Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00822
Entry Name
UniProt Accession
Theoretical PI
6.43
Molecular Weight
254302.1
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
ATP-binding cassette sub-family A member 1
Protein Synonyms/Alias
ATP-binding cassette transporter 1; ABC-1; ATP-binding cassette 1; Cholesterol efflux regulatory protein;
Gene Name
ABCA1
Gene Synonyms/Alias
ABC1; CERP;
Created Date
01-DEC-2000
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
3
Canonical
*****MACWPQLRLL
[1]
S-Palmitoylation
23
Canonical
TFRRRQTCQLLLEVA
[1]
S-Palmitoylation
1110
Canonical
IISHGKLCCVGSSLF
[1]
S-Palmitoylation
1111
Canonical
ISHGKLCCVGSSLFL
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Singaraja RR, Kang MH, Vaid K, Sanders SS, Vilas GL, Arstikaitis P, CoutinhoJ, Drisdel RC, El-Husseini Ael D, Green WN, Berthiaume L, Hayden MR.Palmitoylation of ATP-binding cassette transporter A1 is essential for itstrafficking and function. Circ Res. 2009 Jul 17;105(2):138-47. doi:10.1161/CIRCRESAHA.108.193011. Epub 2009 Jun 25.[PMID:19556522]
Functional Description
cAMP-dependent and sulfonylurea-sensitive anion transporter. Key gatekeeper influencing intracellular cholesterol transport.
Sequence Annotation
Transmembrane: 22 42 Helical.
Topological domain: 43 639 Extracellular.
Transmembrane: 640 660 Helical.
Transmembrane: 683 703 Helical.
Transmembrane: 716 736 Helical.
Transmembrane: 745 765 Helical.
Transmembrane: 777 797 Helical.
Transmembrane: 827 847 Helical.
Transmembrane: 1041 1057 Helical.
Transmembrane: 1351 1371 Helical.
Topological domain: 1372 1656 Extracellular.
Transmembrane: 1657 1677 Helical.
Transmembrane: 1703 1723 Helical.
Transmembrane: 1735 1755 Helical.
Transmembrane: 1768 1788 Helical.
Transmembrane: 1802 1822 Helical.
Transmembrane: 1852 1872 Helical.
Domain: 899 1131 ABC transporter 1.
Domain: 1912 2144 ABC transporter 2.
Nucleotide-binding: 933 940 ATP 1.
Nucleotide-binding: 1946 1953 ATP 2.
Modified residue: 1042 1042 Phosphoserine; by PKA.
Modified residue: 1296 1296 Phosphoserine.
Modified residue: 2054 2054 Phosphoserine; by PKA.
Protein Length
2261 AA.
Protein Sequence
(Canonical)
MACWPQLRLL LWKNLTFRRR QTCQLLLEVA WPLFIFLILI SVRLSYPPYE QHECHFPNKA  60
MPSAGTLPWV QGIICNANNP CFRYPTPGEA PGVVGNFNKS IVARLFSDAR RLLLYSQKDT  120
SMKDMRKVLR TLQQIKKSSS NLKLQDFLVD NETFSGFLYH NLSLPKSTVD KMLRADVILH  180
KVFLQGYQLH LTSLCNGSKS EEMIQLGDQE VSELCGLPRE KLAAAERVLR SNMDILKPIL  240
RTLNSTSPFP SKELAEATKT LLHSLGTLAQ ELFSMRSWSD MRQEVMFLTN VNSSSSSTQI  300
YQAVSRIVCG HPEGGGLKIK SLNWYEDNNY KALFGGNGTE EDAETFYDNS TTPYCNDLMK  360
NLESSPLSRI IWKALKPLLV GKILYTPDTP ATRQVMAEVN KTFQELAVFH DLEGMWEELS  420
PKIWTFMENS QEMDLVRMLL DSRDNDHFWE QQLDGLDWTA QDIVAFLAKH PEDVQSSNGS  480
VYTWREAFNE TNQAIRTISR FMECVNLNKL EPIATEVWLI NKSMELLDER KFWAGIVFTG  540
ITPGSIELPH HVKYKIRMDI DNVERTNKIK DGYWDPGPRA DPFEDMRYVW GGFAYLQDVV  600
EQAIIRVLTG TEKKTGVYMQ QMPYPCYVDD IFLRVMSRSM PLFMTLAWIY SVAVIIKGIV  660
YEKEARLKET MRIMGLDNSI LWFSWFISSL IPLLVSAGLL VVILKLGNLL PYSDPSVVFV  720
FLSVFAVVTI LQCFLISTLF SRANLAAACG GIIYFTLYLP YVLCVAWQDY VGFTLKIFAS  780
LLSPVAFGFG CEYFALFEEQ GIGVQWDNLF ESPVEEDGFN LTTSVSMMLF DTFLYGVMTW  840
YIEAVFPGQY GIPRPWYFPC TKSYWFGEES DEKSHPGSNQ KRISEICMEE EPTHLKLGVS  900
IQNLVKVYRD GMKVAVDGLA LNFYEGQITS FLGHNGAGKT TTMSILTGLF PPTSGTAYIL  960
GKDIRSEMST IRQNLGVCPQ HNVLFDMLTV EEHIWFYARL KGLSEKHVKA EMEQMALDVG  1020
LPSSKLKSKT SQLSGGMQRK LSVALAFVGG SKVVILDEPT AGVDPYSRRG IWELLLKYRQ  1080
GRTIILSTHH MDEADVLGDR IAIISHGKLC CVGSSLFLKN QLGTGYYLTL VKKDVESSLS  1140
