Reviewed, UniProtKB/Swiss-Prot O75027 (ABCB7_HUMAN)

Names and origin

Protein names

Recommended name:
    ATP-binding cassette sub-family B member 7, mitochondrial
Alternative name(s):
    ATP-binding cassette transporter 7
      Short name=ABC transporter 7 protein

Gene names

Name:	ABCB7
Synonyms:	ABC7

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	752 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Could be involved in the transport of heme from the mitochondria to the cytosol. Plays a central role in the maturation of cytosolic iron-sulfur (Fe/S) cluster-containing proteins.
Subunit structure	Homodimer or heterodimer Potential.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein Potential.
Involvement in disease	Defects in ABCB7 are the cause of X-linked sideroblastic anemia with ataxia (ASAT) [MIM:301310]. ASAT is a recessive disorder characterized by an infantile to early childhood onset of nonprogressive cerebellar ataxia and mild anemia with hypochromia and microcytosis. Ref.2 Ref.3 Ref.11
Sequence similarities	Belongs to the ABC transporter superfamily. ABCB family. Heavy Metal importer (TC 3.A.1.210) subfamily. [View classification] Contains 1 ABC transmembrane type-1 domain. Contains 1 ABC transporter domain.

Ontologies

Keywords
Biological process	Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Transit peptide Transmembrane
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	transmembrane transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial inner membrane Ref.2 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Ref.1 Traceable author statement. Source: ProtInc ATPase activity, coupled to transmembrane movement of substances Ref.1 Traceable author statement. Source: ProtInc heme transporter activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75027-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O75027-2)

The sequence of this isoform differs from the canonical sequence as follows:
     56-56: Q → QQ

