ID   FUND2_PIG               Reviewed;         189 AA.
AC   Q864V5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 68.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cheng J.;
RT   "Identification and sequence analysis of Sus scrofa homologous gene of
RT   HCBP6.";
RL   Submitted (FEB-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; AY234859; AAO89276.1; -; mRNA.
DR   RefSeq; NP_998908.1; NM_213743.1.
DR   AlphaFoldDB; Q864V5; -.
DR   STRING; 9823.ENSSSCP00000013626; -.
DR   PaxDb; Q864V5; -.
DR   PeptideAtlas; Q864V5; -.
DR   Ensembl; ENSSSCT00000014010; ENSSSCP00000013626; ENSSSCG00000012817.
DR   Ensembl; ENSSSCT00015051939; ENSSSCP00015020723; ENSSSCG00015039043.
DR   Ensembl; ENSSSCT00025068364; ENSSSCP00025029400; ENSSSCG00025050111.
DR   Ensembl; ENSSSCT00030012654; ENSSSCP00030005674; ENSSSCG00030009272.
DR   Ensembl; ENSSSCT00035086420; ENSSSCP00035036001; ENSSSCG00035064224.
DR   Ensembl; ENSSSCT00040074852; ENSSSCP00040032114; ENSSSCG00040055254.
DR   Ensembl; ENSSSCT00045014485; ENSSSCP00045010044; ENSSSCG00045008605.
DR   Ensembl; ENSSSCT00050101455; ENSSSCP00050044142; ENSSSCG00050074130.
DR   Ensembl; ENSSSCT00055046016; ENSSSCP00055036691; ENSSSCG00055023345.
DR   Ensembl; ENSSSCT00060026502; ENSSSCP00060011278; ENSSSCG00060019630.
DR   Ensembl; ENSSSCT00065024673; ENSSSCP00065010089; ENSSSCG00065018524.
DR   Ensembl; ENSSSCT00070013939; ENSSSCP00070011489; ENSSSCG00070007242.
DR   GeneID; 396564; -.
DR   KEGG; ssc:396564; -.
DR   CTD; 65991; -.
DR   VGNC; VGNC:103944; FUNDC2.
DR   eggNOG; KOG4099; Eukaryota.
DR   GeneTree; ENSGT00940000154783; -.
DR   HOGENOM; CLU_095425_2_0_1; -.
DR   InParanoid; Q864V5; -.
DR   OMA; TERYSMA; -.
DR   OrthoDB; 1431148at2759; -.
DR   TreeFam; TF300280; -.
DR   Proteomes; UP000008227; Chromosome X.
DR   Proteomes; UP000314985; Unassembled WGS sequence.
DR   Bgee; ENSSSCG00000012817; Expressed in longissimus lumborum muscle and 45 other tissues.
DR   ExpressionAtlas; Q864V5; baseline and differential.
DR   Genevisible; Q864V5; SS.
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..189
FT                   /note="FUN14 domain-containing protein 2"
FT                   /id="PRO_0000314618"
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;  20572 MW;  82C1515AC7C4E113 CRC64;
     METSSPRAGS QPAPTAARYF ASCRAEPLRV SSRDQLAEMA AASQGNFEGN FESLDLAELA
     KKQPWWRKLF GQESGPSAEK YSVATQLLIG GVTGWCTGFI FQKVGKLAAT AVGGGFFLLQ
     LANHTGYIKV DWQRVEKDMK KAKEQLKIRK SNQIPTEVKS KAEEVVSFVK KNVLVTGGFF
     GGFLLGMAS