P33897 (ABCD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-binding cassette sub-family D member 1

Alternative name(s):
Adrenoleukodystrophy protein
Short name=ALDP

Gene names

Name:	ABCD1
Synonyms:	ALD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	745 AA.
Sequence status	Complete.
Protein existence	Evidence 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, X-linked (X-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 process	Transport
Cellular component	Membrane Peroxisome
Disease	Disease mutation
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	alpha-linolenic acid metabolic process Traceable author statement. Source: Reactome 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 membrane transport Non-traceable author statement Ref.1. Source: UniProtKB peroxisome organization Inferred from direct assay PubMed 9425230. Source: UniProtKB very long-chain fatty acid catabolic process Inferred from direct assay PubMed 9425230. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome integral to peroxisomal membrane Inferred from direct assay PubMed 10640429. Source: UniProtKB mitochondrion Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from direct assay PubMed 17761426. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay Ref.5. Source: UniProtKB ATPase activity, coupled to transmembrane movement of substances Non-traceable author statement Ref.1. Source: UniProtKB peroxisomal fatty-acyl-CoA transporter activity Inferred from genetic interaction PubMed 18757502. Source: UniProtKB protein homodimerization activity Inferred from direct assay PubMed 17609205PubMed 18757502PubMed 21145416. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-81045,EBI-81045
Abcd1	P48410	2	EBI-81045,EBI-81118	From a different organism.
ABCD3	P28288	2	EBI-81045,EBI-80992

