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P41233 (ABCA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2261 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processTransport
   Cellular componentMembrane
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

cellular response to cholesterol

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

cholesterol metabolic process

Inferred from direct assay PubMed 11559713. Source: MGI

endosomal transport

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle assembly

Inferred from electronic annotation. Source: Ensembl

interleukin-1 beta secretion

Inferred from electronic annotation. Source: Ensembl

intracellular cholesterol transport

Inferred from electronic annotation. Source: Ensembl

lipoprotein biosynthetic process

Inferred from mutant phenotype PubMed 12859204PubMed 15520446. Source: MGI

lipoprotein metabolic process

Inferred from mutant phenotype PubMed 15269218. Source: MGI

lysosome organization

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

phospholipid translocation

Inferred from mutant phenotype PubMed 10878804. Source: MGI

platelet dense granule organization

Inferred from electronic annotation. Source: Ensembl

positive regulation of cAMP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to laminar fluid shear stress

Inferred from electronic annotation. Source: Ensembl

response to low-density lipoprotein particle

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

reverse cholesterol transport

Inferred from mutant phenotype PubMed 17657311. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 10878804. Source: MGI

external side of plasma membrane

Inferred from direct assay PubMed 23931754. Source: MGI

integral component of plasma membrane

Inferred from direct assay PubMed 10878804. Source: MGI

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 10878804. Source: MGI

membrane raft

Inferred from electronic annotation. Source: Ensembl

phagocytic vesicle

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 12869555PubMed 15520449. Source: MGI

   Molecular_functionATP 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: Ensembl

cholesterol transporter activity

Inferred from direct assay PubMed 15520449. Source: MGI

phospholipid transporter activity

Inferred from direct assay PubMed 15520449. Source: MGI

protein binding

Inferred from physical interaction PubMed 16204232PubMed 23931754PubMed 8751592. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22612261ATP-binding cassette sub-family A member 1
PRO_0000093289

Regions

Transmembrane22 – 4221Helical; Potential
Topological domain43 – 639597Extracellular By similarity
Transmembrane640 – 66021Helical; Potential
Transmembrane683 – 70321Helical; Potential
Transmembrane716 – 73621Helical; Potential
Transmembrane745 – 76521Helical; Potential
Transmembrane777 – 79721Helical; Potential
Transmembrane827 – 84721Helical; Potential
Transmembrane941 – 96121Helical; Potential
Transmembrane1351 – 137121Helical; Potential
Topological domain1372 – 1656285Extracellular By similarity
Transmembrane1657 – 167721Helical; Potential
Transmembrane1703 – 172321Helical; Potential
Transmembrane1735 – 175521Helical; Potential
Transmembrane1768 – 178821Helical; Potential
Transmembrane1802 – 182221Helical; Potential
Transmembrane1852 – 187221Helical; Potential
Domain899 – 1131233ABC transporter 1
Domain1912 – 2144233ABC transporter 2
Nucleotide binding933 – 9408ATP 1 Potential
Nucleotide binding1946 – 19538ATP 2 Potential

Amino acid modifications

Modified residue10421Phosphoserine; by PKA By similarity
Modified residue12961Phosphoserine Ref.8
Modified residue20541Phosphoserine; by PKA By similarity
Lipidation31S-palmitoyl cysteine By similarity
Lipidation231S-palmitoyl cysteine By similarity
Lipidation11101S-palmitoyl cysteine By similarity
Lipidation11111S-palmitoyl cysteine By similarity
Glycosylation141N-linked (GlcNAc...) Potential
Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation1511N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation2441N-linked (GlcNAc...) Potential
Glycosylation2921N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation3491N-linked (GlcNAc...) Potential
Glycosylation4001N-linked (GlcNAc...) Potential
Glycosylation4781N-linked (GlcNAc...) Potential
Glycosylation4891N-linked (GlcNAc...) Ref.9
Glycosylation5211N-linked (GlcNAc...) Potential
Glycosylation8201N-linked (GlcNAc...) Potential
Glycosylation11441N-linked (GlcNAc...) Potential
Glycosylation12941N-linked (GlcNAc...) Potential
Glycosylation14531N-linked (GlcNAc...) Potential
Glycosylation14991N-linked (GlcNAc...) Potential
Glycosylation15041N-linked (GlcNAc...) Potential
Glycosylation16371N-linked (GlcNAc...) Potential
Glycosylation20441N-linked (GlcNAc...) Potential
Glycosylation22381N-linked (GlcNAc...) Potential
Disulfide bond75 ↔ 309 By similarity
Disulfide bond1463 ↔ 1477 By similarity

Experimental info

Sequence conflict1567 – 15682Missing in AAG39073. Ref.2
Sequence conflict15681S → T in CAA53530. Ref.1
Sequence conflict20241V → F in CAA53530. Ref.1
Sequence conflict20241Missing in AAG39073. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P41233 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: E041DA4FA73C2660

FASTA2,261253,912
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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-1296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
+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.
CCDSCCDS18187.1.
PIRA54774.
RefSeqNP_038482.3. NM_013454.3.
UniGeneMm.277376.

3D structure databases

ProteinModelPortalP41233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197900. 2 interactions.
STRING10090.ENSMUSP00000030010.

Chemistry

ChEMBLCHEMBL1641361.

Protein family/group databases

TCDB3.A.1.211.1. the atp-binding cassette (abc) superfamily.

PTM databases

PhosphoSiteP41233.

Proteomic databases

MaxQBP41233.
PaxDbP41233.
PRIDEP41233.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030010; ENSMUSP00000030010; ENSMUSG00000015243.
GeneID11303.
KEGGmmu:11303.
UCSCuc008swu.1. mouse.

Organism-specific databases

CTD19.
MGIMGI:99607. Abca1.

Phylogenomic databases

eggNOGCOG1131.
GeneTreeENSGT00720000108414.
HOGENOMHOG000231547.
HOVERGENHBG050436.
InParanoidB1AWZ8.
KOK05641.
OMAFSMRSWS.
OrthoDBEOG78D7J6.
TreeFamTF105191.

Gene expression databases

BgeeP41233.
GenevestigatorP41233.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR026082. ABC_A.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR19229. PTHR19229. 1 hit.
PfamPF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00211. ABC_TRANSPORTER_1. 1 hit.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio278586.
PMAP-CutDBB1AWZ8.
PROP41233.
SOURCESearch...

Entry information

Entry nameABCA1_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot