LOCUS       NP_001269734             704 aa            linear   PRI 05-DEC-2024
DEFINITION  E3 ubiquitin-protein ligase MARCHF7 isoform a [Homo sapiens].
ACCESSION   NP_001269734
VERSION     NP_001269734.1
DBSOURCE    REFSEQ: accession NM_001282805.2
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 704)
  AUTHORS   Shi,X. and Zhang,X.
  TITLE     Control of ATG14 solubility and autophagy by
            MARCHF7/MARCH7-mediated ubiquitination
  JOURNAL   Autophagy 20 (3), 699-700 (2024)
   PUBMED   37915253
  REMARK    GeneRIF: Control of ATG14 solubility and autophagy by
            MARCHF7/MARCH7-mediated ubiquitination.
REFERENCE   2  (residues 1 to 704)
  AUTHORS   Singh,S., Bano,A., Saraya,A., Das,P. and Sharma,R.
  TITLE     Association of MARCH7 with tumor progression and T-cell
            infiltration in esophageal cancer
  JOURNAL   Med Oncol 40 (1), 67 (2022)
   PUBMED   36583798
  REMARK    GeneRIF: Association of MARCH7 with tumor progression and T-cell
            infiltration in esophageal cancer.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 704)
  AUTHORS   Cho,N.H., Cheveralls,K.C., Brunner,A.D., Kim,K., Michaelis,A.C.,
            Raghavan,P., Kobayashi,H., Savy,L., Li,J.Y., Canaj,H., Kim,J.Y.S.,
            Stewart,E.M., Gnann,C., McCarthy,F., Cabrera,J.P., Brunetti,R.M.,
            Chhun,B.B., Dingle,G., Hein,M.Y., Huang,B., Mehta,S.B.,
            Weissman,J.S., Gomez-Sjoberg,R., Itzhak,D.N., Royer,L.A., Mann,M.
            and Leonetti,M.D.
  TITLE     OpenCell: Endogenous tagging for the cartography of human cellular
            organization
  JOURNAL   Science 375 (6585), eabi6983 (2022)
   PUBMED   35271311
REFERENCE   4  (residues 1 to 704)
  AUTHORS   Mahajan,S., Sharma,G.K., Bora,K. and Pattnaik,B.
  TITLE     Identification of novel interactions between host and
            non-structural protein 2C of foot-and-mouth disease virus
  JOURNAL   J Gen Virol 102 (3) (2021)
   PUBMED   33729124
  REMARK    GeneRIF: Identification of novel interactions between host and
            non-structural protein 2C of foot-and-mouth disease virus.
REFERENCE   5  (residues 1 to 704)
  AUTHORS   Luck,K., Kim,D.K., Lambourne,L., Spirohn,K., Begg,B.E., Bian,W.,
            Brignall,R., Cafarelli,T., Campos-Laborie,F.J., Charloteaux,B.,
            Choi,D., Cote,A.G., Daley,M., Deimling,S., Desbuleux,A., Dricot,A.,
            Gebbia,M., Hardy,M.F., Kishore,N., Knapp,J.J., Kovacs,I.A.,
            Lemmens,I., Mee,M.W., Mellor,J.C., Pollis,C., Pons,C.,
            Richardson,A.D., Schlabach,S., Teeking,B., Yadav,A., Babor,M.,
            Balcha,D., Basha,O., Bowman-Colin,C., Chin,S.F., Choi,S.G.,
            Colabella,C., Coppin,G., D'Amata,C., De Ridder,D., De Rouck,S.,
            Duran-Frigola,M., Ennajdaoui,H., Goebels,F., Goehring,L., Gopal,A.,
            Haddad,G., Hatchi,E., Helmy,M., Jacob,Y., Kassa,Y., Landini,S.,
            Li,R., van Lieshout,N., MacWilliams,A., Markey,D., Paulson,J.N.,
            Rangarajan,S., Rasla,J., Rayhan,A., Rolland,T., San-Miguel,A.,
            Shen,Y., Sheykhkarimli,D., Sheynkman,G.M., Simonovsky,E., Tasan,M.,
            Tejeda,A., Tropepe,V., Twizere,J.C., Wang,Y., Weatheritt,R.J.,
            Weile,J., Xia,Y., Yang,X., Yeger-Lotem,E., Zhong,Q., Aloy,P.,
            Bader,G.D., De Las Rivas,J., Gaudet,S., Hao,T., Rak,J.,
            Tavernier,J., Hill,D.E., Vidal,M., Roth,F.P. and Calderwood,M.A.
  TITLE     A reference map of the human binary protein interactome
  JOURNAL   Nature 580 (7803), 402-408 (2020)
   PUBMED   32296183
REFERENCE   6  (residues 1 to 704)
  AUTHORS   Muthukumarana,P.A., Lyons,G.E., Miura,Y., Thompson,L.H., Watson,T.,
            Green,C.J., Shurey,S., Hess,A.D., Rosengard,B.R. and Metcalfe,S.M.
  TITLE     Evidence for functional inter-relationships between FOXP3,
            leukaemia inhibitory factor, and axotrophin/MARCH-7 in
            transplantation tolerance
  JOURNAL   Int Immunopharmacol 6 (13-14), 1993-2001 (2006)
   PUBMED   17161353
  REMARK    GeneRIF: Data suggest that clinical auto-graft versus host disease
            inversely correlates with axotrophin transcript expression.
