FT a FIS1-3 mutant by affecting interaction with FIS1."
FT /evidence="ECO:0000269|PubMed:16247028"
FT MUTAGEN 400
FT /note="F->A: No interaction with FIS1; slight decrease in
FT interaction with DNM1."
FT /evidence="ECO:0000269|PubMed:14517324"
FT MUTAGEN 440
FT /note="H->E,N: Abolishes interaction with DNM1."
FT /evidence="ECO:0000269|PubMed:16272155"
FT MUTAGEN 461
FT /note="R->A: Slight decrease in interaction with FIS1; 20-
FT fold decrease in interaction with DNM1; even distribution
FT along mitochondria not punctate."
FT /evidence="ECO:0000269|PubMed:14517324"
FT MUTAGEN 544
FT /note="N->R: Results in mitochondrial division defect, but
FT has no effect on the interaction with DNM1."
FT /evidence="ECO:0000269|PubMed:16272155"
FT MUTAGEN 605
FT /note="H->E: Abolishes interaction with DNM1."
FT /evidence="ECO:0000269|PubMed:16272155"
FT MUTAGEN 664
FT /note="D->A: Slight decrease in interaction with DNM1."
FT /evidence="ECO:0000269|PubMed:14517324"
FT MUTAGEN 689
FT /note="S->A: Slight decrease in interaction with DNM1."
FT /evidence="ECO:0000269|PubMed:14517324"
FT HELIX 148..161
FT /evidence="ECO:0007829|PDB:2PQN"
FT HELIX 231..289
FT /evidence="ECO:0007829|PDB:2XU6"
SQ SEQUENCE 714 AA; 80032 MW; CA8A23DBB06193A6 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 DSPCVHTFEA HTDEVTALSL DPSFLVSGSQ DRTIRQWDLR SGKCLQTIDL
SFANVLTTST NVDLSKSTLL TQRNERPSIG ALQSFDAALA TGTKDGVVRL WDLRSGKVIR
TLKGHTDAIT SLKFDSACLV TGSYDRTVRI WDLRTGLLNK FHAYSAPVLS LDLFQENAAV
VVADEPSVQI YDSEKDESWS CVEQGNETSV STVKYKENYM VEGRENGDVN IWAV
