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P33897 (ABCD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 167. 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·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 1
Alternative name(s):
Adrenoleukodystrophy protein
Short name=ALDP
Gene names
Name:ABCD1
Synonyms:ALD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length745 AA.
Sequence statusComplete.
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.5

Subunit structure

Can form homodimers and heterodimers with ABCD2/ALDR and ABCD3/PMP70. Dimerization is necessary to form an active transporter. Interacts with PEX19. Ref.4 Ref.7 Ref.8

Subcellular location

Peroxisome membrane; Multi-pass membrane protein.

Involvement in disease

Adrenoleukodystrophy (ALD) [MIM:300100]: A peroxisomal metabolic disorder characterized by progressive multifocal demyelination of the central nervous system and by peripheral adrenal insufficiency (Addison disease). It results in mental deterioration, corticospinal tract dysfunction, and cortical blindness. Different clinical manifestations exist like: cerebral childhood ALD (CALD), adult cerebral ALD (ACALD), adrenomyeloneuropathy (AMN) and 'Addison disease only' (ADO) phenotype.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.5 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.30 Ref.31 Ref.32

The promoter region of ABCD1 is deleted in the chromosome Xq28 deletion syndrome which involves ABCD1 and the neighboring gene BCAP31.

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
   DiseaseDisease mutation
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.5. Source: GOC

alpha-linolenic acid metabolic process

Traceable author statement. Source: Reactome

cellular lipid metabolic process

Traceable author statement. Source: Reactome

fatty acid beta-oxidation

Inferred from direct assay PubMed 17542813PubMed 9425230. Source: UniProtKB

fatty acid beta-oxidation using acyl-CoA oxidase

Traceable author statement. Source: Reactome

linoleic acid metabolic process

Traceable author statement. Source: Reactome

long-chain fatty acid catabolic process

Inferred from genetic interaction PubMed 18757502. Source: UniProtKB

peroxisomal long-chain fatty acid import

Inferred from genetic interaction PubMed 18757502. Source: UniProtKB

peroxisomal membrane transport

Non-traceable author statement Ref.1. Source: UniProtKB

peroxisome organization

Inferred from direct assay PubMed 9425230. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

unsaturated fatty acid metabolic process

Traceable author statement. Source: Reactome

very long-chain fatty acid catabolic process

Inferred from direct assay PubMed 9425230. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 17761426. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

integral component of peroxisomal membrane

Inferred from direct assay PubMed 10640429. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from direct assay PubMed 17761426. Source: UniProtKB

peroxisomal membrane

Inferred from direct assay PubMed 17609205. Source: UniProtKB

peroxisome

Inferred from direct assay Ref.7PubMed 14533738PubMed 17542813PubMed 17761426PubMed 18757502PubMed 20810565PubMed 9425230. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.5. Source: UniProtKB

ATPase activity

Inferred from direct assay Ref.5. Source: UniProtKB

ATPase activity, coupled to transmembrane movement of substances

Non-traceable author statement Ref.1. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 16781659. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.4. Source: IntAct

peroxisomal fatty-acyl-CoA transporter activity

Inferred from genetic interaction PubMed 18757502. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7PubMed 11883941PubMed 17609205. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 17609205PubMed 18757502PubMed 21145416. Source: UniProtKB

transporter activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-81045,EBI-81045
Abcd1P484102EBI-81045,EBI-81118From a different organism.
ABCD3P282882EBI-81045,EBI-80992
PEX19P408553EBI-81045,EBI-594747

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 745745ATP-binding cassette sub-family D member 1
PRO_0000093304

Regions

Transmembrane92 – 11221Helical; Potential
Transmembrane131 – 15121Helical; Potential
Transmembrane238 – 25821Helical; Potential
Transmembrane333 – 35321Helical; Potential
Transmembrane473 – 49321Helical; Potential
Domain94 – 386293ABC transmembrane type-1
Domain474 – 700227ABC transporter
Nucleotide binding507 – 5148ATP By similarity
Region67 – 186120Interaction with PEX19

Amino acid modifications

Modified residue7331Phosphoserine Ref.11 Ref.12
Glycosylation2141N-linked (GlcNAc...) Potential

