LOCUS       NP_573464                757 aa            linear   ROD 12-NOV-2024
DEFINITION  mitofusin-2 [Mus musculus].
ACCESSION   NP_573464 XP_910073 XP_924201 XP_924208 XP_924217 XP_924228
            XP_924237 XP_924250 XP_924257
VERSION     NP_573464.2
DBSOURCE    REFSEQ: accession NM_133201.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Xu,M.X., Xu,T. and An,N.
  TITLE     Suppression of miR-17 Alleviates Acute Respiratory
            Distress-associated Lung Fibrosis by Regulating Mfn2
  JOURNAL   Curr Med Sci 44 (5), 964-970 (2024)
   PUBMED   39446286
  REMARK    GeneRIF: Suppression of miR-17 Alleviates Acute Respiratory
            Distress-associated Lung Fibrosis by Regulating Mfn2.
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Zhang,Y., Ma,L., Wang,Z., Gao,C., Yang,L., Li,M., Tang,X., Yuan,H.,
            Pang,D. and Ouyang,H.
  TITLE     Mfn2R364W, Mfn2G176S, and Mfn2H165R mutations drive
            Charcot-Marie-Tooth type 2A disease by inducing apoptosis and
            mitochondrial oxidative phosphorylation damage
  JOURNAL   Int J Biol Macromol 278 (Pt 1), 134673 (2024)
   PUBMED   39142491
  REMARK    GeneRIF: Mfn2[R364W], Mfn2[G176S], and Mfn2[H165R] mutations drive
            Charcot-Marie-Tooth type 2A disease by inducing apoptosis and
            mitochondrial oxidative phosphorylation damage.
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Lu,L., Ning,Y., Gu,F., Lin,Z., Qin,Y., Feng,L., Tang,M. and Cao,Y.
  TITLE     The circular RNA circSLC16A10 alleviates diabetic retinopathy by
            improving mitochondrial function via the miR-761-5p/MFN2 axis
  JOURNAL   Cell Signal 121, 111283 (2024)
   PUBMED   38960059
  REMARK    GeneRIF: The circular RNA circSLC16A10 alleviates diabetic
            retinopathy by improving mitochondrial function via the
            miR-761-5p/MFN2 axis.
REFERENCE   4  (residues 1 to 757)
  AUTHORS   Kam,M.K., Jung,S.M., Lee,G.E., Lee,S.W., Lee,H.J., Park,Y.H. and
            Lee,D.S.
  TITLE     Mitofusin 1 and 2 overexpression reduces AbetaO-mediated ER stress
            and apoptosis in N2a APPswe cells
  JOURNAL   Cell Mol Biol (Noisy-le-grand) 70 (7), 8-14 (2024)
   PUBMED   39097901
  REMARK    GeneRIF: Mitofusin 1 and 2 overexpression reduces AbetaO-mediated
            ER stress and apoptosis in N2a APPswe cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 757)
  AUTHORS   Liu,D., Liao,P., Li,H., Tong,S., Wang,B., Lu,Y., Gao,Y., Huang,Y.,
            Zhou,H., Shi,L., Papadimitriou,J., Zong,Y., Yuan,J., Chen,P.,
            Chen,Z., Ding,P., Zheng,Y., Zhang,C., Zheng,M. and Gao,J.
  TITLE     Regulation of blood-brain barrier integrity by Dmp1-expressing
            astrocytes through mitochondrial transfer
  JOURNAL   Sci Adv 10 (26), eadk2913 (2024)
   PUBMED   38941455
REFERENCE   6  (residues 1 to 757)
  AUTHORS   Chen,K.H., Guo,X., Ma,D., Guo,Y., Li,Q., Yang,D., Li,P., Qiu,X.,
            Wen,S., Xiao,R.P. and Tang,J.
  TITLE     Dysregulation of HSG triggers vascular proliferative disorders
  JOURNAL   Nat Cell Biol 6 (9), 872-883 (2004)
   PUBMED   15322553
REFERENCE   7  (residues 1 to 757)
  AUTHORS   Koshiba,T., Detmer,S.A., Kaiser,J.T., Chen,H., McCaffery,J.M. and
            Chan,D.C.
  TITLE     Structural basis of mitochondrial tethering by mitofusin complexes
  JOURNAL   Science 305 (5685), 858-862 (2004)
   PUBMED   15297672
  REMARK    GeneRIF: results suggest that the heptad repeat region (HR2) of
            mfn1 functions as a mitochondrial tether before fusion
REFERENCE   8  (residues 1 to 757)
  AUTHORS   Bach,D., Pich,S., Soriano,F.X., Vega,N., Baumgartner,B., Oriola,J.,
            Daugaard,J.R., Lloberas,J., Camps,M., Zierath,J.R.,
            Rabasa-Lhoret,R., Wallberg-Henriksson,H., Laville,M., Palacin,M.,
            Vidal,H., Rivera,F., Brand,M. and Zorzano,A.
  TITLE     Mitofusin-2 determines mitochondrial network architecture and
            mitochondrial metabolism. A novel regulatory mechanism altered in
            obesity
  JOURNAL   J Biol Chem 278 (19), 17190-17197 (2003)
   PUBMED   12598526
REFERENCE   9  (residues 1 to 757)
  AUTHORS   Chen,H., Detmer,S.A., Ewald,A.J., Griffin,E.E., Fraser,S.E. and
            Chan,D.C.
  TITLE     Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion
            and are essential for embryonic development
  JOURNAL   J Cell Biol 160 (2), 189-200 (2003)
   PUBMED   12527753
REFERENCE   10 (residues 1 to 757)
  AUTHORS   Rojo,M., Legros,F., Chateau,D. and Lombes,A.
