Q9UBJ2 (ABCD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-binding cassette sub-family D member 2

Alternative name(s):
Adrenoleukodystrophy-like 1
Adrenoleukodystrophy-related protein
Short name=hALDR

Gene names

Name:	ABCD2
Synonyms:	ALD1, ALDL1, ALDR, ALDRP

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	740 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable transporter.
Subunit structure	Can form heterodimers with ABCD1/ALD and ABCD3/PMP70. Dimerization is necessary to form an active transporter. Interacts with PEX19. Ref.7 Ref.8 Ref.9
Subcellular location	Peroxisome membrane; Multi-pass membrane protein.
Tissue specificity	Predominantly expressed in brain and heart.
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
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC fatty acid beta-oxidation Inferred from genetic interaction PubMed 21145416. Source: UniProtKB positive regulation of fatty acid beta-oxidation Inferred from direct assay PubMed 10196381. Source: UniProtKB transmembrane transport Traceable author statement. Source: Reactome very long-chain fatty acid catabolic process Inferred from genetic interaction PubMed 21145416. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from electronic annotation. Source: Compara peroxisomal membrane Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from electronic annotation. Source: InterPro protein homodimerization activity Inferred from direct assay PubMed 21145416. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 740	740	ATP-binding cassette sub-family D member 2		PRO_0000093306
Regions
	Transmembrane	107 – 127	21	Helical; Potential
	Transmembrane	144 – 164	21	Helical; Potential
	Transmembrane	251 – 271	21	Helical; Potential
	Transmembrane	351 – 371	21	Helical; Potential
	Domain	107 – 399	293	ABC transmembrane type-1
	Domain	478 – 704	227	ABC transporter
	Nucleotide binding	511 – 518	8	ATP Potential
	Region	1 – 218	218	Interaction with PEX19
Amino acid modifications
	Glycosylation	190	1	N-linked (GlcNAc...) Potential
	Glycosylation	227	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	244	1	Q → K in a pancreatic ductal adenocarcinoma sample; somatic mutation. Ref.10		VAR_062664
Experimental info
	Sequence conflict	18	1	S → G in AAB00541. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9UBJ2 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 9F3C8DBB8AB156E3	FASTA	740	83,233
	10 20 30 40 50 60 MTHMLNAAAD RVKWTRSSAA KRAACLVAAA YALKTLYPII GKRLKQSGHG KKKAAAYPAA 70 80 90 100 110 120 ENTEILHCTE TICEKPSPGV NADFFKQLLE LRKILFPKLV TTETGWLCLH SVALISRTFL 130 140 150 160 170 180 SIYVAGLDGK IVKSIVEKKP RTFIIKLIKW LMIAIPATFV NSAIRYLECK LALAFRTRLV 190 200 210 220 230 240 DHAYETYFTN QTYYKVINMD GRLANPDQSL TEDIMMFSQS VAHLYSNLTK PILDVMLTSY 250 260 270 280 290 300 TLIQTATSRG ASPIGPTLLA GLVVYATAKV LKACSPKFGK LVAEEAHRKG YLRYVHSRII 310 320 330 340 350 360 ANVEEIAFYR GHKVEMKQLQ KSYKALADQM NLILSKRLWY IMIEQFLMKY VWSSSGLIMV 370 380 390 400 410 420 AIPIITATGF ADGEDGQKQV MVSERTEAFT TARNLLASGA DAIERIMSSY KEVTELAGYT 430 440 450 460 470 480 ARVYNMFWVF DEVKRGIYKR TAVIQESESH SKNGAKVELP LSDTLAIKGK VIDVDHGIIC 490 500 510 520 530 540 ENVPIITPAG EVVASRLNFK VEEGMHLLIT GPNGCGKSSL FRILSGLWPV YEGVLYKPPP 550 560 570 580 590 600 QHMFYIPQRP YMSLGSLRDQ VIYPDSVDDM HDKGYTDQDL ERILHNVHLY HIVQREGGWD 610 620 630 640 650 660 AVMDWKDVLS GGEKQRMGMA RMFYHKPKYA LLDECTSAVS IDVEGKIFQA AKGAGISLLS 670 680 690 700 710 720 ITHRPSLWKY HTHLLQFDGE GGWRFEQLDT AIRLTLSEEK QKLESQLAGI PKMQQRLNEL 730 740 CKILGEDSVL KTIKNEDETS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A close relative of the adrenoleukodystrophy (ALD) gene codes for a peroxisomal protein with a specific expression pattern." Lombard-Platet G., Savary S., Sarde C.-O., Mandel J.-L., Chimini G. Proc. Natl. Acad. Sci. U.S.A. 93:1265-1269(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"cDNA cloning and mRNA expression of the human adrenoleukodystrophy related protein (ALDRP), a peroxisomal ABC transporter." Holzinger A., Kammerer S., Berger J., Roscher A.A. Biochem. Biophys. Res. Commun. 239:261-264(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Full length cDNA cloning, promoter sequence, and genomic organization of the human adrenoleukodystrophy related (ALDR) gene functionally redundant to the gene responsible for X-linked adrenoleukodystrophy." Holzinger A., Mayerhofer P., Berger J., Lichtner P., Kammerer S., Roscher A.A. Biochem. Biophys. Res. Commun. 258:436-442(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHARACTERIZATION.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Trachea.
[5]	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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Liver.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"Core signaling pathways in human pancreatic cancers revealed by global genomic analyses." Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P., Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., Nikolsky Y. , Hartigan J., Smith D.R., Hidalgo M., Leach S.D., Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C., Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N., Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W. Science 321:1801-1806(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-244.
+	Additional computationally mapped references.

Web resources

ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases
EMBL GenBank DDBJ	U28150 Genomic DNA. Translation: AAB00541.1. AJ000327 mRNA. Translation: CAA03994.1. AF119831 , AF119822, AF119823, AF119824, AF119826, AF119825, AF119827, AF119828, AF119829, AF119830 Genomic DNA. Translation: AAD30439.1. AK314254 mRNA. Translation: BAG36920.1. CH471111 Genomic DNA. Translation: EAW57807.1. BC104901 mRNA. Translation: AAI04902.1. BC104903 mRNA. Translation: AAI04904.1.
IPI	IPI00002618.
PIR	JC5712.
RefSeq	NP_005155.1. NM_005164.3.
UniGene	Hs.117852.
3D structure databases
ProteinModelPortal	Q9UBJ2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UBJ2. 1 interaction.
STRING	9606.ENSP00000310688.
Protein family/group databases
TCDB	3.A.1.203.7. ATP-binding cassette (ABC) superfamily.
PTM databases
PhosphoSite	Q9UBJ2.
Polymorphism databases
DMDM	12643305.
Proteomic databases
PaxDb	Q9UBJ2.
PRIDE	Q9UBJ2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000308666; ENSP00000310688; ENSG00000173208.
GeneID	225.
KEGG	hsa:225.
UCSC	uc001rmb.2. human.
Organism-specific databases
CTD	225.
GeneCards	GC12M039945.
HGNC	HGNC:66. ABCD2.
HPA	HPA040336.
MIM	601081. gene.
neXtProt	NX_Q9UBJ2.
PharmGKB	PA24401.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4178.
HOGENOM	HOG000206081.
HOVERGEN	HBG050438.
InParanoid	Q9UBJ2.
KO	K05676.
OMA	YETYFAN.
OrthoDB	EOG4DFPMX.
PhylomeDB	Q9UBJ2.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
Bgee	Q9UBJ2.
CleanEx	HS_ABCD2.
Genevestigator	Q9UBJ2.
GermOnline	ENSG00000173208. Homo sapiens.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR010509. ABC_Ald_N. IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. IPR017940. ABC_transporter_type1. [Graphical view]
Pfam	PF06472. ABC_membrane_2. 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
GenomeRNAi	225.
NextBio	916.
SOURCE	Search...

Entry information

Entry name

ABCD2_HUMAN

Accession

Primary (citable) accession number: Q9UBJ2
Secondary accession number(s): B2RAM3, Q13210, Q2M3H9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 118 of the entry and version 1 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.