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 745	745	ATP-binding cassette sub-family D member 1		PRO_0000093304
Regions
	Transmembrane	92 – 112	21	Helical; Potential
	Transmembrane	131 – 151	21	Helical; Potential
	Transmembrane	238 – 258	21	Helical; Potential
	Transmembrane	333 – 353	21	Helical; Potential
	Transmembrane	473 – 493	21	Helical; Potential
	Domain	94 – 386	293	ABC transmembrane type-1
	Domain	474 – 700	227	ABC transporter
	Nucleotide binding	507 – 514	8	ATP By similarity
	Region	67 – 186	120	Interaction with PEX19
Amino acid modifications
	Modified residue	733	1	Phosphoserine Ref.11 Ref.12
	Glycosylation	214	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	13	1	N → T Very rare polymorphism; does not affect ALDP function. Ref.27		VAR_013340
	Natural variant	88	1	C → W in X-ALD. Ref.30		VAR_023004
	Natural variant	90	1	E → K in X-ALD.		VAR_009349
	Natural variant	98	1	S → L in X-ALD; CALD type. Ref.27		VAR_000024
	Natural variant	99	1	A → D in X-ALD; AMN-type. Ref.27		VAR_013341
	Natural variant	103	1	S → R in X-ALD.		VAR_009350
	Natural variant	104	1	R → C in X-ALD.		VAR_000025
	Natural variant	104	1	R → H in X-ALD; ADO-type. Ref.18		VAR_000026
	Natural variant	105	1	T → I in X-ALD; ADO-type.		VAR_000027
	Natural variant	105	1	T → P in X-ALD.		VAR_009351
	Natural variant	107	1	L → P in X-ALD; ALD/AMN/ADO-types and asymptomatic.		VAR_000028
	Natural variant	108	1	S → L in X-ALD. Ref.24		VAR_009352
	Natural variant	108	1	S → W in X-ALD; CALD and AMN-types.		VAR_000029
	Natural variant	113	1	R → C in X-ALD.		VAR_009353
	Natural variant	113	1	R → P in X-ALD.		VAR_013342
	Natural variant	116	1	G → R in X-ALD; CALD-type.		VAR_000030
	Natural variant	138 – 141	4	Missing in X-ALD; ALD-type.		VAR_000032
	Natural variant	139	1	Missing in X-ALD. Ref.32		VAR_067239
	Natural variant	141	1	A → T in X-ALD.		VAR_000033
	Natural variant	143	1	P → S in X-ALD. Ref.24		VAR_009354
	Natural variant	148	1	N → S in X-ALD; ADO-type. Ref.15		VAR_000034
	Natural variant	149	1	S → N in X-ALD.		VAR_000035
	Natural variant	152	1	R → C in X-ALD; ADO-type. Ref.30		VAR_000036
	Natural variant	152	1	R → L in X-ALD.		VAR_009355
	Natural variant	152	1	R → P in X-ALD.		VAR_000037
	Natural variant	152	1	R → S in X-ALD.		VAR_009356
	Natural variant	161	1	S → P in X-ALD.		VAR_009357
	Natural variant	163	1	R → H in X-ALD.		VAR_000038
	Natural variant	163	1	R → P in X-ALD.		VAR_009358
	Natural variant	174	1	Y → C in X-ALD.		VAR_009359
	Natural variant	174	1	Y → D in X-ALD; ALD-type. Ref.15		VAR_000039
	Natural variant	174	1	Y → S in X-ALD; CALD-type.		VAR_000040
	Natural variant	178	1	Q → E in X-ALD; AMN-type. Ref.18		VAR_000041
	Natural variant	181	1	Y → C in X-ALD; ALMD-type. Ref.30		VAR_000042
	Natural variant	182	1	R → P in X-ALD.		VAR_000043
	Natural variant	189	1	R → W in X-ALD.		VAR_009360
	Natural variant	190	1	L → P in X-ALD.		VAR_009361
	Natural variant	194	1	D → H in X-ALD.		VAR_000044
	Natural variant	198	1	T → K in X-ALD.		VAR_009362
	Natural variant	198	1	T → R in X-ALD. Ref.32		VAR_067240
	Natural variant	200	1	D → N in X-ALD.		VAR_009363
	Natural variant	200	1	D → V in X-ALD; CALD-type.		VAR_000045
	Natural variant	207	1	S → SAAS in X-ALD.		VAR_013343
	Natural variant	211	1	L → P in X-ALD.		VAR_000046
	Natural variant	213	1	S → C in X-ALD.		VAR_009364
	Natural variant	214	1	N → D in X-ALD.		VAR_009365
	Natural variant	217	1	K → E in X-ALD. Ref.27		VAR_013344
	Natural variant	218	1	P → T in X-ALD.		VAR_009366
	Natural variant	220	1	L → P in X-ALD.		VAR_000047
	Natural variant	221	1	D → G in X-ALD; CALD and AMN-types.		VAR_000048
	Natural variant	224	1	V → E in X-ALD.		VAR_013345
	Natural variant	229	1	L → P in X-ALD.		VAR_009367
	Natural variant	254	1	T → M in X-ALD; AMN-type.		VAR_000049
	Natural variant	254	1	T → P in X-ALD; AMN-type.		VAR_000050
	Natural variant	263	1	P → L in X-ALD; CALD, AMN and AD-types.		VAR_000051
	Natural variant	266	1	G → E in X-ALD. Ref.32		VAR_067241
	Natural variant	266	1	G → R in X-ALD. Ref.15 Ref.32		VAR_000052
	Natural variant	271	1	E → K in X-ALD.		VAR_009368
	Natural variant	274	1	R → W in X-ALD.		VAR_013346
	Natural variant	276	1	K → E in X-ALD; CALD-type.		VAR_000053
	Natural variant	277	1	G → GN in X-ALD; ADO-type.		VAR_000055
	Natural variant	277	1	G → R in X-ALD; AMN-type.		VAR_000054
	Natural variant	277	1	G → W in X-ALD.		VAR_000056
	Natural variant	280	1	R → C in X-ALD.		VAR_013347
	Natural variant	285	1	R → P in X-ALD.		VAR_009369
	Natural variant	291	1	E → D in X-ALD; ACALD and CALD-types.		VAR_000057
	Natural variant	291	1	E → K in X-ALD. Ref.14		VAR_000058
	Natural variant	291	1	Missing in X-ALD; ALD-type.		VAR_000059
	Natural variant	294	1	A → T in X-ALD; AMN-type.		VAR_000060
	Natural variant	296	1	Y → C in X-ALD.		VAR_009370
	Natural variant	298	1	G → D in X-ALD.		VAR_009371
	Natural variant	300	1	E → EVGQ in X-ALD.		VAR_013348
	Natural variant	302	1	E → K in X-ALD.		VAR_009372
	Natural variant	322	1	L → P in X-ALD.		VAR_009373
	Natural variant	336	1	K → M in X-ALD.		VAR_009374
	Natural variant	339	1	W → R in X-ALD.		VAR_013349