Natural variations

Natural variant131N → T Very rare polymorphism; does not affect ALDP function. Ref.27
Corresponds to variant rs183021839 [ dbSNP | Ensembl ].
VAR_013340
Natural variant881C → W in ALD. Ref.30
VAR_023004
Natural variant901E → K in ALD.
VAR_009349
Natural variant981S → L in ALD; CALD type. Ref.27
VAR_000024
Natural variant991A → D in ALD; AMN-type. Ref.27
VAR_013341
Natural variant1031S → R in ALD. Ref.25
VAR_009350
Natural variant1041R → C in ALD.
VAR_000025
Natural variant1041R → H in ALD; ADO-type. Ref.18
VAR_000026
Natural variant1051T → I in ALD; ADO-type.
VAR_000027
Natural variant1051T → P in ALD. Ref.23
VAR_009351
Natural variant1071L → P in ALD; ALD/AMN/ADO-types and asymptomatic. Ref.21
VAR_000028
Natural variant1081S → L in ALD. Ref.24
VAR_009352
Natural variant1081S → W in ALD; CALD and AMN-types.
VAR_000029
Natural variant1131R → C in ALD.
VAR_009353
Natural variant1131R → P in ALD.
VAR_013342
Natural variant1161G → R in ALD; CALD-type. Ref.25
VAR_000030
Natural variant138 – 1414Missing in ALD; ALD-type.
VAR_000032
Natural variant1391Missing in ALD. Ref.32
VAR_067239
Natural variant1411A → T in ALD.
VAR_000033
Natural variant1431P → S in ALD. Ref.23 Ref.24
VAR_009354
Natural variant1481N → S in ALD; ADO-type. Ref.15 Ref.23
VAR_000034
Natural variant1491S → N in ALD.
VAR_000035
Natural variant1521R → C in ALD; ADO-type. Ref.30
VAR_000036
Natural variant1521R → L in ALD.
VAR_009355
Natural variant1521R → P in ALD.
VAR_000037
Natural variant1521R → S in ALD. Ref.25
VAR_009356
Natural variant1611S → P in ALD.
VAR_009357
Natural variant1631R → H in ALD.
VAR_000038
Natural variant1631R → P in ALD.
VAR_009358
Natural variant1741Y → C in ALD. Ref.25
VAR_009359
Natural variant1741Y → D in ALD; ALD-type. Ref.15 Ref.21
VAR_000039
Natural variant1741Y → S in ALD; CALD-type.
VAR_000040
Natural variant1781Q → E in ALD; AMN-type. Ref.18
VAR_000041
Natural variant1811Y → C in ALD; ALMD-type. Ref.30
VAR_000042
Natural variant1821R → P in ALD.
VAR_000043
Natural variant1891R → W in ALD. Ref.25
VAR_009360
Natural variant1901L → P in ALD. Ref.23
VAR_009361
Natural variant1941D → H in ALD.
VAR_000044
Natural variant1981T → K in ALD.
VAR_009362
Natural variant1981T → R in ALD. Ref.32
VAR_067240
Natural variant2001D → N in ALD.
VAR_009363
Natural variant2001D → V in ALD; CALD-type.
VAR_000045
Natural variant2071S → SAAS in ALD.
VAR_013343
Natural variant2111L → P in ALD.
VAR_000046
Natural variant2131S → C in ALD.
VAR_009364
Natural variant2141N → D in ALD.
VAR_009365
Natural variant2171K → E in ALD. Ref.27
VAR_013344
Natural variant2181P → T in ALD. Ref.25
VAR_009366
Natural variant2201L → P in ALD.
VAR_000047
Natural variant2211D → G in ALD; CALD and AMN-types.
VAR_000048
Natural variant2241V → E in ALD.
VAR_013345
Natural variant2291L → P in ALD. Ref.25
VAR_009367
Natural variant2541T → M in ALD; AMN-type. Ref.21
VAR_000049
Natural variant2541T → P in ALD; AMN-type.
VAR_000050
Natural variant2631P → L in ALD; CALD, AMN and AD-types.
VAR_000051
Natural variant2661G → E in ALD. Ref.32
VAR_067241
Natural variant2661G → R in ALD. Ref.15 Ref.32
VAR_000052
Natural variant2711E → K in ALD.
VAR_009368
Natural variant2741R → W in ALD.
VAR_013346
Natural variant2761K → E in ALD; CALD-type.
VAR_000053
Natural variant2771G → GN in ALD; ADO-type.
VAR_000055
Natural variant2771G → R in ALD; AMN-type.
VAR_000054
Natural variant2771G → W in ALD.
VAR_000056
Natural variant2801R → C in ALD.
VAR_013347
Natural variant2851R → P in ALD.
VAR_009369
Natural variant2911E → D in ALD; ACALD and CALD-types.
VAR_000057
Natural variant2911E → K in ALD. Ref.14
VAR_000058
Natural variant2911Missing in ALD; ALD-type.
VAR_000059
Natural variant2941A → T in ALD; AMN-type.
VAR_000060
Natural variant2961Y → C in ALD.
VAR_009370
Natural variant2981G → D in ALD. Ref.23 Ref.25
VAR_009371
Natural variant3001E → EVGQ in ALD.
VAR_013348
Natural variant3021E → K in ALD.
VAR_009372
Natural variant3221L → P in ALD.
VAR_009373
Natural variant3361K → M in ALD.
VAR_009374
Natural variant3391W → R in ALD.
VAR_013349
Natural variant3421S → P in ALD; AMN-type.
VAR_000061
Natural variant3431G → D in ALD.
VAR_013350
Natural variant3431G → S in ALD. Ref.30
VAR_023005
