FUND1_MOUSE
ID FUND1_MOUSE Reviewed; 155 AA.
AC Q9DB70; A2BEA3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=FUN14 domain-containing protein 1;
GN Name=Fundc1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Kidney;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N-3; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
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).
CC -!- FUNCTION: Acts as an activator of hypoxia-induced mitophagy, an
CC important mechanism for mitochondrial quality control. {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via YXXL motif) with MAP1 LC3 family proteins
CC MAP1LC3A, MAP1LC3B and GABARAP. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9DB70; O70405: Ulk1; NbExp=2; IntAct=EBI-10106464, EBI-8390771;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The YXXL motif mediates the interaction with MAP1 LC3 family
CC proteins MAP1LC3A, MAP1LC3B and GABARAP. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Tyr-18 by SRC inhibits activation of mitophagy.
CC Following hypoxia, dephosphorylated at Tyr-18, leading to interaction
CC with MAP1 LC3 family proteins and triggering mitophagy (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FUN14 family. {ECO:0000305}.
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DR EMBL; AK005163; BAB23854.1; -; mRNA.
DR EMBL; AK168868; BAE40687.1; -; mRNA.
DR EMBL; BX005345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466584; EDL35721.1; -; Genomic_DNA.
DR EMBL; BC012515; AAH12515.1; -; mRNA.
DR EMBL; BC030487; AAH30487.1; -; mRNA.
DR CCDS; CCDS30035.1; -.
DR RefSeq; NP_001300674.1; NM_001313745.1.
DR RefSeq; NP_082334.1; NM_028058.4.
DR AlphaFoldDB; Q9DB70; -.
DR IntAct; Q9DB70; 1.
DR MINT; Q9DB70; -.
DR STRING; 10090.ENSMUSP00000026016; -.
DR iPTMnet; Q9DB70; -.
DR PhosphoSitePlus; Q9DB70; -.
DR EPD; Q9DB70; -.
DR jPOST; Q9DB70; -.
DR MaxQB; Q9DB70; -.
DR PaxDb; Q9DB70; -.
DR PeptideAtlas; Q9DB70; -.
DR PRIDE; Q9DB70; -.
DR ProteomicsDB; 271613; -.
DR Antibodypedia; 25165; 242 antibodies from 27 providers.
DR DNASU; 72018; -.
DR Ensembl; ENSMUST00000026016; ENSMUSP00000026016; ENSMUSG00000025040.
DR GeneID; 72018; -.
DR KEGG; mmu:72018; -.
DR UCSC; uc009ssf.1; mouse.
DR CTD; 139341; -.
DR MGI; MGI:1919268; Fundc1.
DR VEuPathDB; HostDB:ENSMUSG00000025040; -.
DR eggNOG; KOG4099; Eukaryota.
DR GeneTree; ENSGT00940000154517; -.
DR InParanoid; Q9DB70; -.
DR OMA; ATVDHRE; -.
DR OrthoDB; 1431148at2759; -.
DR PhylomeDB; Q9DB70; -.
DR TreeFam; TF300280; -.
DR Reactome; R-MMU-8934903; Receptor Mediated Mitophagy.
DR BioGRID-ORCS; 72018; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Fundc1; mouse.
DR PRO; PR:Q9DB70; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9DB70; protein.
DR Bgee; ENSMUSG00000025040; Expressed in facial nucleus and 252 other tissues.
DR ExpressionAtlas; Q9DB70; baseline and differential.
DR Genevisible; Q9DB70; MM.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0010243; P:response to organonitrogen compound; ISO:MGI.
DR InterPro; IPR007014; FUN14.
DR PANTHER; PTHR21346; PTHR21346; 1.
DR Pfam; PF04930; FUN14; 1.
PE 1: Evidence at protein level;
KW Autophagy; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..155
FT /note="FUN14 domain-containing protein 1"
FT /id="PRO_0000271346"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..74
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT MOTIF 18..21
FT /note="YXXL"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 18
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:Q8IVP5"
SQ SEQUENCE 155 AA; 17159 MW; 8AAA46566714ED80 CRC64;
MASRNPPPQD YESDDESYEV LDLTEYARRH HWWNRVFGHS SGPMVEKYSV ATQIVMGGVT
GWCAGFLFQK VGKLAATAVG GGFLLLQVAS HSGYVQIDWK RVEKDVNKAK RQIKKRANKA
APEINNIIEE ATDFIKQNIV ISSGFVGGFL LGLAS