	Natural variant	342	1	S → P in X-ALD; AMN-type.		VAR_000061
	Natural variant	343	1	G → D in X-ALD.		VAR_013350
	Natural variant	343	1	G → S in X-ALD. Ref.30		VAR_023005
	Natural variant	389	1	R → G in X-ALD; AMN-type.		VAR_000062
	Natural variant	389	1	R → H in X-ALD; does not affect protein stability, homo- and heterodimerization with ALDR and PMP70. Ref.4		VAR_000063
	Natural variant	401	1	R → Q in X-ALD; ALD and AMN-types; does not affect protein stability, homo- and heterodimerization with ALDR and PMP70. Ref.4 Ref.15 Ref.26 Ref.31		VAR_000064
	Natural variant	401	1	R → W in X-ALD. Ref.32		VAR_009375
	Natural variant	418	1	R → W in X-ALD; AMN-type. Ref.15 Ref.26		VAR_000065
	Natural variant	427	1	Missing in X-ALD.		VAR_013351
	Natural variant	484	1	P → R in X-ALD; CALD, AMN and ADO-types; significantly decreases homodimerization and abolishes heterodimerization with ALDR and PMP70. Ref.4		VAR_000066
	Natural variant	503	1	L → P in X-ALD. Ref.30		VAR_023006
	Natural variant	507	1	G → V in X-ALD; CALD-types.		VAR_000067
	Natural variant	512	1	G → S in X-ALD; CALD and AS-types; reduced ATPase activity. Ref.5		VAR_000068
	Natural variant	514	1	S → R in X-ALD. Ref.30		VAR_023007
	Natural variant	515	1	S → F in X-ALD. Ref.15		VAR_000069
	Natural variant	516	1	L → P in X-ALD. Ref.31		VAR_067328
	Natural variant	518	1	R → Q in X-ALD; CALD-type. Ref.27 Ref.32		VAR_000070
	Natural variant	518	1	R → W in X-ALD; CALD-type. Ref.16		VAR_000071
	Natural variant	522	1	G → W in X-ALD; AD-type.		VAR_000072
	Natural variant	523	1	L → F in X-ALD. Ref.32		VAR_067242
	Natural variant	528	1	Missing in X-ALD; CALD-type. Ref.18		VAR_000073
	Natural variant	529	1	G → S in X-ALD.		VAR_009376
	Natural variant	534	1	P → L in X-ALD; CALD-type.		VAR_000074
	Natural variant	540	1	F → C in X-ALD. Ref.32		VAR_067243
	Natural variant	540	1	F → S in X-ALD.		VAR_009377
	Natural variant	543	1	P → L in X-ALD. Ref.26		VAR_009378
	Natural variant	544	1	Q → R in X-ALD.		VAR_009379
	Natural variant	552	1	S → P in X-ALD.		VAR_009380
	Natural variant	554	1	R → H in X-ALD. Ref.30		VAR_009381
	Natural variant	556	1	Q → R in X-ALD; ACALD type. Ref.26		VAR_013352
	Natural variant	560	1	P → L in X-ALD; CALD-type. Ref.18 Ref.31 Ref.32		VAR_000075
	Natural variant	560	1	P → R in X-ALD; AMN and ALMD-types.		VAR_000076
	Natural variant	560	1	P → S in X-ALD.		VAR_013353
	Natural variant	566	1	M → K in X-ALD.		VAR_000077
	Natural variant	591	1	R → P in X-ALD.		VAR_013354
	Natural variant	591	1	R → Q in X-ALD; AMN-type; significantly decreases homodimerization and abolishes heterodimerization with ALDR and PMP70. Ref.4		VAR_000078
	Natural variant	591	1	R → W in X-ALD.		VAR_009382
	Natural variant	606	1	S → L in X-ALD; decreased ATP-binding affinity. Ref.5 Ref.16		VAR_000079
	Natural variant	606	1	S → P in X-ALD; CALD, AMN and ALMD-types. Ref.31 Ref.32		VAR_000080
	Natural variant	608	1	G → D in X-ALD; CALD-type. Ref.27		VAR_013355
	Natural variant	609	1	E → G in X-ALD.		VAR_000081
	Natural variant	609	1	E → K in X-ALD; AMN-type.		VAR_000082
	Natural variant	616	1	A → V in X-ALD.		VAR_009383
	Natural variant	617	1	R → C in X-ALD; ALD-type and asymptomatic. Ref.16		VAR_000083
	Natural variant	617	1	R → G in X-ALD; ADO and AMN-types with cerebral involvement.		VAR_000084
	Natural variant	617	1	R → H in X-ALD. Ref.16 Ref.32		VAR_000085
	Natural variant	626	1	A → D in X-ALD.		VAR_013356
	Natural variant	626	1	A → T in X-ALD; CALD and AMN-types. Ref.32		VAR_000086
	Natural variant	629	1	D → H in X-ALD.		VAR_000087
	Natural variant	630	1	E → G in X-ALD.		VAR_009384
	Natural variant	631	1	C → Y in X-ALD.		VAR_009385
	Natural variant	632	1	T → I in X-ALD.		VAR_013357
	Natural variant	632	1	T → P in X-ALD. Ref.32		VAR_067244
	Natural variant	633	1	S → I in X-ALD; asymptomatic. Ref.27		VAR_013358
	Natural variant	633	1	S → R in X-ALD. Ref.32		VAR_009386
	Natural variant	635	1	V → M in X-ALD.		VAR_013359
	Natural variant	636	1	S → I in X-ALD.		VAR_009387
	Natural variant	638	1	D → Y in X-ALD.		VAR_009388
	Natural variant	640	1	E → K in X-ALD. Ref.32		VAR_067245
	Natural variant	646	1	A → P in X-ALD.		VAR_009389
	Natural variant	654	1	L → P in X-ALD.		VAR_009390
	Natural variant	657	1	Missing in X-ALD; CALD-type.		VAR_000088
	Natural variant	660	1	R → P in X-ALD; CALD-type. Ref.27		VAR_013360
	Natural variant	660	1	R → Q in X-ALD. Ref.31		VAR_067329
	Natural variant	660	1	R → W in X-ALD; CALD, ALMD and AS-types.		VAR_000089
	Natural variant	667	1	H → D in X-ALD.		VAR_009391
	Natural variant	668	1	T → I in X-ALD.		VAR_009392
	Natural variant	677	1	G → D in X-ALD. Ref.32		VAR_067246
	Natural variant	679	1	W → R in X-ALD; AMN-type. Ref.22		VAR_000090
	Natural variant	693	1	T → M in X-ALD.		VAR_009393
Experimental info
	Sequence conflict	123	1	V → A in CAA79922. Ref.1
	Sequence conflict	123	1	V → A in CAA83230. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P33897 [UniParc]. Last modified June 7, 2005. Version 2. Checksum: 82F90905F71FFDC8	FASTA	745	82,937
	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

