FIS1_DROME
ID FIS1_DROME Reviewed; 154 AA.
AC B7YZT2; A1Z6G3; B7YZT3; Q8SYX2;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Mitochondrial fission 1 protein {ECO:0000255|PIRNR:PIRNR008835};
GN Name=Fis1 {ECO:0000303|PubMed:18443288, ECO:0000312|FlyBase:FBgn0039969};
GN ORFNames=CG17510 {ECO:0000312|FlyBase:FBgn0039969};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAL48886.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:ANY27232.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=18443288; DOI=10.1073/pnas.0711845105;
RA Yang Y., Ouyang Y., Yang L., Beal M.F., McQuibban A., Vogel H., Lu B.;
RT "Pink1 regulates mitochondrial dynamics through interaction with the
RT fission/fusion machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7070-7075(2008).
RN [6]
RP ERRATUM OF PUBMED:18443288.
RA Yang Y., Ouyang Y., Yang L., Beal M.F., McQuibban A., Vogel H., Lu B.;
RL Proc. Natl. Acad. Sci. U.S.A. 105:17585-17585(2008).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20194754; DOI=10.1073/pnas.0913485107;
RA Ziviani E., Tao R.N., Whitworth A.J.;
RT "Drosophila parkin requires PINK1 for mitochondrial translocation and
RT ubiquitinates mitofusin.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:5018-5023(2010).
CC -!- FUNCTION: Involved in the fragmentation of the mitochondrial network
CC and its perinuclear clustering (PubMed:18443288, PubMed:20194754).
CC Functions downstream of Pink1 and upstream of Drp1 to regulate
CC mitochondrial fission (PubMed:18443288). {ECO:0000269|PubMed:18443288,
CC ECO:0000269|PubMed:20194754}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000255|PIRNR:PIRNR008835}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=C {ECO:0000312|FlyBase:FBgn0039969};
CC IsoId=B7YZT2-1; Sequence=Displayed;
CC Name=E {ECO:0000312|FlyBase:FBgn0039969};
CC IsoId=B7YZT2-2; Sequence=VSP_059257;
CC Name=D {ECO:0000312|FlyBase:FBgn0039969}; Synonyms=F
CC {ECO:0000312|FlyBase:FBgn0039969};
CC IsoId=B7YZT2-3; Sequence=VSP_059256, VSP_059257;
CC Name=A {ECO:0000312|FlyBase:FBgn0039969}; Synonyms=G
CC {ECO:0000312|FlyBase:FBgn0039969};
CC IsoId=B7YZT2-4; Sequence=VSP_059256;
CC -!- DOMAIN: The C-terminus is required for mitochondrial localization,
CC while the N-terminus is necessary for mitochondrial fission.
CC {ECO:0000255|PIRNR:PIRNR008835}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in elongated
CC mitochondria. {ECO:0000269|PubMed:20194754}.
CC -!- SIMILARITY: Belongs to the FIS1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE013599; ACL83061.1; -; Genomic_DNA.
DR EMBL; AE013599; ACL83062.1; -; Genomic_DNA.
DR EMBL; AE013599; ACL83063.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68367.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68368.2; -; Genomic_DNA.
DR EMBL; AE013599; AHN55938.1; -; Genomic_DNA.
DR EMBL; AY071264; AAL48886.1; -; mRNA.
DR EMBL; KX531422; ANY27232.1; -; mRNA.
DR RefSeq; NP_001137607.1; NM_001144135.2. [B7YZT2-1]
DR RefSeq; NP_001137608.1; NM_001144136.3. [B7YZT2-2]
DR RefSeq; NP_001137609.1; NM_001144137.3. [B7YZT2-3]
DR RefSeq; NP_001286140.1; NM_001299211.1. [B7YZT2-4]
DR RefSeq; NP_652100.1; NM_143843.4. [B7YZT2-4]
DR RefSeq; NP_724420.1; NM_165439.4. [B7YZT2-3]
DR AlphaFoldDB; B7YZT2; -.
DR SMR; B7YZT2; -.
DR IntAct; B7YZT2; 1.
DR STRING; 7227.FBpp0271716; -.
DR PaxDb; B7YZT2; -.
DR PRIDE; B7YZT2; -.
DR DNASU; 49892; -.
DR EnsemblMetazoa; FBtr0086073; FBpp0085409; FBgn0039969. [B7YZT2-4]
DR EnsemblMetazoa; FBtr0273208; FBpp0271716; FBgn0039969. [B7YZT2-1]
DR EnsemblMetazoa; FBtr0273209; FBpp0271717; FBgn0039969. [B7YZT2-3]
DR EnsemblMetazoa; FBtr0273210; FBpp0271718; FBgn0039969. [B7YZT2-2]
DR EnsemblMetazoa; FBtr0273211; FBpp0271719; FBgn0039969. [B7YZT2-3]
DR EnsemblMetazoa; FBtr0345012; FBpp0311263; FBgn0039969. [B7YZT2-4]
DR GeneID; 49892; -.
DR KEGG; dme:Dmel_CG17510; -.
DR UCSC; CG17510-RA; d. melanogaster.
DR UCSC; CG17510-RC; d. melanogaster.
DR CTD; 51024; -.
DR FlyBase; FBgn0039969; Fis1.
DR VEuPathDB; VectorBase:FBgn0039969; -.
DR eggNOG; KOG3364; Eukaryota.
DR GeneTree; ENSGT00390000000592; -.
DR InParanoid; B7YZT2; -.
DR OMA; RRDYLYY; -.
DR PhylomeDB; B7YZT2; -.
DR Reactome; R-DME-9603798; Class I peroxisomal membrane protein import.
DR BioGRID-ORCS; 49892; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 49892; -.
DR PRO; PR:B7YZT2; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0039969; Expressed in antenna and 20 other tissues.
DR ExpressionAtlas; B7YZT2; baseline and differential.
DR Genevisible; B7YZT2; DM.
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:0005778; C:peroxisomal membrane; ISS:FlyBase.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0000266; P:mitochondrial fission; IBA:GO_Central.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IGI:FlyBase.
DR GO; GO:0016559; P:peroxisome fission; IBA:GO_Central.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:FlyBase.
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 2: Evidence at transcript level;
KW Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..154
FT /note="Mitochondrial fission 1 protein"
FT /id="PRO_0000442534"
FT TOPO_DOM 1..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..154
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform D and isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_059256"
FT VAR_SEQ 148..154
FT /note="NKQKREK -> K (in isoform E and isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_059257"
SQ SEQUENCE 154 AA; 17771 MW; EB0AE1DD4960AFDB CRC64;
MEDLLNEVVP QEDLERFEKK YHHELELDGE VTTDTKFEYA FCLVRSRYTN DVRKGIMILE
ELARTHPDGR RDYIYYLAFG NARIKEYTSG LKYCRAFLDI ESNDQVRSLE EYIKKEIDKE
VAKGMVVAGG AALVLGGILG LGIAMARNKQ KREK
