ID   FIS1_BOVIN              Reviewed;         152 AA.
AC   Q3T0I5;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Mitochondrial fission 1 protein;
DE   AltName: Full=Fis1 homolog;
GN   Name=FIS1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the fragmentation of the mitochondrial network
CC       and its perinuclear clustering. Plays a minor role in the recruitment
CC       and association of the fission mediator dynamin-related protein 1
CC       (DNM1L) to the mitochondrial surface and mitochondrial fission. Can
CC       induce cytochrome c release from the mitochondrion to the cytosol,
CC       ultimately leading to apoptosis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with DNM1L/DLP1 through the TPR region. Interacts
CC       with MARCH5. Interacts with MIEF1. Interacts with PEX11A, PEX11B and
CC       PEX11G. {ECO:0000250|UniProtKB:Q9Y3D6}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The C-terminus is required for mitochondrial localization,
CC       while the N-terminus is necessary for mitochondrial fission.
CC       {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by MARCH5. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FIS1 family. {ECO:0000305}.
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DR   EMBL; BC102383; AAI02384.1; -; mRNA.
DR   RefSeq; NP_001029956.1; NM_001034784.2.
DR   AlphaFoldDB; Q3T0I5; -.
DR   SMR; Q3T0I5; -.
DR   STRING; 9913.ENSBTAP00000010389; -.
DR   PaxDb; Q3T0I5; -.
DR   PeptideAtlas; Q3T0I5; -.
DR   PRIDE; Q3T0I5; -.
DR   Ensembl; ENSBTAT00000010389; ENSBTAP00000010389; ENSBTAG00000007900.
DR   GeneID; 615565; -.
DR   KEGG; bta:615565; -.
DR   CTD; 51024; -.
DR   VEuPathDB; HostDB:ENSBTAG00000007900; -.
DR   VGNC; VGNC:29014; FIS1.
DR   eggNOG; KOG3364; Eukaryota.
DR   GeneTree; ENSGT00390000000592; -.
DR   HOGENOM; CLU_104368_1_0_1; -.
DR   InParanoid; Q3T0I5; -.
DR   OMA; VTIQTKF; -.
DR   OrthoDB; 1595957at2759; -.
DR   TreeFam; TF315180; -.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000007900; Expressed in pons and 105 other tissues.
DR   ExpressionAtlas; Q3T0I5; baseline and differential.
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:0005777; C:peroxisome; ISS:UniProtKB.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR   GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IBA:GO_Central.
DR   GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR   GO; GO:0016559; P:peroxisome fission; IBA:GO_Central.
DR   GO; GO:0090141; P:positive regulation of mitochondrial fission; ISS:UniProtKB.
DR   GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS: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   2: Evidence at transcript level;
KW   Acetylation; Apoptosis; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
KW   TPR repeat; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   CHAIN           1..152
FT                   /note="Mitochondrial fission 1 protein"
FT                   /id="PRO_0000232436"
FT   TOPO_DOM        1..122
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        144..152
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REPEAT          71..104
FT                   /note="TPR"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y3D6"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y3D6"
SQ   SEQUENCE   152 AA;  16938 MW;  007DEB9872E59E9C CRC64;
     MEAVLNELVS VEDLLKFERK FKSEKAAGSV SKSTQFEYAW CLVRSKYNDD IRKGLALLEE
     LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT EPQNNQAKEL ERLIDKAMKK
     DGLVGMAIVG GMALGVAGLA GLIGLAVSKS KS