Natural variant3891R → G in ALD; AMN-type. Ref.21
VAR_000062
Natural variant3891R → H in ALD; does not affect protein stability, homo- and heterodimerization with ALDR and PMP70. Ref.4
VAR_000063
Natural variant4011R → Q in ALD; ALD and AMN-types; does not affect protein stability, homo- and heterodimerization with ALDR and PMP70. Ref.4 Ref.15 Ref.21 Ref.25 Ref.26 Ref.31
VAR_000064
Natural variant4011R → W in ALD. Ref.25 Ref.32
VAR_009375
Natural variant4181R → W in ALD; AMN-type. Ref.15 Ref.21 Ref.25 Ref.26
VAR_000065
Natural variant4271Missing in ALD.
VAR_013351
Natural variant4841P → R in ALD; CALD, AMN and ADO-types; significantly decreases homodimerization and abolishes heterodimerization with ALDR and PMP70. Ref.4
VAR_000066
Natural variant5031L → P in ALD. Ref.30
VAR_023006
Natural variant5071G → V in ALD; CALD-types.
VAR_000067
Natural variant5121G → S in ALD; CALD and AS-types; reduced ATPase activity. Ref.5
VAR_000068
Natural variant5141S → R in ALD. Ref.30
VAR_023007
Natural variant5151S → F in ALD. Ref.15
VAR_000069
Natural variant5161L → P in ALD. Ref.31
VAR_067328
Natural variant5181R → Q in ALD; CALD-type. Ref.27 Ref.32
VAR_000070
Natural variant5181R → W in ALD; CALD-type. Ref.16
VAR_000071
Natural variant5221G → W in ALD; AD-type.
VAR_000072
Natural variant5231L → F in ALD. Ref.32
VAR_067242
Natural variant5281Missing in ALD; CALD-type. Ref.18
VAR_000073
Natural variant5291G → S in ALD. Ref.23
VAR_009376
Natural variant5341P → L in ALD; CALD-type.
VAR_000074
Natural variant5401F → C in ALD. Ref.32
VAR_067243
Natural variant5401F → S in ALD.
VAR_009377
Natural variant5431P → L in ALD. Ref.25 Ref.26
VAR_009378
Natural variant5441Q → R in ALD.
VAR_009379
Natural variant5521S → P in ALD.
VAR_009380
Natural variant5541R → H in ALD. Ref.25 Ref.30
VAR_009381
Natural variant5561Q → R in ALD; ACALD type. Ref.26
VAR_013352
Natural variant5601P → L in ALD; CALD-type. Ref.18 Ref.31 Ref.32
VAR_000075
Natural variant5601P → R in ALD; AMN and ALMD-types.
VAR_000076
Natural variant5601P → S in ALD.
VAR_013353
Natural variant5661M → K in ALD.
VAR_000077
Natural variant5911R → P in ALD.
VAR_013354
Natural variant5911R → Q in ALD; AMN-type; significantly decreases homodimerization and abolishes heterodimerization with ALDR and PMP70. Ref.4
VAR_000078
Natural variant5911R → W in ALD.
VAR_009382
Natural variant6061S → L in ALD; decreased ATP-binding affinity. Ref.5 Ref.16
VAR_000079
Natural variant6061S → P in ALD; CALD, AMN and ALMD-types. Ref.31 Ref.32
VAR_000080
Natural variant6081G → D in ALD; CALD-type. Ref.27
VAR_013355
Natural variant6091E → G in ALD.
VAR_000081
Natural variant6091E → K in ALD; AMN-type. Ref.21
VAR_000082
Natural variant6161A → V in ALD. Ref.25
VAR_009383
Natural variant6171R → C in ALD; ALD-type and asymptomatic. Ref.16 Ref.21
VAR_000083
Natural variant6171R → G in ALD; ADO and AMN-types with cerebral involvement. Ref.21
VAR_000084
Natural variant6171R → H in ALD. Ref.16 Ref.32
VAR_000085
Natural variant6261A → D in ALD.
VAR_013356
Natural variant6261A → T in ALD; CALD and AMN-types. Ref.32
VAR_000086
Natural variant6291D → H in ALD.
VAR_000087
Natural variant6301E → G in ALD.
VAR_009384
Natural variant6311C → Y in ALD.
VAR_009385
Natural variant6321T → I in ALD.
VAR_013357
Natural variant6321T → P in ALD. Ref.32
VAR_067244
Natural variant6331S → I in ALD; asymptomatic. Ref.27
VAR_013358
Natural variant6331S → R in ALD. Ref.25 Ref.32
VAR_009386
Natural variant6351V → M in ALD.
VAR_013359
Natural variant6361S → I in ALD.
VAR_009387
Natural variant6381D → Y in ALD. Ref.23
VAR_009388
Natural variant6401E → K in ALD. Ref.32
VAR_067245
Natural variant6461A → P in ALD. Ref.25
VAR_009389
Natural variant6541L → P in ALD.
VAR_009390
Natural variant6571Missing in ALD; CALD-type.
VAR_000088
Natural variant6601R → P in ALD; CALD-type. Ref.27
VAR_013360
Natural variant6601R → Q in ALD. Ref.31
VAR_067329
Natural variant6601R → W in ALD; CALD, ALMD and AS-types.
VAR_000089
Natural variant6671H → D in ALD.
VAR_009391
Natural variant6681T → I in ALD.
VAR_009392
Natural variant6771G → D in ALD. Ref.32
VAR_067246
Natural variant6791W → R in ALD; AMN-type. Ref.22
VAR_000090
Natural variant6931T → M in ALD.
VAR_009393

