LOCUS       NP_570964                757 aa            linear   ROD 14-FEB-2025
DEFINITION  mitofusin-2 [Rattus norvegicus].
ACCESSION   NP_570964
VERSION     NP_570964.4
DBSOURCE    REFSEQ: accession NM_130894.5
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 757)
  AUTHORS   Wang,Y., Han,D., Chai,L., Qiu,Y., Liu,J., Li,D., Zhang,Q., Shen,N.,
            Chen,Y., Chen,H., Zhang,J., Wang,Q., Wang,J., Li,S., Xie,X. and
            Li,M.
  TITLE     MFN2-dependent mitochondrial dysfunction contributes to
            Relm-beta-induced pulmonary arterial hypertension via
            USP18/Twist1/miR-214 pathway
  JOURNAL   Eur J Pharmacol 980, 176828 (2024)
   PUBMED   39094924
  REMARK    GeneRIF: MFN2-dependent mitochondrial dysfunction contributes to
            Relm-beta-induced pulmonary arterial hypertension via
            USP18/Twist1/miR-214 pathway.
REFERENCE   2  (residues 1 to 757)
  AUTHORS   Deng,X., Xu,H., Pan,C., Hao,X., Liu,J., Shang,X., Chi,R., Hou,W.
            and Xu,T.
  TITLE     Moderate mechanical strain and exercise reduce inflammation and
            excessive autophagy in osteoarthritis by downregulating mitofusin 2
  JOURNAL   Life Sci 332, 122020 (2023)
   PUBMED   37579836
  REMARK    GeneRIF: Moderate mechanical strain and exercise reduce
            inflammation and excessive autophagy in osteoarthritis by
            downregulating mitofusin 2.
REFERENCE   3  (residues 1 to 757)
  AUTHORS   Wang,S., Sang,X., Li,S., Yang,W., Wang,S., Chen,H. and Lu,C.
  TITLE     Increased Ca2 + transport across the mitochondria-associated
            membranes by Mfn2 inhibiting endoplasmic reticulum stress in
            ischemia/reperfusion kidney injury
  JOURNAL   Sci Rep 13 (1), 17257 (2023)
   PUBMED   37828353
  REMARK    GeneRIF: Increased Ca2 + transport across the
            mitochondria-associated membranes by Mfn2 inhibiting endoplasmic
            reticulum stress in ischemia/reperfusion kidney injury.
            Erratum:[Sci Rep. 2024 Jan 30;14(1):2478. doi:
            10.1038/s41598-024-52771-4.. PMID: 38291111]
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 757)
  AUTHORS   Zhang,R., Yang,A., Zhang,L., He,L., Gu,X., Yu,C., Lu,Z., Wang,C.,
            Zhou,F., Li,F., Ji,L., Xing,J. and Guo,H.
  TITLE     MFN2 deficiency promotes cardiac response to hypobaric hypoxia by
            reprogramming cardiomyocyte metabolism
  JOURNAL   Acta Physiol (Oxf) 239 (1), e14018 (2023)
   PUBMED   37401731
  REMARK    GeneRIF: MFN2 deficiency promotes cardiac response to hypobaric
            hypoxia by reprogramming cardiomyocyte metabolism.
REFERENCE   5  (residues 1 to 757)
  AUTHORS   Ghosal,S., Gebara,E., Ramos-Fernandez,E., Chioino,A., Grosse,J.,
            Guillot de Suduiraut,I., Zanoletti,O., Schneider,B., Zorzano,A.,
            Astori,S. and Sandi,C.
  TITLE     Mitofusin-2 in nucleus accumbens D2-MSNs regulates social dominance
            and neuronal function
  JOURNAL   Cell Rep 42 (7), 112776 (2023)
   PUBMED   37440411
  REMARK    GeneRIF: Mitofusin-2 in nucleus accumbens D2-MSNs regulates social
            dominance and neuronal function.
REFERENCE   6  (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   7  (residues 1 to 757)
  AUTHORS   Ishihara,N., Jofuku,A., Eura,Y. and Mihara,K.
  TITLE     Regulation of mitochondrial morphology by membrane potential, and
            DRP1-dependent division and FZO1-dependent fusion reaction in
            mammalian cells
  JOURNAL   Biochem Biophys Res Commun 301 (4), 891-898 (2003)
   PUBMED   12589796
REFERENCE   8  (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   9  (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
REFERENCE   10 (residues 1 to 757)
  AUTHORS   Santel,A. and Fuller,M.T.
  TITLE     Control of mitochondrial morphology by a human mitofusin
  JOURNAL   J Cell Sci 114 (Pt 5), 867-874 (2001)
   PUBMED   11181170
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000005.1.
            
            On Jun 10, 2007 this sequence version replaced NP_570964.3.
            
            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 :: U41803.2, SRR26643299.25476.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA5760383,
                                           SAMEA5760389 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..757
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="5"
                     /map="5q36"
     Protein         1..757
                     /product="mitofusin-2"
                     /note="transmembrane GTPase MFN2; hypertension-related
                     protein; mitochondrial transmembrane GTPase FZO1A;
                     mitofusin-2-like"
                     /calculated_mol_wt=86050
     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 (Q8R500.1)"
     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 (Q8R500.1)"
     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 (Q8R500.1)"
     Region          129..130
                     /region_name="G2 motif.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01055"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R500.1)"
     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 (Q8R500.1)"
     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 (Q8R500.1)"
     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 (Q8R500.1)"
     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 (Q8R500.1)"
     Site            442
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by PINK1.
                     /evidence=ECO:0000250|UniProtKB:O95140; propagated from
                     UniProtKB/Swiss-Prot (Q8R500.1)"
     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 (Q8R500.1)"
     Site            627..647
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8R500.1)"
     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 (Q8R500.1)"
     CDS             1..757
                     /gene="Mfn2"
                     /gene_synonym="HSG"
                     /coded_by="NM_130894.5:192..2465"
                     /db_xref="GeneID:64476"
                     /db_xref="RGD:628843"
ORIGIN      
        1 msllfsrcns ivtvkkdkrh maevnasplk hfvtakkkin gifeqlgayi qesagfledt
       61 hrnteldpvt teeqvldvkg ylskvrgise vlarrhmkva ffgrtsngks tvinamlwdk
      121 vlpsgightt ncflrvggtd gheafllteg seekksvktv nqlahalhqd eqlhagslvs
      181 vmwpnskcpl lkddlvlmds pgidvtteld swidkfclda dvfvlvanse stlmqtekqf
      241 fhkvserlsr pnifilnnrw dasasepeym eevrrqhmer ctsflvdelg vvdraqagdr
      301 iffvsakevl sarvqkaqgm pegggalaeg fqvrmfefqn ferrfeecis qsavktkfeq
      361 htvrakqiae avrlimdslh iaaqeqrvyc lemreerqdr lrfidkqlel laqdyklrik
      421 qmteeverqv stamaeeirr lsvlvdeyqm dfhpspvvlk vyknelhrhi eeglgrnmsd
      481 rcstaiassl qtmqqdmidg lkpllpvsvr nqidmlvprq cfslsydlnc dklcadfqed
      541 iefhfslgwt mlvnrflgpk nsrrallgyn dqvqrplplt panpsmpplp qgsltqeelm
      601 vsmvtglasl tsrtsmgilv vggvvwkavg wrlialsfgl ygllyvyerl twttrakera
      661 fkrqfveyas eklqliisyt gsncshqvqq elsgtfahlc qqvditrdnl eqeiaamnkk
      721 vealdslqsk akllrnkagw ldselnmfih qylqpsr
//
