ID   FUND2_BOVIN             Reviewed;         190 AA.
AC   Q8MJN0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=FUN14 domain-containing protein 2 {ECO:0000250|UniProtKB:Q9BWH2};
DE   AltName: Full=Hepatitis C virus core-binding protein 6;
GN   Name=FUNDC2 {ECO:0000250|UniProtKB:Q9BWH2}; Synonyms=HCBP6;
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 [MRNA].
RA   Li K., Cheng J., Zhang L., Wang L., Lu Y., Wang G., Liu Y.;
RT   "Cloning and sequence analysis of cDNA encoding hepatitis C virus core-
RT   binding protein 6.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds directly and specifically 1,2-Diacyl-sn-glycero-3-
CC       phospho-(1'-myo-inositol-3',4',5'-bisphosphate) (PIP3) leading to the
CC       recruitment of PIP3 to mitochondria and may play a role in the
CC       regulation of the platelet activation via AKT/GSK3B/cGMP signaling
CC       pathways (By similarity). May act as transcription factor that
CC       regulates SREBP1 (isoform SREBP-1C) expression in order to modulate
CC       triglyceride (TG) homeostasis in hepatocytes (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BWH2, ECO:0000250|UniProtKB:Q9D6K8}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q9BWH2}; Multi-pass membrane protein
CC       {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q9BWH2}.
CC   -!- SIMILARITY: Belongs to the FUN14 family. {ECO:0000305}.
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DR   EMBL; AF375478; AAM46089.1; -; mRNA.
DR   EMBL; BC109698; AAI09699.1; -; mRNA.
DR   RefSeq; NP_776763.1; NM_174338.4.
DR   AlphaFoldDB; Q8MJN0; -.
DR   STRING; 9913.ENSBTAP00000022579; -.
DR   iPTMnet; Q8MJN0; -.
DR   PaxDb; Q8MJN0; -.
DR   PRIDE; Q8MJN0; -.
DR   Ensembl; ENSBTAT00000022579; ENSBTAP00000022579; ENSBTAG00000016977.
DR   GeneID; 281813; -.
DR   KEGG; bta:281813; -.
DR   CTD; 65991; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016977; -.
DR   VGNC; VGNC:29144; FUNDC2.
DR   eggNOG; KOG4099; Eukaryota.
DR   GeneTree; ENSGT00940000154783; -.
DR   HOGENOM; CLU_095425_2_0_1; -.
DR   InParanoid; Q8MJN0; -.
DR   OMA; TERYSMA; -.
DR   OrthoDB; 1431148at2759; -.
DR   TreeFam; TF300280; -.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000016977; Expressed in semitendinosus and 105 other tissues.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR   GO; GO:0035356; P:cellular triglyceride homeostasis; ISS:UniProtKB.
DR   GO; GO:0010543; P:regulation of platelet activation; ISS:UniProtKB.
DR   InterPro; IPR007014; FUN14.
DR   PANTHER; PTHR21346; PTHR21346; 1.
DR   Pfam; PF04930; FUN14; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..190
FT                   /note="FUN14 domain-containing protein 2"
FT                   /id="PRO_0000314614"
FT   TOPO_DOM        1..81
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        103..108
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..165
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..190
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT   MOD_RES         54
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
SQ   SEQUENCE   190 AA;  20577 MW;  59AC4AF3F6CD54D6 CRC64;
     METSTQRTGS HLAQTAAARH SASSRGEAAR VSSRDELAEM AAASQGNFEG KFESLDLAEL
     AKKQPWWRTL FGQESGPSAE KYSVATQLLI GGVTGWCTGF IFQKVGKLAA TAVGGGFFLL
     QLANHTGYIK VDWQRVEKDM KKAKEQLKIR KSNQIPTEVK SKAEEVVSFV KKNVLVTGGF
     FGGFLLGMAS