Experimental info

Sequence conflict1231V → A in CAA79922. Ref.1
Sequence conflict1231V → A in CAA83230. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P33897 [UniParc].

Last modified June 7, 2005. Version 2.
Checksum: 82F90905F71FFDC8

FASTA74582,937
        10         20         30         40         50         60 
MPVLSRPRPW RGNTLKRTAV LLALAAYGAH KVYPLVRQCL APARGLQAPA GEPTQEASGV 

        70         80         90        100        110        120 
AAAKAGMNRV FLQRLLWLLR LLFPRVLCRE TGLLALHSAA LVSRTFLSVY VARLDGRLAR 

       130        140        150        160        170        180 
CIVRKDPRAF GWQLLQWLLI ALPATFVNSA IRYLEGQLAL SFRSRLVAHA YRLYFSQQTY 

       190        200        210        220        230        240 
YRVSNMDGRL RNPDQSLTED VVAFAASVAH LYSNLTKPLL DVAVTSYTLL RAARSRGAGT 

       250        260        270        280        290        300 
AWPSAIAGLV VFLTANVLRA FSPKFGELVA EEARRKGELR YMHSRVVANS EEIAFYGGHE 

       310        320        330        340        350        360 
VELALLQRSY QDLASQINLI LLERLWYVML EQFLMKYVWS ASGLLMVAVP IITATGYSES 

       370        380        390        400        410        420 
DAEAVKKAAL EKKEEELVSE RTEAFTIARN LLTAAADAIE RIMSSYKEVT ELAGYTARVH 

