Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P28288 (ABCD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-binding cassette sub-family D member 3
Alternative name(s):
70 kDa peroxisomal membrane protein
Short name=PMP70
Gene names
Name:ABCD3
Synonyms:PMP70, PXMP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length659 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable transporter. The nucleotide-binding fold acts as an ATP-binding subunit with ATPase activity. Ref.11

Subunit structure

Can form heterodimers with ABCD1/ALD and ABCD2/ALDR. Dimerization is necessary to form an active transporter. Interacts with PEX19. Ref.8 Ref.9 Ref.10

Subcellular location

Peroxisome membrane; Multi-pass membrane protein Ref.10.

Miscellaneous

Mutation in ABCD3 have been found in two individuals affected by Zellweger syndrome. However, the role of ABCD3 in the causation of Zellweger syndrome remains uncertain.

Sequence similarities

Belongs to the ABC transporter superfamily. ABCD family. Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily. [View classification]

Contains 1 ABC transmembrane type-1 domain.

Contains 1 ABC transporter domain.

Ontologies

Keywords
   Biological processTransport
   Cellular componentMembrane
Peroxisome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.11. Source: GOC

fatty acid beta-oxidation

Inferred from genetic interaction PubMed 9425230. Source: UniProtKB

peroxisome organization

Inferred from direct assay PubMed 9425230. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

very long-chain fatty acid catabolic process

Inferred from genetic interaction PubMed 9425230. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

mitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

peroxisomal matrix

Inferred from direct assay PubMed 9765053. Source: UniProtKB

peroxisomal membrane

Inferred from direct assay PubMed 17609205PubMed 21525035. Source: UniProtKB

peroxisome

Inferred from direct assay Ref.10PubMed 11453642PubMed 16344115PubMed 17542813PubMed 19479899PubMed 20007743PubMed 9425230. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.11. Source: UniProtKB

ATPase activity

Inferred from direct assay Ref.11. Source: UniProtKB

ATPase activity, coupled to transmembrane movement of substances

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.10Ref.9PubMed 11453642PubMed 11590176PubMed 11883941PubMed 16344115PubMed 17609205. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 17609205. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABCD1P338972EBI-80992,EBI-81045
PEX19P408554EBI-80992,EBI-594747

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P28288-1)

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: P28288-2)

The sequence of this isoform differs from the canonical sequence as follows:
     277-386: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P28288-3)

The sequence of this isoform differs from the canonical sequence as follows:
     229-236: GPASMMAY → VLGKILWH
     237-659: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 659658ATP-binding cassette sub-family D member 3
PRO_0000093309

Regions

Transmembrane84 – 10421Helical; Potential
Transmembrane126 – 14621Helical; Potential
Transmembrane224 – 24421Helical; Potential
Transmembrane313 – 33321Helical; Potential
Domain85 – 372288ABC transmembrane type-1
Domain440 – 659220ABC transporter
Nucleotide binding473 – 4808ATP Potential
Region2 – 199198Interaction with PEX19
Region2 – 124123Targeting to peroxisomes

Amino acid modifications

Modified residue611N6-acetyllysine By similarity
Modified residue2601N6-acetyllysine Ref.12
Modified residue3991N6-acetyllysine Ref.12
Modified residue5331N6-acetyllysine By similarity
Modified residue6591Phosphoserine By similarity
Glycosylation121N-linked (GlcNAc...) Potential
Glycosylation1061N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence229 – 2368GPASMMAY → VLGKILWH in isoform 3.
VSP_031187
Alternative sequence237 – 659423Missing in isoform 3.
VSP_031188
Alternative sequence277 – 386110Missing in isoform 2.
VSP_031189
Natural variant171G → D in a patient with Zellweger syndrome. Ref.1
VAR_000091

Experimental info

Mutagenesis4781G → R: Decreased ATP-binding affinity. Ref.11
Mutagenesis5721S → I: Decreased ATPase activity. Ref.11
Sequence conflict1751M → K in CAA41416. Ref.2
Sequence conflict191 – 1922QD → LV in CAA58470. Ref.3
Sequence conflict3361P → L in CAA58470. Ref.3
Sequence conflict5031G → R in CAA41416. Ref.2
Sequence conflict5421L → Q in CAA41416. Ref.2
Sequence conflict616 – 63419VGITL…WKHHE → GWHHSLHLCLIGNLFGNIMR in CAA58470. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 2CA976FEB6EB6217

FASTA65975,476
        10         20         30         40         50         60 
MAAFSKYLTA RNSSLAGAAF LLLCLLHKRR RALGLHGKKS GKPPLQNNEK EGKKERAVVD 

        70         80         90        100        110        120 
KVFFSRLIQI LKIMVPRTFC KETGYLVLIA VMLVSRTYCD VWMIQNGTLI ESGIIGRSRK 

       130        140        150        160        170        180 
DFKRYLLNFI AAMPLISLVN NFLKYGLNEL KLCFRVRLTK YLYEEYLQAF TYYKMGNLDN 

       190        200        210        220        230        240 
RIANPDQLLT QDVEKFCNSV VDLYSNLSKP FLDIVLYIFK LTSAIGAQGP ASMMAYLVVS 

       250        260        270        280        290        300 
GLFLTRLRRP IGKMTITEQK YEGEYRYVNS RLITNSEEIA FYNGNKREKQ TVHSVFRKLV 

       310        320        330        340        350        360 
EHLHNFILFR FSMGFIDSII AKYLATVVGY LVVSRPFLDL SHPRHLKSTH SELLEDYYQS 

       370        380        390        400        410        420 
GRMLLRMSQA LGRIVLAGRE MTRLAGFTAR ITELMQVLKD LNHGKYERTM VSQQEKGIEG 

       430        440        450        460        470        480 
VQVIPLIPGA GEIIIADNII KFDHVPLATP NGDVLIRDLN FEVRSGANVL ICGPNGCGKS 

       490        500        510        520        530        540 
SLFRVLGELW PLFGGRLTKP ERGKLFYVPQ RPYMTLGTLR DQVIYPDGRE DQKRKGISDL 

       550        560        570        580        590        600 
VLKEYLDNVQ LGHILEREGG WDSVQDWMDV LSGGEKQRMA MARLFYHKPQ FAILDECTSA 

       610        620        630        640        650 
VSVDVEGYIY SHCRKVGITL FTVSHRKSLW KHHEYYLHMD GRGNYEFKQI TEDTVEFGS 

« Hide

Isoform 2 [UniParc].

Checksum: 1E0139B8A2EEB7E9
Show »

FASTA54962,726
Isoform 3 [UniParc].

Checksum: 314231AA2705E8AB
Show »