REFERENCE   7  (residues 1 to 704)
  AUTHORS   Flierman,D., Coleman,C.S., Pickart,C.M., Rapoport,T.A. and Chau,V.
  TITLE     E2-25K mediates US11-triggered retro-translocation of MHC class I
            heavy chains in a permeabilized cell system
  JOURNAL   Proc Natl Acad Sci U S A 103 (31), 11589-11594 (2006)
   PUBMED   16868077
REFERENCE   8  (residues 1 to 704)
  AUTHORS   Lim,J., Hao,T., Shaw,C., Patel,A.J., Szabo,G., Rual,J.F.,
            Fisk,C.J., Li,N., Smolyar,A., Hill,D.E., Barabasi,A.L., Vidal,M.
            and Zoghbi,H.Y.
  TITLE     A protein-protein interaction network for human inherited ataxias
            and disorders of Purkinje cell degeneration
  JOURNAL   Cell 125 (4), 801-814 (2006)
   PUBMED   16713569
REFERENCE   9  (residues 1 to 704)
  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
REFERENCE   10 (residues 1 to 704)
  AUTHORS   Bartee,E., Mansouri,M., Hovey Nerenberg,B.T., Gouveia,K. and
            Fruh,K.
  TITLE     Downregulation of major histocompatibility complex class I by human
            ubiquitin ligases related to viral immune evasion proteins
  JOURNAL   J Virol 78 (3), 1109-1120 (2004)
   PUBMED   14722266
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK292836.1, AK316382.1, BC003404.1, AI863394.1 and AC009961.11.
            
            Summary: MARCH7 is a member of the MARCH family of membrane-bound
            E3 ubiquitin ligases (EC 6.3.2.19). MARCH proteins add ubiquitin
            (see MIM 191339) to target lysines in substrate proteins, thereby
            signaling their vesicular transport between membrane compartments
            (Bartee et al., 2004 [PubMed 14722266]).[supplied by OMIM, Mar
            2010].
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (a). Variants 1, 2, and 5-13 all encode the same isoform (a).
            
            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 :: AK292836.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000409175.6/ ENSP00000386830.1
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..704
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2q24.2"
     Protein         1..704
                     /product="E3 ubiquitin-protein ligase MARCHF7 isoform a"
                     /EC_number="2.3.2.27"
                     /note="axotrophin; membrane-associated RING-CH protein
                     VII; E3 ubiquitin-protein ligase MARCH7; RING finger
                     protein 177; membrane associated ring finger 7;
                     membrane-associated RING finger protein 7;
                     membrane-associated ring finger (C3HC4) 7, E3 ubiquitin
                     protein ligase; RING-type E3 ubiquitin transferase MARCH7;
                     RING-type E3 ubiquitin transferase MARCHF7; E3
                     ubiquitin-protein ligase MARCHF7"
                     /calculated_mol_wt=77920
     Region          1..126
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H992.1)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22814378; propagated from
                     UniProtKB/Swiss-Prot (Q9H992.1)"
     Region          157..279
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H992.1)"
     Region          294..313
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H992.1)"
     Site            317
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H992.1)"
     Region          319..343
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H992.1)"
     Region          361..425
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H992.1)"
     Site            389
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9H992.1)"
     Region          444..473
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H992.1)"
     Region          552..610
                     /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"
     Region          683..704
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9H992.1)"
     Site            686
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H992.1)"
     Site            687
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H992.1)"
     Site            691
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648; propagated from
                     UniProtKB/Swiss-Prot (Q9H992.1)"
     CDS             1..704
                     /gene="MARCHF7"
                     /gene_synonym="AXO; AXOT; MARCH-VII; MARCH7; RNF177"
                     /coded_by="NM_001282805.2:244..2358"
                     /note="isoform a is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS2210.1"
                     /db_xref="GeneID:64844"
                     /db_xref="HGNC:HGNC:17393"
                     /db_xref="MIM:613334"
ORIGIN      
        1 meskpsripr risvqpsssl sarmmsgsrg sslndtyhsr dssfrldsey qstsasasas
       61 pfqsawyses eitqgarsrs qnqqrdhdsk rpklsctnct tsagrnvgng lntlsdsswr
      121 hsqvprsssm vlgsfgtdlm rerrdlerrt dssisnlmdy shrsgdftts syvqdrvpsy
      181 sqgarpkens mstlqlntss tnhqlpsehq tilssrdsrn slrsnfssre sessrsntqp
      241 gfsysssrde apiisnserv vssqrpfqes sdnegrrttr rllsriassm sstffsrrss
      301 qdslntrsln sensyvspri ltasqsrsnv psasevpdnr aseasqgfrf lrrrwglssl
      361 shnhssesds enfnqesegr ntgpwlsssl rnrctplfsr rrregrdess riptsdtssr
      421 shifrresne vvhleaqndp lgaaanrpqa saasssattg gstsdsaqgg rntgisgilp
      481 gslfrfavpp algsnltdnv mitvdiipsg wnsadgksdk tksapsrdpe rlqkikesll
      541 ledseeeegd lcricqmaaa sssnlliepc kctgslqyvh qdcmkkwlqa kinsgsslea
      601 vttcelckek lelnledfdi helhrahane qaeyefissg lylvvllhlc eqsfsdmmgn
      661 tnepstrvrf inlartlqah medletsedd seedgdhnrt fdia
//