       430        440        450        460        470        480 
EMFQVFEDVQ RCHFKRPREL EDAQAGSGTI GRSGVRVEGP LKIRGQVVDV EQGIICENIP 

       490        500        510        520        530        540 
IVTPSGEVVV ASLNIRVEEG MHLLITGPNG CGKSSLFRIL GGLWPTYGGV LYKPPPQRMF 

       550        560        570        580        590        600 
YIPQRPYMSV GSLRDQVIYP DSVEDMQRKG YSEQDLEAIL DVVHLHHILQ REGGWEAMCD 

       610        620        630        640        650        660 
WKDVLSGGEK QRIGMARMFY HRPKYALLDE CTSAVSIDVE GKIFQAAKDA GIALLSITHR 

       670        680        690        700        710        720 
PSLWKYHTHL LQFDGEGGWK FEKLDSAARL SLTEEKQRLE QQLAGIPKMQ RRLQELCQIL 

       730        740 
GEAVAPAHVP APSPQGPGGL QGAST 

« Hide

References

« Hide 'large scale' references
[1]"Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters."
Mosser J., Douar A.-M., Sarde C.-O., Kioschis P., Feil R., Moser H., Poustka A.-M., Mandel J.-L., Aubourg P.
Nature 361:726-730(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
Tissue: Pancreas.
[4]"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, CHARACTERIZATION OF VARIANTS ALD HIS-389; GLN-401; ARG-484 AND GLN-591.
[5]"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, CHARACTERIZATION OF VARIANTS ALD SER-512 AND LEU-606.
[6]"Adrenoleukodystrophy gene: unexpected homology to a protein involved in peroxisome biogenesis."
Aubourg P., Mosser J., Douar A.-M., Sarde C.-O., Lopez J., Mandel J.-L.
Biochimie 75:293-302(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[7]"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.
[8]"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: INTERACTION WITH PEX19.
[9]"Mutations in the adrenoleukodystrophy gene."
Dodd A., Rowland S.A., Hawkes S.L.J., Kennedy M.A., Love D.R.
Hum. Mutat. 9:500-511(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[10]"ABCD1 mutations and the X-linked adrenoleukodystrophy mutation database: role in diagnosis and clinical correlations."
Kemp S., Pujol A., Waterham H.R., van Geel B.M., Boehm C.D., Raymond G.V., Cutting G.R., Wanders R.J.A., Moser H.W.
Hum. Mutat. 18:499-515(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[11]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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]"Abnormal messenger RNA expression and a missense mutation in patients with X-linked adrenoleukodystrophy."
Cartier N., Sarde C.-O., Douar A.-M., Mosser J., Mandel J.-L., Aubourg P.
Hum. Mol. Genet. 2:1949-1951(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALD LYS-291.
[15]"Missense mutations are frequent in the gene for X-chromosomal adrenoleukodystrophy (ALD)."
Fuchs S., Sarde C.-O., Wedemann H., Schwinger E., Mandel J.-L., Gal A.
Hum. Mol. Genet. 3:1903-1905(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD SER-148; ASP-174; ARG-266; GLN-401; TRP-418 AND PHE-515.
[16]"Identification of mutations in the putative ATP-binding domain of the adrenoleukodystrophy gene."
Fanen P., Guidoux S., Sarde C.-O., Mandel J.-L., Goossens M., Aubourg P.
J. Clin. Invest. 94:516-520(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD TRP-518; LEU-606; CYS-617 AND HIS-617.
[17]"Spectrum of mutations in the gene encoding the adrenoleukodystrophy protein."
Ligtenberg M.J.L., Kemp S., Sarde C.-O., van Geel B.M., Kleijer W.J., Barth P.G., Mandel J.-L., van Oost B.A., Bolhuis P.A.
Am. J. Hum. Genet. 56:44-50(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD.
[18]"Mutations in the gene for X-linked adrenoleukodystrophy in patients with different clinical phenotypes."
Braun A., Ambach H., Kammerer S., Rolinski B., Stoeckler S., Rabl W., Gaertner J., Zierz S., Roscher A.A.
Am. J. Hum. Genet. 56:854-861(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD HIS-104; GLU-178; GLY-528 DEL AND LEU-560.
[19]"Mutational analysis of patients with X-linked adrenoleukodystrophy."
Kok F., Neumann S., Sarde C.-O., Zheng S., Wu K.-H., Wei H.-M., Bergin J., Watkins P.A., Gould S., Sack G., Moser H., Mandel J.-L., Smith K.D.
Hum. Mutat. 6:104-115(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD.
[20]"Mutational and protein analysis of patients and heterozygous women with X-linked adrenoleukodystrophy."
Feigenbaum V., Lombard-Platet G., Guidoux S., Sarde C.-O., Mandel J.-L., Aubourg P.
Am. J. Hum. Genet. 58:1135-1144(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD.
[21]"Identification of mutations in the ALD-gene of 20 families with adrenoleukodystrophy/adrenomyeloneuropathy."