References

	« Hide 'large scale' referencesShow '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. , 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 X-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 X-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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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 X-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 X-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 X-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 X-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 X-ALD HIS-104; GLU-178; LEU-560 AND GLY-528 DEL.
[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 X-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 X-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 X-ALD.
[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 X-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 X-ALD.
[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 X-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 X-ALD.
[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 X-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 X-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 X-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 X-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 X-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 X-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

GeneReviews

ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z21876 mRNA. Translation: CAA79922.1. Z31348 , 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.
IPI	IPI00291373.
PIR	G02500.
RefSeq	NP_000024.2. NM_000033.3.
UniGene	Hs.159546.
3D structure databases
ProteinModelPortal	P33897.
ModBase	Search...
Protein-protein interaction databases
IntAct	P33897. 5 interactions.
STRING	9606.ENSP00000218104.
Protein family/group databases
TCDB	3.A.1.203.3. ATP-binding cassette (ABC) superfamily.
PTM databases
PhosphoSite	P33897.
Polymorphism databases
DMDM	67476960.
Proteomic databases
PaxDb	P33897.
PeptideAtlas	P33897.
PRIDE	P33897.
Protocols and materials databases
DNASU	215.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000218104; ENSP00000218104; ENSG00000101986. ENST00000601366; ENSP00000473207; ENSG00000268757.
GeneID	215.
KEGG	hsa:215.
UCSC	uc004fif.2. human.
Organism-specific databases
CTD	215.
GeneCards	GC0XP152990.
HGNC	HGNC:61. ABCD1.
MIM	300100. phenotype. 300371. gene.
neXtProt	NX_P33897.
Orphanet	139399. Adrenomyeloneuropathy. 139396. X-linked cerebral adrenoleukodystrophy.
PharmGKB	PA24396.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4178.
HOGENOM	HOG000206081.
HOVERGEN	HBG050438.
InParanoid	P33897.
KO	K05675.
OMA	DVAVTAY.
OrthoDB	EOG4DFPMX.
PhylomeDB	P33897.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	P33897.
Bgee	P33897.
CleanEx	HS_ABCD1.
Genevestigator	P33897.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR010509. ABC_Ald_N. IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. IPR017940. ABC_transporter_type1. IPR005283. FA_transporter. [Graphical view]
Pfam	PF06472. ABC_membrane_2. 1 hit. PF00005. ABC_tran. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00954. 3a01203. 1 hit.
PROSITE	PS50929. ABC_TM1F. 1 hit. PS00211. ABC_TRANSPORTER_1. 1 hit. PS50893. ABC_TRANSPORTER_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	215.
NextBio	870.
SOURCE	Search...

Entry information

Entry name

ABCD1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 154 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.