FUND2_MOUSE
ID FUND2_MOUSE Reviewed; 151 AA.
AC Q9D6K8; Q80VT2; Q80YD9; Q8BSM8; Q9D617;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=FUN14 domain-containing protein 2 {ECO:0000305};
DE AltName: Full=Hepatitis C virus core-binding protein 6;
GN Name=Fundc2 {ECO:0000312|MGI:MGI:1914641}; Synonyms=Hcbp6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Cheng J., Li K., Wang L.;
RT "Identification and sequence analysis of a mouse homologous gene HCBP6.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Forelimb, Head, and Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, Eye, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=30576423; DOI=10.1093/cvr/cvy311;
RA Ma Q., Zhang W., Zhu C., Liu J., Chen Q.;
RT "FUNDC2 regulates platelet activation through AKT/GSK-3beta/cGMP axis.";
RL Cardiovasc. Res. 115:1672-1679(2019).
RN [7]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=29786068; DOI=10.1038/s41418-018-0121-8;
RA Ma Q., Zhu C., Zhang W., Ta N., Zhang R., Liu L., Feng D., Cheng H.,
RA Liu J., Chen Q.;
RT "Mitochondrial PIP3-binding protein FUNDC2 supports platelet survival via
RT AKT signaling pathway.";
RL Cell Death Differ. 26:321-331(2019).
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 (PubMed:30576423, PubMed:29786068). May act as transcription
CC factor that regulates SREBP1 (isoform SREBP-1C) expression in order to
CC modulate triglyceride (TG) homeostasis in hepatocytes (By similarity).
CC {ECO:0000250|UniProtKB:Q9BWH2, ECO:0000269|PubMed:29786068,
CC ECO:0000269|PubMed:30576423}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q9BWH2}; Multi-pass membrane protein
CC {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q9BWH2}.
CC -!- TISSUE SPECIFICITY: Highly expressed in platelet (at protein level)
CC (PubMed:29786068, PubMed:30576423). Expressed in liver, brain, heart
CC and muscle (PubMed:29786068). {ECO:0000269|PubMed:29786068,
CC ECO:0000269|PubMed:30576423}.
CC -!- SIMILARITY: Belongs to the FUN14 family. {ECO:0000305}.
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DR EMBL; AY234858; AAO89275.1; -; mRNA.
DR EMBL; AK013460; BAB28867.1; -; mRNA.
DR EMBL; AK014705; BAB29513.1; -; mRNA.
DR EMBL; AK031214; BAC27304.1; -; mRNA.
DR EMBL; AL731844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042794; AAH42794.1; -; mRNA.
DR EMBL; BC049566; AAH49566.2; -; mRNA.
DR EMBL; BC061464; AAH61464.1; -; mRNA.
DR CCDS; CCDS30239.1; -.
DR RefSeq; NP_080402.3; NM_026126.4.
DR AlphaFoldDB; Q9D6K8; -.
DR BioGRID; 212155; 4.
DR IntAct; Q9D6K8; 1.
DR STRING; 10090.ENSMUSP00000033541; -.
DR iPTMnet; Q9D6K8; -.
DR PhosphoSitePlus; Q9D6K8; -.
DR SwissPalm; Q9D6K8; -.
DR EPD; Q9D6K8; -.
DR jPOST; Q9D6K8; -.
DR MaxQB; Q9D6K8; -.
DR PaxDb; Q9D6K8; -.
DR PeptideAtlas; Q9D6K8; -.
DR PRIDE; Q9D6K8; -.
DR ProteomicsDB; 271645; -.
DR Antibodypedia; 31390; 92 antibodies from 17 providers.
DR DNASU; 67391; -.
DR Ensembl; ENSMUST00000033541; ENSMUSP00000033541; ENSMUSG00000031198.
DR GeneID; 67391; -.
DR KEGG; mmu:67391; -.
DR UCSC; uc009tpu.2; mouse.
DR CTD; 65991; -.
DR MGI; MGI:1914641; Fundc2.
DR VEuPathDB; HostDB:ENSMUSG00000031198; -.
DR eggNOG; KOG4099; Eukaryota.
DR GeneTree; ENSGT00940000154783; -.
DR HOGENOM; CLU_095425_2_0_1; -.
DR InParanoid; Q9D6K8; -.
DR OMA; TERYSMA; -.
DR OrthoDB; 1431148at2759; -.
DR PhylomeDB; Q9D6K8; -.
DR TreeFam; TF300280; -.
DR BioGRID-ORCS; 67391; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Fundc2; mouse.
DR PRO; PR:Q9D6K8; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9D6K8; protein.
DR Bgee; ENSMUSG00000031198; Expressed in bone fossa and 242 other tissues.
DR Genevisible; Q9D6K8; MM.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
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; IMP:UniProtKB.
DR InterPro; IPR007014; FUN14.
DR PANTHER; PTHR21346; PTHR21346; 1.
DR Pfam; PF04930; FUN14; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..151
FT /note="FUN14 domain-containing protein 2"
FT /id="PRO_0000314617"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..69
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..151
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q9BWH2"
FT CONFLICT 30..31
FT /note="KL -> NS (in Ref. 2; BAB29513)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="A -> D (in Ref. 2; BAC27304)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 151 AA; 16564 MW; 7EC4C8B9301D64ED CRC64;
MAANSQGNFD GKFEALDLAE LTKKQPWWRK LFGQESGPSA EKYSVATQLV IGGVTGWCTG
FVFQKVGKLA ATAVGGGFFL LQLANHTGYI KVDWQRVEKD MKKAKEQLKI RKNKQIPTEV
KSKAEEVVSF VKKNVLVTGG FFGGFLLGMA S