FASTA23627,121

References

« Hide 'large scale' references
[1]"Mutations in the 70K peroxisomal membrane protein gene in Zellweger syndrome."
Gaertner J., Moser H., Valle D.
Nat. Genet. 1:16-23(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-17.
Tissue: Liver.
[2]"Nucleotide sequence of the human 70 kDa peroxisomal membrane protein: a member of ATP-binding cassette transporters."
Kamijo K., Kamijo T., Ueno I., Osumi T., Hashimoto T.
Biochim. Biophys. Acta 1129:323-327(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[3]"Genomic organization of the 70-kDa peroxisomal membrane protein gene (PXMP1)."
Gaertner J., Jimenez-Sanchez G., Roerig P., Valle D.
Genomics 48:203-208(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Brain and Lung.
[8]"Homo- and heterodimerization of peroxisomal ATP-binding cassette half-transporters."
Liu L.X., Janvier K., Berteaux-Lecellier V., Cartier N., Benarous R., Aubourg P.
J. Biol. Chem. 274:32738-32743(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[9]"Human adrenoleukodystrophy protein and related peroxisomal ABC transporters interact with the peroxisomal assembly protein PEX19p."
Gloeckner C.J., Mayerhofer P.U., Landgraf P., Muntau A.C., Holzinger A., Gerber J.-K., Kammerer S., Adamski J., Roscher A.A.
Biochem. Biophys. Res. Commun. 271:144-150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PEX19.
Tissue: Brain.
[10]"PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis."
Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.
J. Cell Biol. 148:931-944(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PEX19.
[11]"Characterization and functional analysis of the nucleotide binding fold in human peroxisomal ATP binding cassette transporters."
Roerig P., Mayerhofer P., Holzinger A., Gaertner J.
FEBS Lett. 492:66-72(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-478 AND SER-572.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-260 AND LYS-399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M81182 mRNA. Translation: AAA60128.1.
X58528 mRNA. Translation: CAA41416.1.
X83467 expand/collapse EMBL AC list , X83468, X83469, X83470, X83471, X83472, X83473, X83474, X83475, X83476, X83477, X83478, X83479, X83480, X83481, X83482, X83483, X83484, X83485, X83486, X83487, X83488, X83489 Genomic DNA. Translation: CAA58470.1.
BT006644 mRNA. Translation: AAP35290.1.
AL138758, AC093117, AC118469 Genomic DNA. Translation: CAC15960.2.
CH471097 Genomic DNA. Translation: EAW73049.1.
CH471097 Genomic DNA. Translation: EAW73050.1.
CH471097 Genomic DNA. Translation: EAW73047.1.
CH471097 Genomic DNA. Translation: EAW73048.1.
BC009712 mRNA. Translation: AAH09712.1.
BC068509 mRNA. Translation: AAH68509.1.
CCDSCCDS44175.1. [P28288-3]
CCDS749.1. [P28288-1]
PIRS20313.
RefSeqNP_001116146.1. NM_001122674.1. [P28288-3]
NP_002849.1. NM_002858.3. [P28288-1]
UniGeneHs.700576.

3D structure databases

ProteinModelPortalP28288.
SMRP28288. Positions 427-640.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111783. 41 interactions.
IntActP28288. 12 interactions.
MINTMINT-3010926.
STRING9606.ENSP00000359233.

Protein family/group databases

TCDB3.A.1.203.1. the atp-binding cassette (abc) superfamily.

PTM databases

PhosphoSiteP28288.

Polymorphism databases

DMDM130358.

Proteomic databases

MaxQBP28288.
PaxDbP28288.
PeptideAtlasP28288.
PRIDEP28288.

Protocols and materials databases

DNASU5825.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315713; ENSP00000326880; ENSG00000117528. [P28288-3]
ENST00000370214; ENSP00000359233; ENSG00000117528. [P28288-1]
ENST00000394233; ENSP00000377780; ENSG00000117528. [P28288-2]
GeneID5825.
KEGGhsa:5825.
UCSCuc001dqm.4. human. [P28288-3]
uc001dqn.4. human. [P28288-1]
uc009wdr.3. human. [P28288-2]

Organism-specific databases

CTD5825.
GeneCardsGC01P094883.
HGNCHGNC:67. ABCD3.
HPAHPA032026.
HPA032027.
MIM170995. gene.
neXtProtNX_P28288.
PharmGKBPA24402.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4178.
HOGENOMHOG000206081.
HOVERGENHBG050438.
InParanoidP28288.
KOK05677.
OrthoDBEOG70ZZMP.
PhylomeDBP28288.
TreeFamTF105205.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP28288.
BgeeP28288.
CleanExHS_ABCD3.
GenevestigatorP28288.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR010509. ABC_Peroxi_TM.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR005283. FA_transporter.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF06472. ABC_membrane_2. 1 hit.
PF00005. ABC_tran. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF90123. SSF90123. 1 hit.
TIGRFAMsTIGR00954. 3a01203. 1 hit.
PROSITEPS50929. ABC_TM1F. 1 hit.
PS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSABCD3. human.
GeneWikiABCD3.
GenomeRNAi5825.
NextBio22689.
PROP28288.
SOURCESearch...

Entry information

Entry nameABCD3_HUMAN
AccessionPrimary (citable) accession number: P28288
Secondary accession number(s): D3DT46 expand/collapse secondary AC list , Q15271, Q6NUN5, Q96DA3, Q9H529
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM