ID   FUND1_RAT               Reviewed;         155 AA.
AC   Q5BJS4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=FUN14 domain-containing protein 1;
GN   Name=Fundc1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; BC091353; AAH91353.1; -; mRNA.
DR   RefSeq; NP_001020198.1; NM_001025027.1.
DR   AlphaFoldDB; Q5BJS4; -.
DR   STRING; 10116.ENSRNOP00000004676; -.
DR   iPTMnet; Q5BJS4; -.
DR   PhosphoSitePlus; Q5BJS4; -.
DR   PaxDb; Q5BJS4; -.
DR   PRIDE; Q5BJS4; -.
DR   Ensembl; ENSRNOT00000004676; ENSRNOP00000004676; ENSRNOG00000003470.
DR   GeneID; 363442; -.
DR   KEGG; rno:363442; -.
DR   UCSC; RGD:1563372; rat.
DR   CTD; 139341; -.
DR   RGD; 1563372; Fundc1.
DR   eggNOG; KOG4099; Eukaryota.
DR   GeneTree; ENSGT00940000154517; -.
DR   HOGENOM; CLU_095425_2_0_1; -.
DR   InParanoid; Q5BJS4; -.
DR   OMA; ATVDHRE; -.
DR   OrthoDB; 1431148at2759; -.
DR   PhylomeDB; Q5BJS4; -.
DR   TreeFam; TF300280; -.
DR   Reactome; R-RNO-8934903; Receptor Mediated Mitophagy.
DR   PRO; PR:Q5BJS4; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000003470; Expressed in thymus and 20 other tissues.
DR   Genevisible; Q5BJS4; RN.
DR   GO; GO:0031307; C:integral component of mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISO:RGD.
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; IDA:RGD.
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_0000271347"
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:22673903"
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