P41233 (ABCA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
ATP-binding cassette transporter 1
Short name=ABC-1
Short name=ATP-binding cassette 1

Gene names

Name:	Abca1
Synonyms:	Abc1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2261 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	cAMP-dependent and sulfonylurea-sensitive anion transporter. Key gatekeeper influencing intracellular cholesterol transport By similarity.
Subunit structure	Interacts with MEGF10. Ref.7
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Tissue specificity	Widely expressed in adult tissues. Highest levels are found in pregnant uterus and uterus.
Induction	Down-regulated by endotoxins (LPS) or cytokines (TNF and IL-1) in J774 macrophages. The down-regulation by endotoxin in macrophages is not likely to be mediated by the liver X receptor/retinoic X receptor (LXR/RXR). Ref.5 Ref.6
Domain	Multifunctional polypeptide with two homologous halves, each containing a hydrophobic membrane-anchoring domain and an ATP binding cassette (ABC) domain.
Post-translational modification	Phosphorylation on Ser-2054 regulates phospholipid efflux By similarity. Palmitoylation by DHHC8 is essential for membrane localization By similarity.
Sequence similarities	Belongs to the ABC transporter superfamily. ABCA family. Contains 2 ABC transporter domains.
Sequence caution	The sequence AAG39073.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA53530.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transport
Cellular component	Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara cellular response to lipopolysaccharide Inferred from direct assay PubMed 19752193. Source: UniProtKB cellular response to retinoic acid Inferred from direct assay PubMed 19752193. Source: UniProtKB cholesterol efflux Inferred from direct assay PubMed 12869555PubMed 15520449. Source: MGI cholesterol homeostasis Inferred from electronic annotation. Source: Compara cholesterol metabolic process Inferred from direct assay PubMed 11559713. Source: MGI endosomal transport Inferred from electronic annotation. Source: Compara high-density lipoprotein particle assembly Inferred from electronic annotation. Source: Compara interleukin-1 beta secretion Inferred from electronic annotation. Source: Compara intracellular cholesterol transport Inferred from electronic annotation. Source: Compara lysosome organization Inferred from electronic annotation. Source: Compara peptide secretion Inferred from mutant phenotype PubMed 15269218. Source: MGI phagocytosis, engulfment Inferred from mutant phenotype PubMed 10878804. Source: MGI phospholipid efflux Inferred from direct assay PubMed 15520449. Source: MGI phospholipid homeostasis Inferred from electronic annotation. Source: Compara phospholipid translocation Inferred from mutant phenotype PubMed 10878804. Source: MGI platelet dense granule organization Inferred from electronic annotation. Source: Compara positive regulation of cAMP biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of cholesterol efflux Inferred from mutant phenotype PubMed 15210959. Source: BHF-UCL protein lipidation Inferred from mutant phenotype PubMed 16204232. Source: MGI regulation of Cdc42 protein signal transduction Inferred from electronic annotation. Source: Compara response to laminar fluid shear stress Inferred from electronic annotation. Source: Compara response to low-density lipoprotein particle stimulus Inferred from electronic annotation. Source: Compara reverse cholesterol transport Inferred from mutant phenotype PubMed 17657311. Source: BHF-UCL
