LOCUS       NP_001258625             752 aa            linear   PRI 27-APR-2025
DEFINITION  iron-sulfur clusters transporter ABCB7, mitochondrial isoform 2
            [Homo sapiens].
ACCESSION   NP_001258625
VERSION     NP_001258625.1
DBSOURCE    REFSEQ: accession NM_001271696.3
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 752)
  AUTHORS   Feng,S., Jia,J., Lv,G. and Wang,Y.
  TITLE     Knockdown of ABCB7 inhibits esophageal cancer progression by
            inhibiting the TGF-beta/Smad signaling
  JOURNAL   Arch Biochem Biophys 742, 109620 (2023)
   PUBMED   37142077
  REMARK    GeneRIF: Knockdown of ABCB7 inhibits esophageal cancer progression
            by inhibiting the TGF-beta/Smad signaling.
REFERENCE   2  (residues 1 to 752)
  AUTHORS   Clough,C.A., Pangallo,J., Sarchi,M., Ilagan,J.O., North,K.,
            Bergantinos,R., Stolla,M.C., Naru,J., Nugent,P., Kim,E.,
            Stirewalt,D.L., Subramaniam,A.R., Abdel-Wahab,O., Abkowitz,J.L.,
            Bradley,R.K. and Doulatov,S.
  TITLE     Coordinated missplicing of TMEM14C and ABCB7 causes ring
            sideroblast formation in SF3B1-mutant myelodysplastic syndrome
  JOURNAL   Blood 139 (13), 2038-2049 (2022)
   PUBMED   34861039
  REMARK    GeneRIF: Coordinated missplicing of TMEM14C and ABCB7 causes ring
            sideroblast formation in SF3B1-mutant myelodysplastic syndrome.
REFERENCE   3  (residues 1 to 752)
  AUTHORS   Morgenstern,M., Peikert,C.D., Lubbert,P., Suppanz,I., Klemm,C.,
            Alka,O., Steiert,C., Naumenko,N., Schendzielorz,A., Melchionda,L.,
            Muhlhauser,W.W.D., Knapp,B., Busch,J.D., Stiller,S.B.,
            Dannenmaier,S., Lindau,C., Licheva,M., Eickhorst,C., Galbusera,R.,
            Zerbes,R.M., Ryan,M.T., Kraft,C., Kozjak-Pavlovic,V., Drepper,F.,
            Dennerlein,S., Oeljeklaus,S., Pfanner,N., Wiedemann,N. and
            Warscheid,B.
  TITLE     Quantitative high-confidence human mitochondrial proteome and its
            dynamics in cellular context
  JOURNAL   Cell Metab 33 (12), 2464-2483 (2021)
   PUBMED   34800366
REFERENCE   4  (residues 1 to 752)
  AUTHORS   Nie,Z., Yan,Q., Shen,Y. and Yang,X.
  TITLE     Expression, purification and microscopic characterization of human
            ATP-binding cassette sub-family B member 7 protein
  JOURNAL   Protein Expr Purif 183, 105860 (2021)
   PUBMED   33689857
  REMARK    GeneRIF: Expression, purification and microscopic characterization
            of human ATP-binding cassette sub-family B member 7 protein.
REFERENCE   5  (residues 1 to 752)
  AUTHORS   Pearson,S.A. and Cowan,J.A.
  TITLE     Evolution of the human mitochondrial ABCB7 [2Fe-2S](GS)4 cluster
            exporter and the molecular mechanism of an E433K disease-causing
            mutation
  JOURNAL   Arch Biochem Biophys 697, 108661 (2021)
   PUBMED   33157103
  REMARK    GeneRIF: Evolution of the human mitochondrial ABCB7 [2Fe-2S](GS)4
            cluster exporter and the molecular mechanism of an E433K
            disease-causing mutation.
REFERENCE   6  (residues 1 to 752)
  AUTHORS   Csere,P., Lill,R. and Kispal,G.
  TITLE     Identification of a human mitochondrial ABC transporter, the
            functional orthologue of yeast Atm1p
  JOURNAL   FEBS Lett 441 (2), 266-270 (1998)
   PUBMED   9883897
REFERENCE   7  (residues 1 to 752)
  AUTHORS   Shimada,Y., Okuno,S., Kawai,A., Shinomiya,H., Saito,A., Suzuki,M.,
            Omori,Y., Nishino,N., Kanemoto,N., Fujiwara,T., Horie,M. and
            Takahashi,E.
  TITLE     Cloning and chromosomal mapping of a novel ABC transporter gene
            (hABC7), a candidate for X-linked sideroblastic anemia with
            spinocerebellar ataxia
  JOURNAL   J Hum Genet 43 (2), 115-122 (1998)
   PUBMED   9621516
REFERENCE   8  (residues 1 to 752)
  AUTHORS   Savary,S., Allikmets,R., Denizot,F., Luciani,M.F., Mattei,M.G.,
            Dean,M. and Chimini,G.
  TITLE     Isolation and chromosomal mapping of a novel ATP-binding cassette
            transporter conserved in mouse and human
  JOURNAL   Genomics 41 (2), 275-278 (1997)
   PUBMED   9143506
REFERENCE   9  (residues 1 to 752)
  AUTHORS   Allikmets,R., Gerrard,B., Hutchinson,A. and Dean,M.
  TITLE     Characterization of the human ABC superfamily: isolation and
            mapping of 21 new genes using the expressed sequence tags database
  JOURNAL   Hum Mol Genet 5 (10), 1649-1655 (1996)
   PUBMED   8894702
REFERENCE   10 (residues 1 to 752)
  AUTHORS   Bekri,S., D'Hooghe,M. and Vermeersch,P.
