ID   MFFB_DANRE              Reviewed;         230 AA.
AC   Q7SZQ4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Mitochondrial fission factor homolog B;
GN   ORFNames=zgc:66022;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA   Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT   analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
CC   -!- FUNCTION: Plays a role in mitochondrial and peroxisomal fission.
CC       Promotes the recruitment and association of the fission mediator
CC       dynamin-related protein 1 (DNM1L) to the mitochondrial surface (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Single-pass type IV membrane protein {ECO:0000250}. Peroxisome
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Tango11 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; BC056301; AAH56301.1; -; mRNA.
DR   RefSeq; NP_956830.1; NM_200536.1.
DR   AlphaFoldDB; Q7SZQ4; -.
DR   SMR; Q7SZQ4; -.
DR   iPTMnet; Q7SZQ4; -.
DR   Ensembl; ENSDART00000059195; ENSDARP00000059194; ENSDARG00000053753.
DR   GeneID; 393508; -.
DR   KEGG; dre:393508; -.
DR   CTD; 393508; -.
DR   ZFIN; ZDB-GENE-040426-1510; mffa.
DR   eggNOG; ENOG502R96B; Eukaryota.
DR   GeneTree; ENSGT00390000009776; -.
DR   HOGENOM; CLU_066026_0_0_1; -.
DR   InParanoid; Q7SZQ4; -.
DR   OMA; ERIVVAX; -.
DR   OrthoDB; 1383657at2759; -.
DR   PhylomeDB; Q7SZQ4; -.
DR   TreeFam; TF325506; -.
DR   PRO; PR:Q7SZQ4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 15.
DR   Bgee; ENSDARG00000053753; Expressed in brain and 24 other tissues.
DR   ExpressionAtlas; Q7SZQ4; baseline.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
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   GO; GO:0006626; P:protein targeting to mitochondrion; IBA:GO_Central.
DR   InterPro; IPR039433; Mff-like_dom.
DR   InterPro; IPR008518; Mff/Tango-11.
DR   PANTHER; PTHR16501; PTHR16501; 2.
DR   Pfam; PF05644; Miff; 2.
PE   1: Evidence at protein level;
KW   Coiled coil; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Peroxisome; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..230
FT                   /note="Mitochondrial fission factor homolog B"
FT                   /id="PRO_0000289189"
FT   TOPO_DOM        1..210
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..228
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        229..230
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          117..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          179..210
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        129..144
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18307296"
SQ   SEQUENCE   230 AA;  26253 MW;  895E17B309FE6BB3 CRC64;
     MSGAAFPSPT AEIAEMNRIH YELEYTEGIS QRMRIPEQLK VAPYGSEDQE LPDHELLHTA
     MMHVPERIIV AGHSDDMPFP RDLDLIQSTP QESTLSLKTP PRVLTLSDRP LDFLEMEQTS
     SVSHPSEEVR TQTKTRRERS VSENAGVHHN GPLARNDSAF ALATLDSTLE GGTDDMAVVD
     ATSLRRQIVK LNRRLQLLEE ENKERAKREM VMYSITVAFW LVNSWVWFRR