ID   A0A1J1I263_9DIPT        Unreviewed;       177 AA.
AC   A0A1J1I263;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   RecName: Full=Mitochondrial fission 1 protein {ECO:0000256|PIRNR:PIRNR008835};
GN   ORFNames=CLUMA_CG007890 {ECO:0000313|EMBL:CRK94381.1};
OS   Clunio marinus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC   Clunio.
OX   NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK94381.1, ECO:0000313|Proteomes:UP000183832};
RN   [1] {ECO:0000313|EMBL:CRK94381.1, ECO:0000313|Proteomes:UP000183832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the fragmentation of the mitochondrial network
CC       and its perinuclear clustering. {ECO:0000256|PIRNR:PIRNR008835}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC       outer membrane {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004572}.
CC   -!- DOMAIN: The C-terminus is required for mitochondrial localization,
CC       while the N-terminus is necessary for mitochondrial fission.
CC       {ECO:0000256|PIRNR:PIRNR008835}.
CC   -!- SIMILARITY: Belongs to the FIS1 family. {ECO:0000256|ARBA:ARBA00008937,
CC       ECO:0000256|PIRNR:PIRNR008835}.
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DR   EMBL; CVRI01000038; CRK94381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J1I263; -.
DR   STRING; 568069.A0A1J1I263; -.
DR   OrthoDB; 2997323at2759; -.
DR   Proteomes; UP000183832; Unassembled WGS sequence.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000266; P:mitochondrial fission; IEA:UniProtKB-UniRule.
DR   CDD; cd12212; Fis1; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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:SF0; MITOCHONDRIAL FISSION 1 PROTEIN; 1.
DR   PANTHER; PTHR13247; TETRATRICOPEPTIDE REPEAT PROTEIN 11 TPR REPEAT PROTEIN 11; 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; TPR-like; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR008835};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|PIRNR:PIRNR008835};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787,
KW   ECO:0000256|PIRNR:PIRNR008835};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        154..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   177 AA;  20305 MW;  62C38E6DC580AF70 CRC64;
     MDIVIKTEAW DEVLSNCCMW SSKDTPTNME EILSDTITPQ ELEKFEKVYM KELHEKKCVT
     AKTQFEYAWC LIRSKYGADI NNGIKIFEGL CKDNPDDKRD YIYYLAIAYC RIKDLPTSQN
     YVKAFLEIEP NNQQVLLLDE YIEKEMSKEF KKDAAIAGGA LLVFGGLLGL GFALAKK
//