  TITLE     X-Linked Sideroblastic Anemia and Ataxia - RETIRED CHAPTER, FOR
            HISTORICAL REFERENCE ONLY
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301496
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BP228998.1, AF133659.1,
            AA403157.1 and AL359545.12.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary: The membrane-associated protein encoded by this gene is a
            member of the superfamily of ATP-binding cassette (ABC)
            transporters. ABC proteins transport various molecules across
            extra- and intra-cellular membranes. ABC genes are divided into
            seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20,
            White). This protein is a member of the MDR/TAP subfamily. Members
            of the MDR/TAP subfamily are involved in multidrug resistance as
            well as antigen presentation. This gene encodes a half-transporter
            involved in the transport of heme from the mitochondria to the
            cytosol. With iron/sulfur cluster precursors as its substrates,
            this protein may play a role in metal homeostasis. Mutations in
            this gene have been associated with mitochondrial iron accumulation
            and isodicentric (X)(q13) and sideroblastic anemia. Alternatively
            spliced transcript variants encoding multiple isoforms have been
            observed for this gene. [provided by RefSeq, Nov 2012].
            
            Transcript Variant: This variant (2) uses an alternate in-frame
            splice site in the 5' coding region, compared to variant 1. This
            results in a shorter protein (isoform 2), compared to isoform 1.
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            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 :: SRR11853565.30546.1,
                                           SRR14038193.2082345.1 [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: inferred from homology
            MANE Ensembl match                 :: ENST00000373394.8/
                                                  ENSP00000362492.3
            RefSeq Select criteria             :: based on manual assertion,
                                                  conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..752
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xq13.3"
     Protein         1..752
                     /product="iron-sulfur clusters transporter ABCB7,
                     mitochondrial isoform 2"
                     /note="ATP-binding cassette sub-family B member 7,
                     mitochondrial; ABC transporter 7 protein; ATP-binding
                     cassette transporter 7; ATP-binding cassette, sub-family B
                     (MDR/TAP), member 7; iron-sulfur clusters transporter
                     ABCB7, mitochondrial"
                     /calculated_mol_wt=80115
     transit_peptide 1..22
                     /note="Mitochondrion. /evidence=ECO:0000255; propagated
                     from UniProtKB/Swiss-Prot (O75027.2)"
                     /calculated_mol_wt=2545
     mat_peptide     23..752
                     /product="Iron-sulfur clusters transporter ABCB7,
                     mitochondrial. /id=PRO_0000000249"
                     /note="propagated from UniProtKB/Swiss-Prot (O75027.2)"
                     /calculated_mol_wt=80115
     Region          125..711
                     /region_name="ATM1"
                     /note="ABC-type transport system involved in Fe-S cluster
                     assembly, permease and ATPase components
                     [Posttranslational modification, protein turnover,
                     chaperones]; COG5265"
                     /db_xref="CDD:444078"
     Site            141..161
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75027.2)"
     Site            186..206
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75027.2)"
     Site            216
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O75027.2)"
     Site            251
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (O75027.2)"
     Site            260..280
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75027.2)"
     Site            291..311
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75027.2)"
     Site            336
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q704E8; propagated from
                     UniProtKB/Swiss-Prot (O75027.2)"
     Site            340
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q704E8; propagated from
                     UniProtKB/Swiss-Prot (O75027.2)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q704E8; propagated from
                     UniProtKB/Swiss-Prot (O75027.2)"
     Site            383..403
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75027.2)"
     Site            410..430
                     /site_type="transmembrane region"
                     /note="propagated from UniProtKB/Swiss-Prot (O75027.2)"
     CDS             1..752
                     /gene="ABCB7"
                     /gene_synonym="ABC7; ASAT; Atm1p; EST140535"
                     /coded_by="NM_001271696.3:12..2270"
                     /note="isoform 2 is encoded by transcript variant 2"
                     /db_xref="CCDS:CCDS65291.1"
                     /db_xref="GeneID:22"
                     /db_xref="HGNC:HGNC:48"
                     /db_xref="MIM:300135"
ORIGIN      
        1 mallamhswr waaaaaafek rrhsailirp lvsvsgsgpq wrphqlgalg tarayqipes
       61 lksitwqrlg kgnsgqflda akalqvwpli ekrtcwhgha ggglhtdpke glkdvdtrki
      121 ikamlsyvwp kdrpdlrarv aislgflgga kamnivvpfm fkyavdslnq msgnmlnlsd
      181 apntvatmat avligygvsr agaaffnevr navfgkvaqn sirriaknvf lhlhnldlgf
      241 hlsrqtgals kaidrgtrgi sfvlsalvfn llpimfevml vsgvlyykcg aqfalvtlgt
      301 lgtytaftva vtrwrtrfri emnkadndag naaidsllny etvkyfnner yeaqrydgfl
      361 ktyetaslks tstlamlnfg qsaifsvglt aimvlasqgi vagtltvgdl vmvngllfql
      421 slplnflgtv yretrqalid mntlftllkv dtqikdkvma splqitpqta tvafdnvhfe
      481 yiegqkvlsg isfevpagkk vaivggsgsg kstivrllfr fyepqkgsiy lagqniqdvs
      541 leslrravgv vpqdavlfhn tiyynllygn isaspeevya vaklaglhda ilrmphgydt
      601 qvgerglkls ggekqrvaia railkdppvi lydeatssld siteetilga mkdvvkhrts
      661 ifiahrlstv vdadeiivld qgkvaergth hgllanphsi ysemwhtqss rvqnhdnpkw
      721 eakkeniske eerkklqeei vnsvkgcgnc sc
//
