LOCUS       NP_001012087             692 aa            linear   ROD 03-APR-2024
DEFINITION  E3 ubiquitin-protein ligase MARCHF7 [Rattus norvegicus].
ACCESSION   NP_001012087 XP_229946
VERSION     NP_001012087.1
DBSOURCE    REFSEQ: accession NM_001012087.1
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 692)
  AUTHORS   Zhao,K., Yang,Y., Zhang,G., Wang,C., Wang,D., Wu,M. and Mei,Y.
  TITLE     Regulation of the Mdm2-p53 pathway by the ubiquitin E3 ligase
            MARCH7
  JOURNAL   EMBO Rep 19 (2), 305-319 (2018)
   PUBMED   29295817
REFERENCE   2  (residues 1 to 692)
  AUTHORS   Flach,K., Ramminger,E., Hilbrich,I., Arsalan-Werner,A.,
            Albrecht,F., Herrmann,L., Goedert,M., Arendt,T. and Holzer,M.
  TITLE     Axotrophin/MARCH7 acts as an E3 ubiquitin ligase and ubiquitinates
            tau protein in vitro impairing microtubule binding
  JOURNAL   Biochim Biophys Acta 1842 (9), 1527-1538 (2014)
   PUBMED   24905733
REFERENCE   3  (residues 1 to 692)
  AUTHORS   Zhao,B., Ito,K., Iyengar,P.V., Hirose,S. and Nakamura,N.
  TITLE     MARCH7 E3 ubiquitin ligase is highly expressed in developing
            spermatids of rats and its possible involvement in head and tail
            formation
  JOURNAL   Histochem Cell Biol 139 (3), 447-460 (2013)
   PUBMED   23104140
  REMARK    GeneRIF: The results suggest that MARCH7 is involved in
            spermiogenesis by regulating the structural and functional
            integrity of the head and tail of developing spermatids.
REFERENCE   4  (residues 1 to 692)
  AUTHORS   Nathan,J.A., Sengupta,S., Wood,S.A., Admon,A., Markson,G.,
            Sanderson,C. and Lehner,P.J.
  TITLE     The ubiquitin E3 ligase MARCH7 is differentially regulated by the
            deubiquitylating enzymes USP7 and USP9X
  JOURNAL   Traffic 9 (7), 1130-1145 (2008)
   PUBMED   18410486
REFERENCE   5  (residues 1 to 692)
  AUTHORS   Metcalfe,S.M., Muthukumarana,P.A., Thompson,H.L., Haendel,M.A. and
            Lyons,G.E.
  TITLE     Leukaemia inhibitory factor (LIF) is functionally linked to
            axotrophin and both LIF and axotrophin are linked to regulatory
            immune tolerance
  JOURNAL   FEBS Lett 579 (3), 609-614 (2005)
   PUBMED   15670816
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC083842.1.
            
            On Feb 11, 2005 this sequence version replaced XP_229946.2.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC083842.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132272, SAMD00132280
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..692
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q21"
     Protein         1..692
                     /product="E3 ubiquitin-protein ligase MARCHF7"
                     /EC_number="2.3.2.27"
                     /note="E3 ubiquitin-protein ligase MARCH7; MARCH-VII;
                     RING-type E3 ubiquitin transferase MARCHF7;
                     membrane-associated RING-CH protein VII;
                     membrane-associated RING finger protein 7; RING-type E3
                     ubiquitin transferase MARCH7; axotrophin;
                     membrane-associated ring finger (C3HC4) 7, E3 ubiquitin
                     protein ligase"
                     /calculated_mol_wt=76221
     Region          1..165
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI50.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:Q9H992; propagated from
                     UniProtKB/Swiss-Prot (Q5XI50.1)"
     Region          201..280
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI50.1)"
     Region          296..343
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI50.1)"
     Site            318
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H992; propagated from
                     UniProtKB/Swiss-Prot (Q5XI50.1)"
     Region          360..425
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI50.1)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H992; propagated from
                     UniProtKB/Swiss-Prot (Q5XI50.1)"
     Region          440..474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI50.1)"
     Region          512..532
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q5XI50.1)"
     Region          550..611
                     /region_name="RING_CH-C4HC3_MARCH7"
                     /note="RING-CH finger, H2 subclass (C4HC3-type), found in
                     membrane-associated RING-CH7 (MARCH7); cd16812"
                     /db_xref="CDD:438461"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q9H992; propagated from
                     UniProtKB/Swiss-Prot (Q5XI50.1)"
     Site            688
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9H992; propagated from
                     UniProtKB/Swiss-Prot (Q5XI50.1)"
     CDS             1..692
                     /gene="Marchf7"
                     /gene_synonym="Axot; March7"
                     /coded_by="NM_001012087.1:190..2268"
                     /db_xref="GeneID:311059"
                     /db_xref="RGD:1308993"
ORIGIN      
        1 meskpsripr risvqpsgsl sarmvsgnrg tslndsyhsr dssfrldsey qsasasasas
       61 pyqstwyses eitqgarsrs qnqqrdhdsk rpklsctnct stsagrnigs glntlsdssw
      121 rpgqvprsss mvlgsfgtdl mrerrdlerr rdssisslmd yshrsgdfta payvqervps
      181 sysqgarpke naantlqlns stnhqlpseh qtvpssrdss rssfrshfsp rqsesfrnss
      241 hpafsylssr netptissse ragssqrpfq essdnegrrt trrllsrias smsstffsrr
      301 ssqdslntrs lssenyispr tltsqsrnng asssevndgr aseasqgfrf lrrrwglssl
      361 sqnhssepda enfnqesegr ntgpwlsssl rnrctplfsr rrregrdess rispsdvppr
      421 shlfrresne vvhleaqgds lgaaasrpqa sgasgnasas gstpdlpqgg rntgiagilp
      481 gslfrfavpp algsnltdnv titvdiipsg wssadgksek aksapsrdpe klqkikesll
      541 ledsdeeeeg dlcricqmaa asssnlliep ckctgslqyv hqecmkkwlq akinsgssle
      601 avttcelcke klqlnledfd ihelhrahan eqaeyefiss glylvvllhl ceqsfsdmmg
      661 ntiepstrvr finlartlqa hmedletsed ef
//