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 752		ATP-binding cassette sub-family B member 7, mitochondrial		PRO_0000000249
Regions
	Transmembrane	141 – 161	21	Potential
	Transmembrane	186 – 206	21	Potential
	Transmembrane	260 – 280	21	Potential
	Transmembrane	291 – 311	21	Potential
	Transmembrane	383 – 403	21	Potential
	Transmembrane	410 – 430	21	Potential
	Domain	140 – 436	297	ABC transmembrane type-1
	Domain	472 – 706	235	ABC transporter
	Nucleotide binding	505 – 512	8	ATP Potential
Amino acid modifications
	Modified residue	216	1	N6-acetyllysine Ref.10
	Modified residue	251	1	N6-acetyllysine Ref.10
Natural variations
	Alternative sequence	56	1	Q → QQ in isoform 2.		VSP_014635
	Natural variant	315	1	R → G		VAR_022872
	Natural variant	346	1	F → I		VAR_022873
	Natural variant	400	1	I → M in ASAT. Ref.2		VAR_009156
	Natural variant	411	1	V → L in ASAT. Ref.11		VAR_022874
	Natural variant	433	1	E → K in ASAT; impaired maturation of cytosolic Fe/S proteins. Ref.3		VAR_012640
	Natural variant	580	1	A → V: dbSNP rs1340989.		VAR_055471
	Natural variant	581	1	V → A: dbSNP rs1340989.		VAR_037972
Experimental info
	Sequence conflict	141	1	A → P in AAC39865. Ref.4
	Sequence conflict	258	1	R → K in BAA28861. Ref.1
	Sequence conflict	271 – 276	6	LLPIMF → PLPNHV in AAC39865. Ref.4
	Sequence conflict	280	1	L → LL in AAC39865. Ref.4
	Sequence conflict	290	1	G → C in AAC39865. Ref.4
	Sequence conflict	293 – 297	5	FALVT → LLGN in AAC39865. Ref.4
	Sequence conflict	320 – 324	5	IEMNK → LEIDQ in AAC39865. Ref.4
	Sequence conflict	542	1	E → V in AAD47141. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: B1FFA57ABD24FB90	FASTA	752	82,641
	10 20 30 40 50 60 MALLAMHSWR WAAAAAAFEK RRHSAILIRP LVSVSGSGPQ WRPHQLGALG TARAYQIPES 70 80 90 100 110 120 LKSITWQRLG KGNSGQFLDA AKALQVWPLI EKRTCWHGHA GGGLHTDPKE GLKDVDTRKI 130 140 150 160 170 180 IKAMLSYVWP KDRPDLRARV AISLGFLGGA KAMNIVVPFM FKYAVDSLNQ MSGNMLNLSD 190 200 210 220 230 240 APNTVATMAT AVLIGYGVSR AGAAFFNEVR NAVFGKVAQN SIRRIAKNVF LHLHNLDLGF 250 260 270 280 290 300 HLSRQTGALS KAIDRGTRGI SFVLSALVFN LLPIMFEVML VSGVLYYKCG AQFALVTLGT 310 320 330 340 350 360 LGTYTAFTVA VTRWRTRFRI EMNKADNDAG NAAIDSLLNY ETVKYFNNER YEAQRYDGFL 370 380 390 400 410 420 KTYETASLKS TSTLAMLNFG QSAIFSVGLT AIMVLASQGI VAGTLTVGDL VMVNGLLFQL 430 440 450 460 470 480 SLPLNFLGTV YRETRQALID MNTLFTLLKV DTQIKDKVMA SPLQITPQTA TVAFDNVHFE 490 500 510 520 530 540 YIEGQKVLSG ISFEVPAGKK VAIVGGSGSG KSTIVRLLFR FYEPQKGSIY LAGQNIQDVS 550 560 570 580 590 600 LESLRRAVGV VPQDAVLFHN TIYYNLLYGN ISASPEEVYA VAKLAGLHDA ILRMPHGYDT 610 620 630 640 650 660 QVGERGLKLS GGEKQRVAIA RAILKDPPVI LYDEATSSLD SITEETILGA MKDVVKHRTS 670 680 690 700 710 720 IFIAHRLSTV VDADEIIVLD QGKVAERGTH HGLLANPHSI YSEMWHTQSS RVQNHDNPKW 730 740 750 EAKKENISKE EERKKLQEEI VNSVKGCGNC SC
	Isoform 2. Checksum: 9B96042C55C3C62F	FASTA	753	82,769
	10 20 30 40 50 60 MALLAMHSWR WAAAAAAFEK RRHSAILIRP LVSVSGSGPQ WRPHQLGALG TARAYQQIPE 70 80 90 100 110 120 SLKSITWQRL GKGNSGQFLD AAKALQVWPL IEKRTCWHGH AGGGLHTDPK EGLKDVDTRK 130 140 150 160 170 180 IIKAMLSYVW PKDRPDLRAR VAISLGFLGG AKAMNIVVPF MFKYAVDSLN QMSGNMLNLS 190 200 210 220 230 240 DAPNTVATMA TAVLIGYGVS RAGAAFFNEV RNAVFGKVAQ NSIRRIAKNV FLHLHNLDLG 250 260 270 280 290 300 FHLSRQTGAL SKAIDRGTRG ISFVLSALVF NLLPIMFEVM LVSGVLYYKC GAQFALVTLG 310 320 330 340 350 360 TLGTYTAFTV AVTRWRTRFR IEMNKADNDA GNAAIDSLLN YETVKYFNNE RYEAQRYDGF 370 380 390 400 410 420 LKTYETASLK STSTLAMLNF GQSAIFSVGL TAIMVLASQG IVAGTLTVGD LVMVNGLLFQ 430 440 450 460 470 480 LSLPLNFLGT VYRETRQALI DMNTLFTLLK VDTQIKDKVM ASPLQITPQT ATVAFDNVHF 490 500 510 520 530 540 EYIEGQKVLS GISFEVPAGK KVAIVGGSGS GKSTIVRLLF RFYEPQKGSI YLAGQNIQDV 550 560 570 580 590 600 SLESLRRAVG VVPQDAVLFH NTIYYNLLYG NISASPEEVY AVAKLAGLHD AILRMPHGYD 610 620 630 640 650 660 TQVGERGLKL SGGEKQRVAI ARAILKDPPV ILYDEATSSL DSITEETILG AMKDVVKHRT 670 680 690 700 710 720 SIFIAHRLST VVDADEIIVL DQGKVAERGT HHGLLANPHS IYSEMWHTQS SRVQNHDNPK 730 740 750 WEAKKENISK EEERKKLQEE IVNSVKGCGN CSC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and chromosomal mapping of a novel ABC transporter gene (hABC7), a candidate for X-linked sideroblastic anemia with spinocerebellar ataxia." Shimada Y., Okuno S., Kawai A., Shinomiya H., Saito A., Suzuki M., Omori Y., Nishino N., Kanemoto N., Fujiwara T., Horie M., Takahashi E. J. Hum. Genet. 43:115-122(1998) [PubMed: 9621516] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLY-315 AND ILE-346. Tissue: Placenta.
