MIGA2_BOVIN
ID MIGA2_BOVIN Reviewed; 593 AA.
AC Q1JPG0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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};
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 MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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 Interacts with PLD6/MitoPLD. {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; BT025393; ABF57349.1; -; mRNA.
DR RefSeq; NP_001069521.1; NM_001076053.1.
DR RefSeq; XP_005213362.1; XM_005213305.3.
DR AlphaFoldDB; Q1JPG0; -.
DR STRING; 9913.ENSBTAP00000014090; -.
DR PaxDb; Q1JPG0; -.
DR PRIDE; Q1JPG0; -.
DR Ensembl; ENSBTAT00000014090; ENSBTAP00000014090; ENSBTAG00000010653.
DR GeneID; 535315; -.
DR KEGG; bta:535315; -.
DR CTD; 84895; -.
DR VEuPathDB; HostDB:ENSBTAG00000010653; -.
DR VGNC; VGNC:31474; MIGA2.
DR eggNOG; KOG3831; Eukaryota.
DR GeneTree; ENSGT00390000008565; -.
DR HOGENOM; CLU_031519_2_1_1; -.
DR InParanoid; Q1JPG0; -.
DR OMA; YDICLDF; -.
DR OrthoDB; 341855at2759; -.
DR TreeFam; TF313896; -.
DR Reactome; R-BTA-1483166; Synthesis of PA.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000010653; Expressed in retina and 105 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:0060348; P:bone development; IEA:Ensembl.
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; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..593
FT /note="Mitoguardin 2"
FT /id="PRO_0000313658"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 101..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BK03"
FT MOD_RES 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BK03"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BK03"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L4E1"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BK03"
FT MOD_RES 273
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7L4E1"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L4E1"
SQ SEQUENCE 593 AA; 65433 MW; 568904EBC2BC48D2 CRC64;
MAFRRTEGMS MIQALAMTVA EIPVFLYTTF GQSAFSQLRL TPGLRKVLFA TALGTVALAL
AAHQLKRRRR KKKQVGPEMG GEHLGTVPLP ILMARKVPSV KKGYSNRRVQ SPSSKSNDTL
SGISSIEPSK HSGSSHSLAS MVVVNSSSPT AACSGPWETR GIEESVTTAD GNAESLYMQG
MELFEEALQK WEQALSVGQR GDSGSTPTPG DGLRNPETAS EALSEPESQR KEFAEKLESL
LHRAYHLQEE FGSTFPADSM LLDLERTLML PLTEGSLRLR ADDGDSLTSE DSFFSATELF
ESLQVGDYPI PLSRPAAAYE EALQLVKEGK VPCRTLRTEL LGCYSDQDFL AKLHCVRQAF
EGLLEDKSHQ LFFGEVGRQM VTGLMTKAEK SPKGFLESYE EMLSYALRPE TWATTRLELE
GRGVVCMSFF DIVLDFILMD AFEDLENPPS SVLAVLRNRW LSDSFKETAL ATACWSVLKA
KRRLLMVPDG FISHFYSVSE HVSPVLAFGF LGPKPQLSEV CAFFKHQIVQ YLTDMFDLDN
VRYTSVPALA EDILQLSRRR SEILLGYLGV PAASSIGLNG VLPRENGPPE ALQ
