MIGA2_DANRE
ID MIGA2_DANRE Reviewed; 596 AA.
AC Q5BLE2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Mitoguardin 2 {ECO:0000250|UniProtKB:Q7L4E1};
DE AltName: Full=Protein FAM73B {ECO:0000305};
GN Name=miga2 {ECO:0000250|UniProtKB:Q7L4E1};
GN Synonyms=fam73b {ECO:0000250|UniProtKB:Q7L4E1};
GN ORFNames=zgc:113131 {ECO:0000303|Ref.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2005) 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; BC090475; AAH90475.1; -; mRNA.
DR RefSeq; NP_001013575.1; NM_001013557.1.
DR AlphaFoldDB; Q5BLE2; -.
DR STRING; 7955.ENSDARP00000109341; -.
DR PaxDb; Q5BLE2; -.
DR GeneID; 541431; -.
DR KEGG; dre:541431; -.
DR CTD; 84895; -.
DR ZFIN; ZDB-GENE-050320-135; miga2.
DR eggNOG; KOG3831; Eukaryota.
DR InParanoid; Q5BLE2; -.
DR OrthoDB; 341855at2759; -.
DR PhylomeDB; Q5BLE2; -.
DR Reactome; R-DRE-1483166; Synthesis of PA.
DR PRO; PR:Q5BLE2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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..596
FT /note="Mitoguardin 2"
FT /id="PRO_0000313660"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 67..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 596 AA; 66256 MW; 4651C1003B6055F6 CRC64;
MSFRSAEGVS IMQALAMTVA EIPVFLYSTF GQSIFSQLKL SPSLKKVLFA TALGSVALAL
TAHQLKRRGR KRKQTLGKEA QKPVGIPEQL LRSSRPASLK RGPVPARQMM SPSTRSNDTL
SGVSSIAQSK HSSSSHSIAS MRVPSSPNQS VNAGAAWEAE PVAEEPAVGE DANAENLYLM
GMELFEEALR KWELALNIRH RSHSRASASN SQGSELVERH SPEVRNHQFA ERLETLLHRA
YHLQEDFGST IPPDSLLADL ESEGTLILPT LGSSHPIQDD DATTVTSDDS FFSAAELFET
FSLEDSFHLL KPAALYEEAL SLVKDGDVAC RSLRTELLEC YSDQDFLAKL HCVRQAFQVL
LLDETHRMFF METGKQMISG LLVKANKSPK AFLESYEDML QYTQREETWP VSKMELEGRG
VVCMNFFDIV LDFILMDAFE DLESPPSSVV AVLRNRWLSD SFKETALATA CWSVLKAKRR
LLMVPDGFIA HFYVISEHVS PVLAFGFLGP HQHLSEVCTI FKQQIVQYLK DMFDHDKVRF
TSVPSLAEDI LRLSHRRADI LMGYLGIENL PETNGALPKS PCQAESGNLD ASGQQD