Krasemann E.W., Meier V., Korenke G.C., Hunneman D.H., Hanefeld F.
Hum. Genet. 97:194-197(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD PRO-107; ASP-174; MET-254; GLY-389; GLN-401; TRP-418; LYS-609; CYS-617 AND GLY-617.
[22]"First missense mutation (W679R) in exon 10 of the adrenoleukodystrophy gene in siblings with adrenomyeloneuropathy."
Korenke G.C., Krasemann E., Meier V., Beuche W., Hunneman D.H., Hanefeld F.
Hum. Mutat. Suppl. 1:S204-S206(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALD ARG-679.
[23]"X-linked adrenomyeloneuropathy associated with 14 novel ALD-gene mutations: no correlation between type of mutation and age of onset."
Wichers M., Kohler W., Brennemann W., Boese V., Sokolowski P., Bidlingmaier F., Ludwig M.
Hum. Genet. 105:116-119(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD PRO-105; SER-143; SER-148; PRO-190; ASP-298; SER-529 AND TYR-638.
[24]"Two novel missense mutations causing adrenoleukodystrophy in Italian patients."
Perusi C., Gomez-Lira M., Mottes M., Pignatti P.F., Bertini E., Cappa M., Vigliani M.C., Schiffer D., Rizzuto N., Salviati A.
Mol. Cell. Probes 13:179-182(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD LEU-108 AND SER-143.
[25]"Determination of 30 X-linked adrenoleukodystrophy mutations, including 15 not previously described."
Lachtermacher M.B., Seuanez H.N., Moser A.B., Moser H.W., Smith K.D.
Hum. Mutat. 15:348-353(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD ARG-103; ARG-116; SER-152; CYS-174; TRP-189; THR-218; PRO-229; ASP-298; GLN-401; TRP-401; TRP-418; LEU-543; HIS-554; VAL-616; ARG-633 AND PRO-646.
[26]"Detection of mutations in the ALD gene (ABCD1) in seven Italian families: description of four novel mutations."
Lira M.G., Mottes M., Pignatti P.F., Medica I., Uziel G., Cappa M., Bertini E., Rizzuto N., Salviati A.
Hum. Mutat. 16:271-271(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD GLN-401; TRP-418; LEU-543 AND ARG-556.
[27]"Eight novel ABCD1 gene mutations and three polymorphisms in patients with X-linked adrenoleukodystrophy: the first polymorphism causing an amino acid exchange."
Dvorakova L., Storkanova G., Unterrainer G., Hujova J., Kmoch S., Zeman J., Hrebicek M., Berger J.
Hum. Mutat. 18:52-60(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD LEU-98; ASP-99; GLU-217; GLN-518; ASP-608; ILE-633 AND PRO-660, VARIANT THR-13.
[28]"Characterisation of two mutations in the ABCD1 gene leading to low levels of normal ALDP."
Guimaraes C.P., Lemos M., Menezes I., Coelho T., Sa-Miranda C., Azevedo J.E.
Hum. Genet. 109:616-622(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALD VAL-GLY-GLN-300 INS.
[29]"Contiguous deletion of the X-linked adrenoleukodystrophy gene (ABCD1) and DXS1357E: a novel neonatal phenotype similar to peroxisomal biogenesis disorders."
Corzo D., Gibson W., Johnson K., Mitchell G., LePage G., Cox G.F., Casey R., Zeiss C., Tyson H., Cutting G.R., Raymond G.V., Smith K.D., Watkins P.A., Moser A.B., Moser H.W., Steinberg S.J.
Am. J. Hum. Genet. 70:1520-1531(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CONTIGUOUS ABCD1/DXS1375E DELETION SYNDROME.
[30]"Identification of seven novel mutations in ABCD1 by a DHPLC-based assay in Italian patients with X-linked adrenoleukodystrophy."
Montagna G., Di Biase A., Cappa M., Melone M.A.B., Piantadosi C., Colabianchi D., Patrono C., Attori L., Cannelli N., Cotrufo R., Salvati S., Santorelli F.M.
Hum. Mutat. 25:222-222(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD TRP-88; CYS-152; CYS-181; SER-343; PRO-503; ARG-514 AND HIS-554.
[31]"Molecular analysis of ABCD1 gene in Indian patients with X-linked adrenoleukodystrophy."
Shukla P., Gupta N., Gulati S., Ghosh M., Vasisht S., Sharma R., Gupta A.K., Kalra V., Kabra M.
Clin. Chim. Acta 412:2289-2295(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD GLN-401; PRO-516; LEU-560; PRO-606 AND GLN-660.
[32]"X-linked adrenoleukodystrophy: ABCD1 de novo mutations and mosaicism."
Wang Y., Busin R., Reeves C., Bezman L., Raymond G., Toomer C.J., Watkins P.A., Snowden A., Moser A., Naidu S., Bibat G., Hewson S., Tam K., Clarke J.T., Charnas L., Stetten G., Karczeski B., Cutting G., Steinberg S.
Mol. Genet. Metab. 104:160-166(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALD LEU-139 DEL; ARG-198; ARG-266; GLU-266; TRP-401; GLN-518; PHE-523; CYS-540; LEU-560; PRO-606; HIS-617; THR-626; PRO-632; ARG-633; LYS-640 AND ASP-677.
+Additional computationally mapped references.