  TITLE     Membrane topology and mitochondrial targeting of mitofusins,
            ubiquitous mammalian homologs of the transmembrane GTPase Fzo
  JOURNAL   J Cell Sci 115 (Pt 8), 1663-1674 (2002)
   PUBMED   11950885
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY131209.1, AL607066.23 and AK042080.1.
            
            On Dec 29, 2006 this sequence version replaced NP_573464.1.
            
            Transcript Variant: This variant (2) differs in the 5' UTR compared
            to variant 1. All variants (1 through 7) encode the same protein.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC046503.1, AK042080.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164131, SAMN01164139
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 78.56 cM"
     Protein         1..757
                     /product="mitofusin-2"
                     /note="hypertension related protein 1; HSG protein;
                     transmembrane GTPase MFN2; mitochondrial assembly
                     regulatory factor"
                     /calculated_mol_wt=86057
     Region          30..94
                     /region_name="Part of a helix bundle domain, formed by
                     helices from N-terminal and C-terminal regions.
                     /evidence=ECO:0000250|UniProtKB:Q8IWA4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80U63.3)"
     Region          97..349
                     /region_name="DLP_2"
                     /note="Dynamin-like protein including dynamins,
                     mitofusins, and guanylate-binding proteins; cd09912"
                     /db_xref="CDD:206739"
     Region          103..110
                     /region_name="G1 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80U63.3)"
     Site            103..110
                     /site_type="other"
                     /note="G1 box"
                     /db_xref="CDD:206739"
     Site            order(105..111,202,258..259,261,305..307)
                     /site_type="other"
                     /note="GTP/Mg2+ binding site [chemical binding]"
                     /db_xref="CDD:206739"
     Site            111
                     /site_type="phosphorylation"
                     /note="Phosphothreonine, by PINK1.
                     /evidence=ECO:0000250|UniProtKB:O95140; propagated from
                     UniProtKB/Swiss-Prot (Q80U63.3)"
     Region          129..130
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80U63.3)"
     Site            130
                     /site_type="other"
                     /note="G2 box"
                     /db_xref="CDD:206739"
     Site            132..134
                     /site_type="other"
                     /note="Switch I region"
                     /db_xref="CDD:206739"
     Region          199..202
                     /region_name="G3 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80U63.3)"
     Site            199..202
                     /site_type="other"
                     /note="G3 box"
                     /db_xref="CDD:206739"
     Site            order(201..202,221..222)
                     /site_type="other"
                     /note="Switch II region"
                     /db_xref="CDD:206739"
     Region          258..261
                     /region_name="G4 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80U63.3)"
     Site            258..261
                     /site_type="other"
                     /note="G4 box"
                     /db_xref="CDD:206739"
     Region          288
                     /region_name="G5 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80U63.3)"
     Site            305..307
                     /site_type="other"
                     /note="G5 box"
                     /db_xref="CDD:206739"
     Region          359..385
                     /region_name="Part of a helix bundle domain, formed by
                     helices from N-terminal and C-terminal regions.
                     /evidence=ECO:0000250|UniProtKB:Q8IWA4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80U63.3)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80U63.3)"
     Region          596..754
                     /region_name="Fzo_mitofusin"
                     /note="fzo-like conserved region; pfam04799"
                     /db_xref="CDD:461432"
     Site            605..625
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80U63.3)"
     Site            627..647
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80U63.3)"
     Region          722..753
                     /region_name="Part of a helix bundle domain, formed by
                     helices from N-terminal and C-terminal regions.
                     /evidence=ECO:0000250|UniProtKB:Q8IWA4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80U63.3)"
     CDS             1..757
                     /gene="Mfn2"
                     /gene_synonym="D630023P19Rik; Fzo"
                     /coded_by="NM_133201.3:400..2673"
                     /db_xref="CCDS:CCDS38965.1"
                     /db_xref="GeneID:170731"
                     /db_xref="MGI:MGI:2442230"
ORIGIN      
        1 msllfsrcns ivtvkkdkrh maevnasplk hfvtakkkin gifeqlgayi qesasfledt
       61 hrnteldpvt teeqvldvkg ylskvrgise vlarrhmkva ffgrtsngks tvinamlwdk
      121 vlpsgightt ncflrvggtd gheafllteg seekksvktv nqlahalhqd eqlhagsmvs
      181 vmwpnskcpl lkddlvlmds pgidvtteld swidkfclda dvfvlvanse stlmqtekqf
      241 fhkvserlsr pnifilnnrw dasasepeym eevrrqhmer ctsflvdelg vvdraqagdr
      301 iffvsakevl sarvqkaqgm pegggalaeg fqvrmfefqn ferqfeecis qsavktkfeq
      361 htvrakqiae avrlimdslh iaaqeqrvyc lemreerqdr lrfidkqlel laqdyklrik
      421 qiteeverqv stamaeeirr lsvlvdeyqm dfhpspvvlk vyknelhrhi eeglgrnlsd
      481 rcstaiassl qtmqqdmidg lkpllpvsmr nqidmlvprq cfslsydlnc dklcadfqed
      541 iefhfslgwt mlvnrflgpk nsrrallgys dqvqrplplt panpsmpplp qssltqeelm
      601 vsmvtglasl tsrtsmgilv vggvvwkavg wrlialsfgl ygllyvyerl twttkakera
      661 fkrqfveyas eklqliisyt gsncshqvqq elsgtfahlc qqvditrdnl eqeiaamnkk
      721 vealdslqsr akllrnkagw ldselnmfth qylqpsr
//
