ID   MIGA2_XENLA             Reviewed;         589 AA.
AC   Q6GR21;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Mitoguardin 2 {ECO:0000250|UniProtKB:Q7L4E1};
DE   AltName: Full=Protein FAM73B {ECO:0000305};
GN   Name=miga2 {ECO:0000250|UniProtKB:Q7L4E1}; Synonyms=fam73b;
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=Embryo;
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:Q7L4E1}.
CC   -!- SUBUNIT: Homodimer and heterodimer; forms heterodimers with miga1.
CC       {ECO:0000250|UniProtKB:Q7L4E1}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q7L4E1}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the mitoguardin family. {ECO:0000305}.
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DR   EMBL; BC071113; AAH71113.1; -; mRNA.
DR   RefSeq; NP_001085347.1; NM_001091878.1.
DR   AlphaFoldDB; Q6GR21; -.
DR   GeneID; 443773; -.
DR   KEGG; xla:443773; -.
DR   CTD; 443773; -.
DR   Xenbase; XB-GENE-996693; miga2.L.
DR   OrthoDB; 341855at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 443773; Expressed in liver and 19 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..589
FT                   /note="Mitoguardin 2"
FT                   /id="PRO_0000313661"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          87..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   589 AA;  65281 MW;  FC0684CAD369F4E4 CRC64;
     MAFQRAEGMS IIQALAMTVA EIPVFLYTTF GQSTFSQLRL SPGLRKVLFA TALGTVALAL
     AAHQLKRRKH KKKQITADNG GLKLGGVPGS VLPVRRSSSA KKGYSRSRVQ SPSSKSNDTL
     SGISSLDPSK HSSSSHSLAS VVAVNSSSIN AAPAGPWESP EMDETLEEGD SNAENLYIQG
     MELFEEALHK WEQALNVGQR CRSNTPASQV NDLLNQSCSE GLSEDSQSGH FAGKLEALLY
     RAYNLQEEFG TSIPPDDLLM DLEGSLIFPL VESRRALMMD DEGSSTSEDS FFSAAELFET
     LQLNEVPFLP TKPAAAYEEA LKLVHTGEVA CRTLRTELLG CYNDQDFLAK LHCVRQAFEV
     LLLDDGNQLF FGEVGKQMIT GLMQKAEKNP KGFLENYEEM LRYALKQDTW ATTQRELKGR
     GVVCMNFFDI ALDFILMDAF EDLESPPSSV LAVLRNRWLS DSFKETALAT ACWSVLKAKR
     RLLMVPDGFI SHFYSVSEHV SPVLAYGFLG PKEHLTEVCN FFKNQIVQYL KDMFDLDNVR
     YSTIQSLAED ILHLSRRRSD ILLGYLGVET VREMNGAVPV QTTEAELDL