ID   FUND2_MACMU             Reviewed;         189 AA.
AC   Q7YRC0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 55.
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   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cheng J., Li K., Wang L., Liu Y., Zhong Y., Li L.;
RT   "Identification and sequence analysis of a monkey gene homologous to human
RT   hepatitis C virus core protein-binding protein 6.";
RL   Submitted (JUL-2003) 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; AY340968; AAQ17075.1; -; mRNA.
DR   RefSeq; NP_001028072.1; NM_001032900.1.
DR   AlphaFoldDB; Q7YRC0; -.
DR   STRING; 9544.ENSMMUP00000020086; -.
DR   GeneID; 574259; -.
DR   KEGG; mcc:574259; -.
DR   CTD; 65991; -.
DR   eggNOG; KOG4099; Eukaryota.
DR   InParanoid; Q7YRC0; -.
DR   OrthoDB; 1431148at2759; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
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: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..189
FT                   /note="FUN14 domain-containing protein 2"
FT                   /id="PRO_0000314616"
FT   TOPO_DOM        1..80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..107
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..164
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        186..189
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH2"
SQ   SEQUENCE   189 AA;  20678 MW;  672FB6C4512B0EE9 CRC64;
     METSAPRAGS QVVATTERHS AACRADPLRV SSRDKLTEMA ASTQGNFDGN FESLDLAEFA
     KKQPWWRKLF GQESGPSAEK YSVATQLFIG GVTGWCTGFI FQNVGKLAAT AVGGGFFLLQ
     LANHTGYIKV DWQRVEKDMK KAKEQLKIRK SNQMPTEVRS KAEEVVSFVK KNVLVTGGFF
     GGFLLGMAS