ID   MIGA1_XENLA             Reviewed;         570 AA.
AC   Q6NRB7;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Mitoguardin 1 {ECO:0000250|UniProtKB:Q8NAN2};
DE   AltName: Full=Protein FAM73A {ECO:0000305};
GN   Name=miga1 {ECO:0000250|UniProtKB:Q8NAN2};
GN   Synonyms=fam73a {ECO:0000250|UniProtKB:Q8NAN2};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulator of mitochondrial fusion: acts by forming homo- and
CC       heterodimers at the mitochondrial outer membrane and facilitating the
CC       formation of pld6/MitoPLD dimers. May act by regulating phospholipid
CC       metabolism via pld6/MitoPLD. {ECO:0000250|UniProtKB:Q8NAN2}.
CC   -!- SUBUNIT: Homodimer and heterodimer; forms heterodimers with miga2.
CC       {ECO:0000250|UniProtKB:Q8NAN2}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q8NAN2}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the mitoguardin family. {ECO:0000305}.
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DR   EMBL; BC070842; AAH70842.1; -; mRNA.
DR   RefSeq; NP_001084810.1; NM_001091341.1.
DR   AlphaFoldDB; Q6NRB7; -.
DR   SMR; Q6NRB7; -.
DR   DNASU; 431851; -.
DR   GeneID; 431851; -.
DR   CTD; 431851; -.
DR   Xenbase; XB-GENE-5861525; miga1.L.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 431851; Expressed in egg cell and 17 other tissues.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR   InterPro; IPR019392; Miga.
DR   PANTHER; PTHR21508; PTHR21508; 1.
DR   Pfam; PF10265; Miga; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..570
FT                   /note="Mitoguardin 1"
FT                   /id="PRO_0000285649"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   570 AA;  64699 MW;  C6F621DF8D067E0F CRC64;
     MTETQHIFRL TVHRFMDFPL SIYSSFTQLK PTPGLKKIIA VAAISGVSLI FLACHLKRKR
     GKKKINAPQT EPGQFILQCS RHVAEKGSSC SSSRQNLTLS LGSIKERGSQ SHLNGDLCSK
     YSGSMQSLAS VQSCHSCACI NSNSWDKTDE DEINIPVTTP ENLYLMGMEL FEEALRRWEQ
     ALTFRSRQAE DEANCSSIKL GAGDAIAEEN IEDVISADFI HKLEALLQRA YRLQEEFEAT
     LGASDPASLA NDIDKDTDIT VMDNGGDFQQ RDTLSIASTD SFLSAAELAD NQDMRATCGL
     DSLYHHALYE EAMQLAEEGK VHCRVLRTEM LECLGDSDFL AKLHCIRQAF QEIILQRENR
     IFLMGTGRKL LSALIVKARK NPKKFEDAYF DMMSFLEQPE SWDTVEKELL SRGMKCMNFY
     DIVLDFIVMD SLEDLENPPL SIQNVVRNRW LNSSFKETAV TSSCWSVLRQ KKQEMKVPNG
     FFANFYTVCE QLCPVLAWGF LGPRSSLHDL CCFYKAQIMY FLKDIFDFEK VRYSDVEHLA
     EDIMKCLQRR TELTVVYTGE ESARRPPVLN