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 10878804. Source: MGI integral to plasma membrane Inferred from direct assay PubMed 10878804. Source: MGI membrane raft Inferred from electronic annotation. Source: Compara phagocytic vesicle Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from electronic annotation. Source: InterPro anion transmembrane transporter activity Inferred from direct assay PubMed 9006906. Source: BHF-UCL apolipoprotein A-I receptor activity Inferred from electronic annotation. Source: Compara cholesterol transporter activity Inferred from direct assay PubMed 15520449. Source: MGI phospholipid transporter activity Inferred from direct assay PubMed 15520449. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2261	2261	ATP-binding cassette sub-family A member 1		PRO_0000093289
Regions
	Transmembrane	22 – 42	21	Helical; Potential
	Topological domain	43 – 639	597	Extracellular By similarity
	Transmembrane	640 – 660	21	Helical; Potential
	Transmembrane	683 – 703	21	Helical; Potential
	Transmembrane	716 – 736	21	Helical; Potential
	Transmembrane	745 – 765	21	Helical; Potential
	Transmembrane	777 – 797	21	Helical; Potential
	Transmembrane	827 – 847	21	Helical; Potential
	Transmembrane	941 – 961	21	Helical; Potential
	Transmembrane	1351 – 1371	21	Helical; Potential
	Topological domain	1372 – 1656	285	Extracellular By similarity
	Transmembrane	1657 – 1677	21	Helical; Potential
	Transmembrane	1703 – 1723	21	Helical; Potential
	Transmembrane	1735 – 1755	21	Helical; Potential
	Transmembrane	1768 – 1788	21	Helical; Potential
	Transmembrane	1802 – 1822	21	Helical; Potential
	Transmembrane	1852 – 1872	21	Helical; Potential
	Domain	899 – 1131	233	ABC transporter 1
	Domain	1912 – 2144	233	ABC transporter 2
	Nucleotide binding	933 – 940	8	ATP 1 Potential
	Nucleotide binding	1946 – 1953	8	ATP 2 Potential
Amino acid modifications
	Modified residue	1042	1	Phosphoserine; by PKA By similarity
	Modified residue	1141	1	Phosphoserine Ref.8
	Modified residue	1147	1	Phosphoserine Ref.8
	Modified residue	2054	1	Phosphoserine; by PKA By similarity
	Lipidation	3	1	S-palmitoyl cysteine By similarity
	Lipidation	23	1	S-palmitoyl cysteine By similarity
	Lipidation	1110	1	S-palmitoyl cysteine By similarity
	Lipidation	1111	1	S-palmitoyl cysteine By similarity
	Glycosylation	14	1	N-linked (GlcNAc...) Potential
	Glycosylation	98	1	N-linked (GlcNAc...) Potential
	Glycosylation	151	1	N-linked (GlcNAc...) Potential
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
	Glycosylation	196	1	N-linked (GlcNAc...) Potential
	Glycosylation	244	1	N-linked (GlcNAc...) Potential
	Glycosylation	292	1	N-linked (GlcNAc...) Potential
	Glycosylation	337	1	N-linked (GlcNAc...) Potential
	Glycosylation	349	1	N-linked (GlcNAc...) Potential
	Glycosylation	400	1	N-linked (GlcNAc...) Potential
	Glycosylation	478	1	N-linked (GlcNAc...) Potential
	Glycosylation	489	1	N-linked (GlcNAc...) Ref.9
	Glycosylation	521	1	N-linked (GlcNAc...) Potential
	Glycosylation	820	1	N-linked (GlcNAc...) Potential
	Glycosylation	1144	1	N-linked (GlcNAc...) Potential
	Glycosylation	1294	1	N-linked (GlcNAc...) Potential
	Glycosylation	1453	1	N-linked (GlcNAc...) Potential
	Glycosylation	1499	1	N-linked (GlcNAc...) Potential
	Glycosylation	1504	1	N-linked (GlcNAc...) Potential
	Glycosylation	1637	1	N-linked (GlcNAc...) Potential
	Glycosylation	2044	1	N-linked (GlcNAc...) Potential
	Glycosylation	2238	1	N-linked (GlcNAc...) Potential
	Disulfide bond	75 ↔ 309		By similarity
	Disulfide bond	1463 ↔ 1477		By similarity
Experimental info
	Sequence conflict	1567 – 1568	2	Missing in AAG39073. Ref.2
	Sequence conflict	1568	1	S → T in CAA53530. Ref.1
