MIGA2_MOUSE
ID MIGA2_MOUSE Reviewed; 593 AA.
AC Q8BK03; A6PX05; Q3U4J7; Q3UST7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Mitoguardin 2 {ECO:0000250|UniProtKB:Q7L4E1};
DE AltName: Full=Protein FAM73B;
GN Name=Miga2 {ECO:0000250|UniProtKB:Q7L4E1};
GN Synonyms=Fam73b {ECO:0000250|UniProtKB:Q7L4E1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Corpora quadrigemina, Dendritic cell, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-228, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; THR-206; SER-220;
RP SER-224; SER-228; THR-273 AND SER-276, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26711011; DOI=10.1016/j.molcel.2015.11.017;
RA Zhang Y., Liu X., Bai J., Tian X., Zhao X., Liu W., Duan X., Shang W.,
RA Fan H.Y., Tong C.;
RT "Mitoguardin regulates mitochondrial fusion through MitoPLD and is required
RT for neuronal homeostasis.";
RL Mol. Cell 61:111-124(2016).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=26716412; DOI=10.18632/oncotarget.6713;
RA Liu X.M., Zhang Y.P., Ji S.Y., Li B.T., Tian X., Li D., Tong C., Fan H.Y.;
RT "Mitoguardin-1 and -2 promote maturation and the developmental potential of
RT mouse oocytes by maintaining mitochondrial dynamics and functions.";
RL Oncotarget 7:1155-1167(2016).
CC -!- FUNCTION: Regulator of mitochondrial fusion (PubMed:26711011). Acts by
CC forming homo- and heterodimers at the mitochondrial outer membrane and
CC facilitating the formation of PLD6/MitoPLD dimers. May act by
CC regulating phospholipid metabolism via PLD6/MitoPLD (By similarity).
CC {ECO:0000250|UniProtKB:Q7L4E1, ECO:0000269|PubMed:26711011}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BK03-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BK03-2; Sequence=VSP_030093, VSP_030094;
CC -!- DISRUPTION PHENOTYPE: Mitochondrial fragmentation: mitochondria become
CC round and show loss of cristae (PubMed:26711011). Female mice show
CC decreased quality of oocytes (PubMed:26716412). Mice lacking both Miga1
CC and Miga2 show strongly reduced quality of oocytes and are subfertile
CC (PubMed:26716412). {ECO:0000269|PubMed:26711011,
CC ECO:0000269|PubMed:26716412}.
CC -!- SIMILARITY: Belongs to the mitoguardin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE32434.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK077618; BAC36904.1; -; mRNA.
DR EMBL; AK140122; BAE24244.1; -; mRNA.
DR EMBL; AK154200; BAE32434.1; ALT_INIT; mRNA.
DR EMBL; AL954388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051404; AAH51404.1; -; mRNA.
DR CCDS; CCDS15880.1; -. [Q8BK03-1]
DR RefSeq; NP_001229336.1; NM_001242407.1. [Q8BK03-1]
DR RefSeq; NP_780601.1; NM_175392.3. [Q8BK03-1]
DR AlphaFoldDB; Q8BK03; -.
DR STRING; 10090.ENSMUSP00000097787; -.
DR iPTMnet; Q8BK03; -.
DR PhosphoSitePlus; Q8BK03; -.
DR EPD; Q8BK03; -.
DR jPOST; Q8BK03; -.
DR MaxQB; Q8BK03; -.
DR PaxDb; Q8BK03; -.
DR PeptideAtlas; Q8BK03; -.
DR PRIDE; Q8BK03; -.
DR ProteomicsDB; 295909; -. [Q8BK03-1]
DR ProteomicsDB; 295910; -. [Q8BK03-2]
DR Antibodypedia; 50430; 22 antibodies from 10 providers.
DR Ensembl; ENSMUST00000077977; ENSMUSP00000077127; ENSMUSG00000026858. [Q8BK03-1]
DR Ensembl; ENSMUST00000100214; ENSMUSP00000097787; ENSMUSG00000026858. [Q8BK03-1]
DR Ensembl; ENSMUST00000140075; ENSMUSP00000135519; ENSMUSG00000026858. [Q8BK03-2]
DR GeneID; 108958; -.
DR KEGG; mmu:108958; -.
DR UCSC; uc008jcf.2; mouse. [Q8BK03-2]
DR UCSC; uc008jcg.2; mouse. [Q8BK03-1]
DR CTD; 84895; -.
DR MGI; MGI:1922035; Miga2.
DR VEuPathDB; HostDB:ENSMUSG00000026858; -.
DR eggNOG; KOG3831; Eukaryota.
DR GeneTree; ENSGT00390000008565; -.
DR HOGENOM; CLU_031519_2_1_1; -.
DR InParanoid; Q8BK03; -.
DR OMA; YDICLDF; -.
DR OrthoDB; 341855at2759; -.
DR PhylomeDB; Q8BK03; -.
DR TreeFam; TF313896; -.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR BioGRID-ORCS; 108958; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Fam73b; mouse.
DR PRO; PR:Q8BK03; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BK03; protein.
DR Bgee; ENSMUSG00000026858; Expressed in brown adipose tissue and 256 other tissues.
DR ExpressionAtlas; Q8BK03; baseline and differential.
DR Genevisible; Q8BK03; MM.
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; IMP:MGI.
DR GO; GO:0008053; P:mitochondrial fusion; IMP:UniProtKB.
DR InterPro; IPR019392; Miga.
DR PANTHER; PTHR21508; PTHR21508; 1.
DR Pfam; PF10265; Miga; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..593
FT /note="Mitoguardin 2"
FT /id="PRO_0000313659"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 98..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..229
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 199..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 273
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 391..443
FT /note="SPKGFLESYEEMLSYALRPETWATTRLELEGRGVACMSFFDIVLDFILMDAF
FT E -> VAGVGLLQIPLRTLPQAGLLLCFVLFCRLLTGFLTQKSWACEVTQWVQDWQPE
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030093"
FT VAR_SEQ 444..593
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030094"
SQ SEQUENCE 593 AA; 65548 MW; 24992DA0CB628794 CRC64;
MAFRRTEGMS MIQALAMTVA EIPVFLYTTF GQSAFSQLRL TPGLRKVLFA TALGTVALAL
AAHQLKRRRR KKKQVGPEMG GEQLGTVPMP ILMARKVPSV KKGCSSRRVQ SPSSKSNDTL
SGISSIEPSK HSGSSHSLAS MVVVNSSSPT AACSGSWEAR GMEESVPTTD GSAESLYVQG
MELFEEALQK WEQALSVGQR GDGGSTPTPG DSLQNPDTAS EALSEPESQR REFAEKLESL
LHRAYHLQEE FGSTFPSDSM LLDLERTLML PLTEGSLRLR ADDEDSLTSE DSFFSATEIF
ESLQIGEYPL PLSRPAAAYE EALQLVKEGR VPCRTLRTEL LGCYSDQDFL AKLHCVRQAF
EGLLEERSNQ IFFGEVGRQM VTGLMTKAEK SPKGFLESYE EMLSYALRPE TWATTRLELE
GRGVACMSFF DIVLDFILMD AFEDLENPPS SVLAVLRNRW LSDSFKETAL ATACWSVLKA
KRRLLMVPDG FISHFYSVSE HVSPVLAFGF LGPKPQLSEV CAFFKHQIVQ YLRDMFDLDN
VRYTSVPALA EDILQLSRRR SEILLGYLGA PVASSIGLNG PLPRENGPLE ELQ