SCRNSSSTVS YLKKEDSVSQ SSSDAGLGSD HESDTLTIDV SAISNLIRKH VSEARLVEDI  1200
GHELTYVLPY EAAKEGAFVE LFHEIDDRLS DLGISSYGIS ETTLEEIFLK VAEESGVDAE  1260
TSDGTLPARR NRRAFGDKQS CLRPFTEDDA ADPNDSDIDP ESRETDLLSG MDGKGSYQVK  1320
GWKLTQQQFV ALLWKRLLIA RRSRKGFFAQ IVLPAVFVCI ALVFSLIVPP FGKYPSLELQ  1380
PWMYNEQYTF VSNDAPEDTG TLELLNALTK DPGFGTRCME GNPIPDTPCQ AGEEEWTTAP  1440
VPQTIMDLFQ NGNWTMQNPS PACQCSSDKI KKMLPVCPPG AGGLPPPQRK QNTADILQDL  1500
TGRNISDYLV KTYVQIIAKS LKNKIWVNEF RYGGFSLGVS NTQALPPSQE VNDAIKQMKK  1560
HLKLAKDSSA DRFLNSLGRF MTGLDTKNNV KVWFNNKGWH AISSFLNVIN NAILRANLQK  1620
GENPSHYGIT AFNHPLNLTK QQLSEVALMT TSVDVLVSIC VIFAMSFVPA SFVVFLIQER  1680
VSKAKHLQFI SGVKPVIYWL SNFVWDMCNY VVPATLVIII FICFQQKSYV SSTNLPVLAL  1740
LLLLYGWSIT PLMYPASFVF KIPSTAYVVL TSVNLFIGIN GSVATFVLEL FTDNKLNNIN  1800
DILKSVFLIF PHFCLGRGLI DMVKNQAMAD ALERFGENRF VSPLSWDLVG RNLFAMAVEG  1860
VVFFLITVLI QYRFFIRPRP VNAKLSPLND EDEDVRRERQ RILDGGGQND ILEIKELTKI  1920
YRRKRKPAVD RICVGIPPGE CFGLLGVNGA GKSSTFKMLT GDTTVTRGDA FLNKNSILSN  1980
IHEVHQNMGY CPQFDAITEL LTGREHVEFF ALLRGVPEKE VGKVGEWAIR KLGLVKYGEK  2040
YAGNYSGGNK RKLSTAMALI GGPPVVFLDE PTTGMDPKAR RFLWNCALSV VKEGRSVVLT  2100
SHSMEECEAL CTRMAIMVNG RFRCLGSVQH LKNRFGDGYT IVVRIAGSNP DLKPVQDFFG  2160
LAFPGSVLKE KHRNMLQYQL PSSLSSLARI FSILSQSKKR LHIEDYSVSQ TTLDQVFVNF  2220
AKDQSDDDHL KDLSLHKNQT VVDVAVLTSF LQDEKVKESY V                      2261
FASTA
(Canonical)
>LipidDB-9606-00822|O95477
MACWPQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKA
MPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDT
SMKDMRKVLRTLQQIKKSSSNLKLQDFLVDNETFSGFLYHNLSLPKSTVDKMLRADVILH
KVFLQGYQLHLTSLCNGSKSEEMIQLGDQEVSELCGLPREKLAAAERVLRSNMDILKPIL
RTLNSTSPFPSKELAEATKTLLHSLGTLAQELFSMRSWSDMRQEVMFLTNVNSSSSSTQI
YQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAETFYDNSTTPYCNDLMK
NLESSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDLEGMWEELS
PKIWTFMENSQEMDLVRMLLDSRDNDHFWEQQLDGLDWTAQDIVAFLAKHPEDVQSSNGS
VYTWREAFNETNQAIRTISRFMECVNLNKLEPIATEVWLINKSMELLDERKFWAGIVFTG
ITPGSIELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVV
EQAIIRVLTGTEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIV
YEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFV
FLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFTLKIFAS
LLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTSVSMMLFDTFLYGVMTW
YIEAVFPGQYGIPRPWYFPCTKSYWFGEESDEKSHPGSNQKRISEICMEEEPTHLKLGVS
IQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIL
GKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVG
LPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ
GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLS
SCRNSSSTVSYLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDI
GHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAE
TSDGTLPARRNRRAFGDKQSCLRPFTEDDAADPNDSDIDPESRETDLLSGMDGKGSYQVK
GWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQ
PWMYNEQYTFVSNDAPEDTGTLELLNALTKDPGFGTRCMEGNPIPDTPCQAGEEEWTTAP
VPQTIMDLFQNGNWTMQNPSPACQCSSDKIKKMLPVCPPGAGGLPPPQRKQNTADILQDL
TGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGVSNTQALPPSQEVNDAIKQMKK
HLKLAKDSSADRFLNSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQK
GENPSHYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQER
VSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLAL
LLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTDNKLNNIN
DILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEG
VVFFLITVLIQYRFFIRPRPVNAKLSPLNDEDEDVRRERQRILDGGGQNDILEIKELTKI
YRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSN
IHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEK
YAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLT
SHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQDFFG
LAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNF
AKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV
Gene Ontology
GO:0030139; C:endocytic vesicle; IDA:BHF-UCL
GO:0009897; C:external side of plasma membrane; IEA:Ensembl
GO:0005794; C:Golgi apparatus; IEA:Ensembl
GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL
GO:0045121; C:membrane raft; IDA:BHF-UCL
GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL
GO:0045335; C:phagocytic vesicle; IDA:BHF-UCL
GO:0005886; C:plasma membrane; IDA:BHF-UCL
GO:0008509; F:anion transmembrane transporter activity; ISS:BHF-UCL
GO:0034186; F:apolipoprotein A-I binding; IPI:BHF-UCL
GO:0034188; F:apolipoprotein A-I receptor activity; IDA:BHF-UCL
GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL
GO:0005524; F:ATP binding; IDA:BHF-UCL
GO:0016887; F:ATPase activity; IEA:InterPro
GO:0051117; F:ATPase binding; IPI:BHF-UCL
GO:0015485; F:cholesterol binding; IC:BHF-UCL
GO:0017127; F:cholesterol transporter activity; IDA:BHF-UCL
GO:0005543; F:phospholipid binding; IC:BHF-UCL
GO:0005548; F:phospholipid transporter activity; IDA:BHF-UCL
GO:0005102; F:receptor binding; IPI:BHF-UCL
GO:0031267; F:small GTPase binding; IPI:BHF-UCL
GO:0019905; F:syntaxin binding; IPI:BHF-UCL
GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IDA:GOC
GO:0044255; P:cellular lipid metabolic process; TAS:Reactome
GO:0071397; P:cellular response to cholesterol; IEA:Ensembl
GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl
GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl
GO:0033344; P:cholesterol efflux; IDA:BHF-UCL
GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL
GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL
GO:0016197; P:endosomal transport; IDA:BHF-UCL
GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:BHF-UCL
GO:0034380; P:high-density lipoprotein particle assembly; IMP:BHF-UCL
GO:0050702; P:interleukin-1 beta secretion; IMP:BHF-UCL
GO:0032367; P:intracellular cholesterol transport; IMP:BHF-UCL
GO:0042157; P:lipoprotein metabolic process; TAS:Reactome
GO:0007040; P:lysosome organization; IDA:BHF-UCL
GO:0010887; P:negative regulation of cholesterol storage; TAS:BHF-UCL
GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; TAS:BHF-UCL
GO:0002790; P:peptide secretion; IEA:Ensembl
GO:0006911; P:phagocytosis, engulfment; IEA:Ensembl
GO:0033700; P:phospholipid efflux; IDA:BHF-UCL
GO:0055091; P:phospholipid homeostasis; IMP:BHF-UCL
GO:0045332; P:phospholipid translocation; IEA:Ensembl
GO:0060155; P:platelet dense granule organization; IMP:BHF-UCL
GO:0030819; P:positive regulation of cAMP biosynthetic process; IMP:BHF-UCL
GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl
GO:0006497; P:protein lipidation; IEA:Ensembl
GO:0032489; P:regulation of Cdc42 protein signal transduction; IMP:BHF-UCL
GO:0042493; P:response to drug; IEA:Ensembl
GO:0034616; P:response to laminar fluid shear stress; IEP:BHF-UCL
GO:0055098; P:response to low-density lipoprotein particle; IEP:BHF-UCL
GO:0007584; P:response to nutrient; IEA:Ensembl
GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL
GO:0044281; P:small molecule metabolic process; TAS:Reactome
Interpro
InterPro; IPR003593; AAA+_ATPase
InterPro; IPR026082; ABC_A
InterPro; IPR003439; ABC_transporter-like
InterPro; IPR017871; ABC_transporter_CS
InterPro; IPR027417; P-loop_NTPase
Pfam
Pfam; PF00005; ABC_tran;
SMART
SMART; SM00382; AAA;
PROSITE
PROSITE; PS00211; ABC_TRANSPORTER_1;
PROSITE; PS50893; ABC_TRANSPORTER_2;
PRINTS