ABCA1_MOUSE
ID ABCA1_MOUSE Reviewed; 2261 AA.
AC P41233; B1AWZ8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Phospholipid-transporting ATPase ABCA1 {ECO:0000250|UniProtKB:O95477};
DE EC=7.6.2.1 {ECO:0000250|UniProtKB:O95477};
DE AltName: Full=ATP-binding cassette sub-family A member 1;
DE AltName: Full=ATP-binding cassette transporter 1;
DE Short=ABC-1;
DE Short=ATP-binding cassette 1;
GN Name=Abca1 {ECO:0000312|MGI:MGI:99607}; Synonyms=Abc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DBA/2J; TISSUE=Macrophage;
RX PubMed=8088782; DOI=10.1006/geno.1994.1237;
RA Luciani M.-F., Denizot F., Savary S., Mattei M.-G., Chimini G.;
RT "Cloning of two novel ABC transporters mapping on human chromosome 9.";
RL Genomics 21:150-159(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=11352567; DOI=10.1006/geno.2000.6467;
RA Qiu Y., Cavelier L., Chiu S., Yang X., Rubin E., Cheng J.-F.;
RT "Human and mouse ABCA1 comparative sequencing and transgenesis studies
RT revealing novel regulatory sequences.";
RL Genomics 73:66-76(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION BY LIPOPOLYSACCHARIDE.
RX PubMed=12032171;
RA Kaplan R., Gan X., Menke J.G., Wright S.D., Cai T.-Q.;
RT "Bacterial lipopolysaccharide induces expression of ABCA1 but not ABCG1 via
RT an LXR-independent pathway.";
RL J. Lipid Res. 43:952-959(2002).
RN [6]
RP DOWN-REGULATION BY ENDOTOXIN.
RX PubMed=12777468; DOI=10.1194/jlr.m300100-jlr200;
RA Khovidhunkit W., Moser A.H., Shigenaga J.K., Grunfeld C., Feingold K.R.;
RT "Endotoxin down-regulates ABCG5 and ABCG8 in mouse liver and ABCA1 and
RT ABCG1 in J774 murine macrophages: differential role of LXR.";
RL J. Lipid Res. 44:1728-1736(2003).
RN [7]
RP INTERACTION WITH MEGF10.
RX PubMed=17205124; DOI=10.1371/journal.pone.0000120;
RA Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V.,
RA Zhou Z., Chimini G.;
RT "Cooperation between engulfment receptors: the case of ABCA1 and MEGF10.";
RL PLoS ONE 1:E120-E120(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1296, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-489.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1296, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the translocation of specific phospholipids from
CC the cytoplasmic to the extracellular/lumenal leaflet of membrane
CC coupled to the hydrolysis of ATP. Thereby, participates in phospholipid
CC transfer to apoliproteins to form nascent high density
CC lipoproteins/HDLs. Transports preferentially phosphatidylcholine over
CC phosphatidylserine. May play a similar role in the efflux of
CC intracellular cholesterol to apoliproteins and the formation of nascent
CC high density lipoproteins/HDLs. {ECO:0000250|UniProtKB:O95477}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000250|UniProtKB:O95477};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a
CC 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O95477};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584;
CC Evidence={ECO:0000250|UniProtKB:O95477};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O =
CC a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95477};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC Evidence={ECO:0000250|UniProtKB:O95477};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingomyelin(in) + ATP + H2O = a sphingomyelin(out) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:38903, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95477};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38904;
CC Evidence={ECO:0000250|UniProtKB:O95477};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O95477};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000250|UniProtKB:O95477};
CC -!- ACTIVITY REGULATION: ATPase activity is decreased by cholesterol and
CC ceramide. ATPase activity is stimulated by phosphatidylcholine and to a
CC lesser degree by phosphatidylserine and sphingomyelin. Phospholipid
CC translocase activity is highly reduced by berylium fluoride and
CC aluminum flouride and reduced by N-ethylmaleimide.
CC {ECO:0000250|UniProtKB:O95477}.
CC -!- SUBUNIT: Interacts with MEGF10 (PubMed:17205124). May interact with
CC APOE1; functionally associated with APOE1 in the biogenesis of HDLs (By
CC similarity). Interacts with ABCA8; this interaction potentiates
CC cholesterol efflux (By similarity). Interacts with ABCA12 and NR1H2;
CC this interaction is required for ABCA1 localization to the cell surface
CC and is necessary for its normal activity and stability (By similarity).
CC {ECO:0000250|UniProtKB:O95477, ECO:0000269|PubMed:17205124}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95477};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O95477}. Endosome
CC {ECO:0000250|UniProtKB:O95477}.
CC -!- TISSUE SPECIFICITY: Widely expressed in adult tissues. Highest levels
CC are found in pregnant uterus and uterus.
CC -!- INDUCTION: Down-regulated by endotoxins (LPS) or cytokines (TNF and IL-
CC 1) in J774 macrophages. The down-regulation by endotoxin in macrophages
CC is not likely to be mediated by the liver X receptor/retinoic X
CC receptor (LXR/RXR). {ECO:0000269|PubMed:12032171}.