Web resources

X-ALD gene mutation database
ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z21876 mRNA. Translation: CAA79922.1.
Z31348 expand/collapse EMBL AC list , Z31006, Z31007, Z31008, Z31009, Z31010 Genomic DNA. Translation: CAA83230.1.
U52111 Genomic DNA. No translation available.
BC015541 mRNA. Translation: AAH15541.1.
BC025358 mRNA. Translation: AAH25358.1.
CCDSCCDS14728.1.
PIRG02500.
RefSeqNP_000024.2. NM_000033.3.
UniGeneHs.159546.

3D structure databases

ProteinModelPortalP33897.
SMRP33897. Positions 466-675.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106717. 17 interactions.
IntActP33897. 6 interactions.
STRING9606.ENSP00000218104.

Protein family/group databases

TCDB3.A.1.203.3. the atp-binding cassette (abc) superfamily.

PTM databases

PhosphoSiteP33897.

Polymorphism databases

DMDM67476960.

Proteomic databases

MaxQBP33897.
PaxDbP33897.
PeptideAtlasP33897.
PRIDEP33897.

Protocols and materials databases

DNASU215.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000218104; ENSP00000218104; ENSG00000101986.
ENST00000601366; ENSP00000473207; ENSG00000268757.
GeneID215.
KEGGhsa:215.
UCSCuc004fif.2. human.

Organism-specific databases

CTD215.
GeneCardsGC0XP152990.
GeneReviewsABCD1.
HGNCHGNC:61. ABCD1.
HPAHPA035214.
MIM300100. phenotype.
300371. gene.
neXtProtNX_P33897.
Orphanet139399. Adrenomyeloneuropathy.
369942. CADDS.
139396. X-linked cerebral adrenoleukodystrophy.
PharmGKBPA24396.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4178.
HOGENOMHOG000206081.
HOVERGENHBG050438.
InParanoidP33897.
KOK05675.
OMAIPKMQRR.
PhylomeDBP33897.
TreeFamTF105205.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP33897.
BgeeP33897.
CleanExHS_ABCD1.
GenevestigatorP33897.

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

GeneWikiABCD1.
GenomeRNAi215.
NextBio870.
PROP33897.
SOURCESearch...

Entry information

Entry nameABCD1_HUMAN
AccessionPrimary (citable) accession number: P33897
Secondary accession number(s): Q6GTZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 7, 2005
Last modified: July 9, 2014
This is version 167 of the entry and version 2 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 X

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