	Sequence conflict	2024	1	V → F in CAA53530. Ref.1
	Sequence conflict	2024	1	Missing in AAG39073. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P41233 [UniParc]. Last modified July 27, 2011. Version 4. Checksum: E041DA4FA73C2660	FASTA	2,261	253,912
	10 20 30 40 50 60 MACWPQLRLL LWKNLTFRRR QTCQLLLEVA WPLFIFLILI SVRLSYPPYE QHECHFPNKA 70 80 90 100 110 120 MPSAGTLPWV QGIICNANNP CFRYPTPGEA PGVVGNFNKS IVSRLFSDAQ RLLLYSQRDT 130 140 150 160 170 180 SIKDMHKVLR MLRQIKHPNS NLKLQDFLVD NETFSGFLQH NLSLPRSTVD SLLQANVGLQ 190 200 210 220 230 240 KVFLQGYQLH LASLCNGSKL EEIIQLGDAE VSALCGLPRK KLDAAERVLR YNMDILKPVV 250 260 270 280 290 300 TKLNSTSHLP TQHLAEATTV LLDSLGGLAQ ELFSTKSWSD MRQEVMFLTN VNSSSSSTQI 310 320 330 340 350 360 YQAVSRIVCG HPEGGGLKIK SLNWYEDNNY KALFGGNNTE EDVDTFYDNS TTPYCNDLMK 370 380 390 400 410 420 NLESSPLSRI IWKALKPLLV GKILYTPDTP ATRQVMAEVN KTFQELAVFH DLEGMWEELS 430 440 450 460 470 480 PQIWTFMENS QEMDLVRTLL DSRGNDQFWE QKLDGLDWTA QDIMAFLAKN PEDVQSPNGS 490 500 510 520 530 540 VYTWREAFNE TNQAIQTISR FMECVNLNKL EPIPTEVRLI NKSMELLDER KFWAGIVFTG 550 560 570 580 590 600 ITPDSVELPH HVKYKIRMDI DNVERTNKIK DGYWDPGPRA DPFEDMRYVW GGFAYLQDVV 610 620 630 640 650 660 EQAIIRVLTG SEKKTGVYVQ QMPYPCYVDD IFLRVMSRSM PLFMTLAWIY SVAVIIKSIV 670 680 690 700 710 720 YEKEARLKET MRIMGLDNGI LWFSWFVSSL IPLLVSAGLL VVILKLGNLL PYSDPSVVFV 730 740 750 760 770 780 FLSVFAMVTI LQCFLISTLF SRANLAAACG GIIYFTLYLP YVLCVAWQDY VGFSIKIFAS 790 800 810 820 830 840 LLSPVAFGFG CEYFALFEEQ GIGVQWDNLF ESPVEEDGFN LTTAVSMMLF DTFLYGVMTW 850 860 870 880 890 900 YIEAVFPGQY GIPRPWYFPC TKSYWFGEEI DEKSHPGSSQ KGVSEICMEE EPTHLRLGVS 910 920 930 940 950 960 IQNLVKVYRD GMKVAVDGLA LNFYEGQITS FLGHNGAGKT TTMSILTGLF PPTSGTAYIL 970 980 990 1000 1010 1020 GKDIRSEMSS IRQNLGVCPQ HNVLFDMLTV EEHIWFYARL KGLSEKHVKA EMEQMALDVG 1030 1040 1050 1060 1070 1080 LPPSKLKSKT SQLSGGMQRK LSVALAFVGG SKVVILDEPT AGVDPYSRRG IWELLLKYRQ 1090 1100 1110 1120 1130 1140 GRTIILSTHH MDEADILGDR IAIISHGKLC CVGSSLFLKN QLGTGYYLTL VKKDVESSLS 1150 1160 1170 1180 1190 1200 SCRNSSSTVS CLKKEDSVSQ SSSDAGLGSD HESDTLTIDV SAISNLIRKH VSEARLVEDI 1210 1220 1230 1240 1250 1260 GHELTYVLPY EAAKEGAFVE LFHEIDDRLS DLGISSYGIS ETTLEEIFLK VAEESGVDAE 1270 1280 1290 1300 1310 1320 TSDGTLPARR NRRAFGDKQS CLHPFTEDDA VDPNDSDIDP ESRETDLLSG MDGKGSYQLK 1330 1340 1350 1360 1370 1380 GWKLTQQQFV ALLWKRLLIA RRSRKGFFAQ IVLPAVFVCI ALVFSLIVPP FGKYPSLELQ 1390 1400 1410 1420 1430 1440 PWMYNEQYTF VSNDAPEDMG TQELLNALTK DPGFGTRCME GNPIPDTPCL AGEEDWTISP 1450 1460 1470 1480 1490 1500 VPQSIVDLFQ NGNWTMKNPS PACQCSSDKI KKMLPVCPPG AGGLPPPQRK QKTADILQNL 1510 1520 1530 1540 1550 1560 TGRNISDYLV KTYVQIIAKS LKNKIWVNEF RYGGFSLGVS NSQALPPSHE VNDAIKQMKK 1570 1580 1590 1600 1610 1620 LLKLTKDSSA DRFLSSLGRF MAGLDTKNNV KVWFNNKGWH AISSFLNVIN NAILRANLQK 1630 1640 1650 1660 1670 1680 GENPSQYGIT AFNHPLNLTK QQLSEVALMT TSVDVLVSIC VIFAMSFVPA SFVVFLIQER 1690 1700 1710 1720 1730 1740 VSKAKHLQFI SGVKPVIYWL SNFVWDMCNY VVPATLVIII FICFQQKSYV SSTNLPVLAL 1750 1760 1770 1780 1790 1800 LLLLYGWSIT PLMYPASFVF KIPSTAYVVL TSVNLFIGIN GSVATFVLEL FTNNKLNDIN 1810 1820 1830 1840 1850 1860 DILKSVFLIF PHFCLGRGLI DMVKNQAMAD ALERFGENRF VSPLSWDLVG RNLFAMAVEG 1870 1880 1890 1900 1910 1920 VVFFLITVLI QYRFFIRPRP VKAKLPPLND EDEDVRRERQ RILDGGGQND ILEIKELTKI 1930 1940 1950 1960 1970 1980 YRRKRKPAVD RICIGIPPGE CFGLLGVNGA GKSTTFKMLT GDTPVTRGDA FLNKNSILSN 1990 2000 2010 2020 2030 2040 IHEVHQNMGY CPQFDAITEL LTGREHVEFF ALLRGVPEKE VGKVGEWAIR KLGLVKYGEK 2050 2060 2070 2080 2090 2100 YASNYSGGNK RKLSTAMALI GGPPVVFLDE PTTGMDPKAR RFLWNCALSI VKEGRSVVLT 2110 2120 2130 2140 2150 2160 SHSMEECEAL CTRMAIMVNG RFRCLGSVQH LKNRFGDGYT IVVRIAGSNP DLKPVQEFFG 2170 2180 2190 2200 2210 2220 LAFPGSVLKE KHRNMLQYQL PSSLSSLARI FSILSQSKKR LHIEDYSVSQ TTLDQVFVNF 2230 2240 2250 2260 AKDQSDDDHL KDLSLHKNQT VVDVAVLTSF LQDEKVKESY V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of two novel ABC transporters mapping on human chromosome 9." Luciani M.-F., Denizot F., Savary S., Mattei M.-G., Chimini G. Genomics 21:150-159(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: DBA/2. Tissue: Macrophage.
[2]	"Human and mouse ABCA1 comparative sequencing and transgenesis studies revealing novel regulatory sequences." Qiu Y., Cavelier L., Chiu S., Yang X., Rubin E., Cheng J.-F. Genomics 73:66-76(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C57BL/6J.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Bacterial lipopolysaccharide induces expression of ABCA1 but not ABCG1 via an LXR-independent pathway." Kaplan R., Gan X., Menke J.G., Wright S.D., Cai T.-Q. J. Lipid Res. 43:952-959(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY LIPOPOLYSACCHARIDE.
[6]	"Endotoxin down-regulates ABCG5 and ABCG8 in mouse liver and ABCA1 and ABCG1 in J774 murine macrophages: differential role of LXR." Khovidhunkit W., Moser A.H., Shigenaga J.K., Grunfeld C., Feingold K.R. J. Lipid Res. 44:1728-1736(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DOWN-REGULATION BY ENDOTOXIN.
[7]	"Cooperation between engulfment receptors: the case of ABCA1 and MEGF10." Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V., Zhou Z., Chimini G. PLoS ONE 1:E120-E120(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MEGF10.
[8]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1141 AND SER-1147, MASS SPECTROMETRY. Tissue: Liver.
[9]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-489, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75926 mRNA. Translation: CAA53530.1. Different initiation. AF287263 Genomic DNA. Translation: AAG39073.1. Different initiation. AL807243, AL772397 Genomic DNA. Translation: CAM18883.1. AL772397, AL807243 Genomic DNA. Translation: CAM27437.1. CH466565 Genomic DNA. Translation: EDL02285.1.
IPI	IPI00112614.
PIR	A54774.
RefSeq	NP_038482.3. NM_013454.3.
UniGene	Mm.277376.
3D structure databases
ProteinModelPortal	P41233.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000030010.
Protein family/group databases
TCDB	3.A.1.211.1. ATP-binding cassette (ABC) superfamily.
PTM databases
PhosphoSite	P41233.
Proteomic databases
PaxDb	P41233.
PRIDE	P41233.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030010; ENSMUSP00000030010; ENSMUSG00000015243.
GeneID	11303.
KEGG	mmu:11303.
Organism-specific databases
CTD	19.
MGI	MGI:99607. Abca1.
Phylogenomic databases
eggNOG	COG1131.
GeneTree	ENSGT00700000104253.
HOGENOM	HOG000231547.
HOVERGEN	HBG050436.
InParanoid	B1AWZ8.
KO	K05641.
OMA	EEEWTTA.
OrthoDB	EOG44F686.
Gene expression databases
Bgee	P41233.
Genevestigator	P41233.
GermOnline	ENSMUSG00000015243. Mus musculus.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR026082. ABC_A. IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. [Graphical view]
PANTHER	PTHR19229. PTHR19229. 1 hit.
Pfam	PF00005. ABC_tran. 2 hits. [Graphical view]
SMART	SM00382. AAA. 2 hits. [Graphical view]
PROSITE	PS00211. ABC_TRANSPORTER_1. 1 hit. PS50893. ABC_TRANSPORTER_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1641361.
NextBio	278586.
PMAP-CutDB	B1AWZ8.
SOURCE	Search...

Entry information

Entry name

ABCA1_MOUSE

Accession

Primary (citable) accession number: P41233
Secondary accession number(s): B1AWZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 128 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program