CC -!- DOMAIN: Multifunctional polypeptide with two homologous halves, each
CC containing a hydrophobic membrane-anchoring domain and an ATP binding
CC cassette (ABC) domain.
CC -!- PTM: Phosphorylation on Ser-2054 regulates phospholipid efflux.
CC {ECO:0000250|UniProtKB:O95477}.
CC -!- PTM: Palmitoylated by ZDHHC8. Palmitoylation is essential for
CC localization to the plasma membrane. {ECO:0000250|UniProtKB:O95477}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG39073.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA53530.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X75926; CAA53530.1; ALT_INIT; mRNA.
DR EMBL; AF287263; AAG39073.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL772397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466565; EDL02285.1; -; Genomic_DNA.
DR CCDS; CCDS18187.1; -.
DR PIR; A54774; A54774.
DR RefSeq; NP_038482.3; NM_013454.3.
DR AlphaFoldDB; P41233; -.
DR SMR; P41233; -.
DR BioGRID; 197900; 1.
DR CORUM; P41233; -.
DR IntAct; P41233; 2.
DR STRING; 10090.ENSMUSP00000030010; -.
DR BindingDB; P41233; -.
DR ChEMBL; CHEMBL1641361; -.
DR TCDB; 3.A.1.211.1; the atp-binding cassette (abc) superfamily.
DR GlyConnect; 2139; 2 N-Linked glycans (1 site).
DR GlyGen; P41233; 22 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P41233; -.
DR PhosphoSitePlus; P41233; -.
DR SwissPalm; P41233; -.
DR jPOST; P41233; -.
DR MaxQB; P41233; -.
DR PaxDb; P41233; -.
DR PeptideAtlas; P41233; -.
DR PRIDE; P41233; -.
DR ProteomicsDB; 285949; -.
DR Antibodypedia; 14760; 592 antibodies from 38 providers.
DR DNASU; 11303; -.
DR Ensembl; ENSMUST00000030010; ENSMUSP00000030010; ENSMUSG00000015243.
DR GeneID; 11303; -.
DR KEGG; mmu:11303; -.
DR UCSC; uc008swu.1; mouse.
DR CTD; 19; -.
DR MGI; MGI:99607; Abca1.
DR VEuPathDB; HostDB:ENSMUSG00000015243; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000154658; -.
DR HOGENOM; CLU_000604_19_0_1; -.
DR InParanoid; P41233; -.
DR OMA; CLFICIA; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; P41233; -.
DR TreeFam; TF105191; -.
DR Reactome; R-MMU-8963896; HDL assembly.
DR Reactome; R-MMU-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR BioGRID-ORCS; 11303; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Abca1; mouse.
DR PRO; PR:P41233; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P41233; protein.
DR Bgee; ENSMUSG00000015243; Expressed in stroma of bone marrow and 254 other tissues.
DR Genevisible; P41233; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030139; C:endocytic vesicle; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:MGI.
DR GO; GO:0097708; C:intracellular vesicle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0034186; F:apolipoprotein A-I binding; ISO:MGI.
DR GO; GO:0034188; F:apolipoprotein A-I receptor activity; ISO:MGI.
DR GO; GO:0034185; F:apolipoprotein binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:MGI.
DR GO; GO:0120020; F:cholesterol transfer activity; IDA:MGI.
DR GO; GO:0140328; F:floppase activity; ISS:UniProtKB.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; ISO:MGI.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; ISO:MGI.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; ISO:MGI.
DR GO; GO:0005548; F:phospholipid transporter activity; IDA:MGI.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0046623; F:sphingolipid floppase activity; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
DR GO; GO:0033344; P:cholesterol efflux; IDA:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; IDA:MGI.
DR GO; GO:0030301; P:cholesterol transport; ISO:MGI.
DR GO; GO:0016197; P:endosomal transport; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0140115; P:export across plasma membrane; IMP:ARUK-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; ISO:MGI.
DR GO; GO:0032367; P:intracellular cholesterol transport; ISO:MGI.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IMP:MGI.
DR GO; GO:0042157; P:lipoprotein metabolic process; IMP:MGI.
DR GO; GO:0007040; P:lysosome organization; ISO:MGI.
DR GO; GO:0002790; P:peptide secretion; IMP:MGI.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:MGI.
DR GO; GO:0033700; P:phospholipid efflux; IDA:MGI.
DR GO; GO:0055091; P:phospholipid homeostasis; ISO:MGI.
DR GO; GO:0045332; P:phospholipid translocation; IMP:MGI.
DR GO; GO:0015914; P:phospholipid transport; ISO:MGI.
DR GO; GO:0060155; P:platelet dense granule organization; ISO:MGI.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
DR GO; GO:0090108; P:positive regulation of high-density lipoprotein particle assembly; IMP:UniProtKB.
DR GO; GO:0006497; P:protein lipidation; IMP:MGI.
DR GO; GO:0009306; P:protein secretion; IMP:