[2]	"Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A)." Allikmets R., Raskind W.H., Hutchinson A., Schueck N.D., Dean M., Koeller D.M. Hum. Mol. Genet. 8:743-749(1999) [PubMed: 10196363] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASAT MET-400.
[3]	"Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation." Bekri S., Kispal G., Lange H., Fitzsimons E., Tolmie J., Lill R., Bishop D.F. Blood 96:3256-3264(2000) [PubMed: 11050011] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASAT LYS-433.
[4]	"Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning." Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z. Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed: 9653160] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Umbilical cord blood.
[5]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[6]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Muscle.
[8]	"Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p." Csere P., Lill R., Kispal G. FEBS Lett. 441:266-270(1998) [PubMed: 9883897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-752 (ISOFORM 1).
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216 AND LYS-251, MASS SPECTROMETRY.
[11]	"X-linked cerebellar ataxia and sideroblastic anaemia associated with a missense mutation in the ABC7 gene predicting V411L." Maguire A., Hellier K., Hammans S., May A. Br. J. Haematol. 115:910-917(2001) [PubMed: 11843825] [Abstract] Cited for: VARIANT ASAT LEU-411, VARIANTS GLY-315 AND ILE-346.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB005289 mRNA. Translation: BAA28861.1. AF133659 mRNA. Translation: AAD33045.1. AF241887 , AF241872, AF241873, AF241874, AF241875, AF241876, AF241877, AF241878, AF241879, AF241880, AF241881, AF241882, AF241883, AF241884, AF241885, AF241886 Genomic DNA. Translation: AAK20173.1. AF038950 mRNA. Translation: AAC39865.1. BT009918 mRNA. Translation: AAP88920.1. AL360179, AL359545 Genomic DNA. Translation: CAH70564.1. AL360179, AL359545 Genomic DNA. Translation: CAH70565.1. AL359545, AL360179 Genomic DNA. Translation: CAI41573.1. AL359545, AL360179 Genomic DNA. Translation: CAI41574.1. BC006323 mRNA. Translation: AAH06323.1. AF078777 mRNA. Translation: AAD47141.1.
IPI	IPI00306748. IPI00556553.
RefSeq	NP_004290.2.
UniGene	Hs.370480
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O75027.
Protein family/group databases
TCDB	3.A.1.210.4. ATP-binding cassette (ABC) superfamily.
PTM databases
PhosphoSite	O75027.
Proteomic databases
PRIDE	O75027.
Genome annotation databases
Ensembl	ENST00000373394; ENSP00000362492; ENSG00000131269; Homo sapiens. [Genome view]
GeneID	22.
KEGG	hsa:22.
UCSC	uc004ebz.1. human. uc004eca.1. human.
Organism-specific databases
CTD	22.
GeneCards	GC0XM074189.
H-InvDB	HIX0016880. HIX0028475.
HGNC	HGNC:48. ABCB7.
MIM	300135. gene. 301310. phenotype.
Orphanet	2802. Anemia, sideroblastic, X-linked - ataxia.
PharmGKB	PA24389.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	O75027.
OMA	NEENIFA
Gene expression databases
ArrayExpress	O75027.
Bgee	O75027.
CleanEx	HS_ABCB7.
Genevestigator	O75027.
GermOnline	ENSG00000131269. Homo sapiens.
Family and domain databases
InterPro	IPR011527. ABC_TM_1. IPR001140. ABC_TM_transpt. IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. IPR017940. ABC_transporter_type1. IPR003593. ATPase_AAA+_core. [Graphical view]
Pfam	PF00664. ABC_membrane. 1 hit. PF00005. ABC_tran. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
PROSITE	PS50929. ABC_TM1F. 1 hit. PS00211. ABC_TRANSPORTER_1. 1 hit. PS50893. ABC_TRANSPORTER_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	65.
SOURCE	Search...

Entry information

Entry name

ABCB7_HUMAN

Accession

Primary (citable) accession number: O75027
Secondary accession number(s): O75345 , Q5VWY7, Q5VWY8, Q9BRE1, Q9UND1, Q9UP01

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 1, 2000
Last modified:	November 24, 2009
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.