FIS1_YEAST
ID FIS1_YEAST Reviewed; 155 AA.
AC P40515; D6VVL9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Mitochondrial fission 1 protein;
DE AltName: Full=Mitochondrial division protein 2;
GN Name=FIS1; Synonyms=MDV2; OrderedLocusNames=YIL065C;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
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, INTERACTION WITH MDV1, AND MUTAGENESIS OF LEU-80.
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12514182; DOI=10.1074/jbc.m212725200;
RA Beilharz T., Egan B., Silver P.A., Hofmann K., Lithgow T.;
RT "Bipartite signals mediate subcellular targeting of tail-anchored membrane
RT proteins in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:8219-8223(2003).
RN [8]
RP FUNCTION.
RX PubMed=12679388; DOI=10.1242/jcs.00423;
RA Jakobs S., Martini N., Schauss A.C., Egner A., Westermann B., Hell S.W.;
RT "Spatial and temporal dynamics of budding yeast mitochondria lacking the
RT division component Fis1p.";
RL J. Cell Sci. 116:2005-2014(2003).
RN [9]
RP INTERACTION WITH DNM1 AND MDV1.
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 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 [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [12]
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).
RN [13]
RP STRUCTURE BY NMR.
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).
CC -!- FUNCTION: Has a role in mitochondrial fission. Has a role in outer
CC membrane fission but not matrix separation. Required for targeting MDV1
CC to the mitochondria. Regulates the assembly of DNM1 into punctate
CC structures, in the mitochondrial tubules, promoting mitochondrial
CC membrane constriction and/or division. {ECO:0000269|PubMed:11038182,
CC ECO:0000269|PubMed:11038183, ECO:0000269|PubMed:12163467,
CC ECO:0000269|PubMed:12679388, ECO:0000269|PubMed:23530241}.
CC -!- SUBUNIT: Interacts with DNM1 and MDV1. {ECO:0000269|PubMed:12163467,
CC ECO:0000269|PubMed:14517324}.
CC -!- INTERACTION:
CC P40515; P36130: CAF4; NbExp=4; IntAct=EBI-25059, EBI-26394;
CC P40515; P47025: MDV1; NbExp=5; IntAct=EBI-25059, EBI-26032;
CC P40515; Q12118: SGT2; NbExp=3; IntAct=EBI-25059, EBI-31784;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:11038183, ECO:0000269|PubMed:12514182,
CC ECO:0000269|PubMed:14576278}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11038183, ECO:0000269|PubMed:12514182,
CC ECO:0000269|PubMed:14576278}.
CC -!- DOMAIN: The C-terminus is required for mitochondrial localization,
CC while the N-terminus is necessary for mitochondrial fission.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 2410 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FIS1 family. {ECO:0000305}.
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DR EMBL; Z38060; CAA86158.1; -; Genomic_DNA.
DR EMBL; AY557851; AAS56177.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08485.1; -; Genomic_DNA.
DR PIR; S48414; S48414.
DR RefSeq; NP_012199.3; NM_001179415.3.
DR PDB; 1Y8M; NMR; -; A=1-138.
DR PDB; 2PQN; X-ray; 2.15 A; A=1-129.
DR PDB; 2PQR; X-ray; 1.88 A; A/B=1-129.
DR PDB; 3O48; X-ray; 1.75 A; A=1-127.
DR PDB; 3UUX; X-ray; 3.90 A; A/C=1-129.
DR PDBsum; 1Y8M; -.
DR PDBsum; 2PQN; -.
DR PDBsum; 2PQR; -.
DR PDBsum; 3O48; -.
DR PDBsum; 3UUX; -.
DR AlphaFoldDB; P40515; -.
DR SMR; P40515; -.
DR BioGRID; 34927; 299.
DR DIP; DIP-1897N; -.
DR IntAct; P40515; 8.
DR MINT; P40515; -.
DR STRING; 4932.YIL065C; -.
DR iPTMnet; P40515; -.
DR MaxQB; P40515; -.
DR PaxDb; P40515; -.
DR PRIDE; P40515; -.
DR EnsemblFungi; YIL065C_mRNA; YIL065C; YIL065C.
DR GeneID; 854745; -.
DR KEGG; sce:YIL065C; -.
DR SGD; S000001327; FIS1.
DR VEuPathDB; FungiDB:YIL065C; -.
DR eggNOG; KOG3364; Eukaryota.
DR GeneTree; ENSGT00390000000592; -.
DR HOGENOM; CLU_104368_2_0_1; -.
DR InParanoid; P40515; -.
DR OMA; VTIQTKF; -.
DR BioCyc; YEAST:G3O-31333-MON; -.
DR Reactome; R-SCE-9603798; Class I peroxisomal membrane protein import.
DR EvolutionaryTrace; P40515; -.
DR PRO; PR:P40515; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40515; protein.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0000266; P:mitochondrial fission; IMP:SGD.
DR GO; GO:0016559; P:peroxisome fission; IGI:SGD.
DR GO; GO:0007031; P:peroxisome organization; IMP:SGD.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IDA:UniProtKB.
DR CDD; cd12212; Fis1; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR016543; Fis1.
DR InterPro; IPR033745; Fis1_cytosol.
DR InterPro; IPR028061; Fis1_TPR_C.
DR InterPro; IPR028058; Fis1_TPR_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13247; PTHR13247; 1.
DR Pfam; PF14853; Fis1_TPR_C; 1.
DR Pfam; PF14852; Fis1_TPR_N; 1.
DR PIRSF; PIRSF008835; TPR_repeat_11_Fis1; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..155
FT /note="Mitochondrial fission 1 protein"
FT /id="PRO_0000202982"
FT TOPO_DOM 1..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..155
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT MUTAGEN 80
FT /note="L->P: In fis1-L80P; no interaction with MDV1;
FT mitochondrial fission is blocked; DNM1 assembly at punctate
FT structures normal as in wild-type."
FT /evidence="ECO:0000269|PubMed:12163467"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3O48"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:3O48"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3O48"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:3O48"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1Y8M"
FT HELIX 55..71
FT /evidence="ECO:0007829|PDB:3O48"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:3O48"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:3O48"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:3O48"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:3O48"
SQ SEQUENCE 155 AA; 17733 MW; BD62D19524770536 CRC64;
MTKVDFWPTL KDAYEPLYPQ QLEILRQQVV SEGGPTATIQ SRFNYAWGLI KSTDVNDERL
GVKILTDIYK EAESRRRECL YYLTIGCYKL GEYSMAKRYV DTLFEHERNN KQVGALKSMV
EDKIQKETLK GVVVAGGVLA GAVAVASFFL RNKRR
