FUND1_BOVIN
ID FUND1_BOVIN Reviewed; 155 AA.
AC F1N5S9; A6QQX3;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=FUN14 domain-containing protein 1;
GN Name=FUNDC1;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; DAAA02073542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150029; AAI50030.1; -; mRNA.
DR RefSeq; NP_001098452.1; NM_001104982.1.
DR AlphaFoldDB; F1N5S9; -.
DR SMR; F1N5S9; -.
DR STRING; 9913.ENSBTAP00000002144; -.
DR PaxDb; F1N5S9; -.
DR PRIDE; F1N5S9; -.
DR Ensembl; ENSBTAT00000002144; ENSBTAP00000002144; ENSBTAG00000001637.
DR GeneID; 518258; -.
DR KEGG; bta:518258; -.
DR CTD; 139341; -.
DR VEuPathDB; HostDB:ENSBTAG00000001637; -.
DR VGNC; VGNC:29143; FUNDC1.
DR eggNOG; KOG4099; Eukaryota.
DR GeneTree; ENSGT00940000154517; -.
DR HOGENOM; CLU_095425_2_0_1; -.
DR InParanoid; F1N5S9; -.
DR OMA; ATVDHRE; -.
DR OrthoDB; 1431148at2759; -.
DR TreeFam; TF300280; -.
DR Reactome; R-BTA-8934903; Receptor Mediated Mitophagy.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000001637; Expressed in adenohypophysis and 105 other tissues.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR InterPro; IPR007014; FUN14.
DR PANTHER; PTHR21346; PTHR21346; 1.
DR Pfam; PF04930; FUN14; 1.
PE 2: Evidence at transcript 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_0000416275"
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:0000250|UniProtKB:Q8IVP5"
FT MOD_RES 18
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:Q8IVP5"
FT CONFLICT 113
FT /note="I -> V (in Ref. 2; AAI50030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 155 AA; 17173 MW; AB9F3271D5BC7CAF CRC64;
MATRNPPPQE YESDDDSYEV LDLTEYARRH HWWNRVFGHS SGPMVEKYSV ATQIVMGGVS
GWCAGFLFQK VGKLAATAVG GGFLLLQIAS HSGYVQIDWK RVEKDVNKAK RQIKKRANKA
APEINNIIEE ATEFVKQNIV ISSGFVGGFL LGLAS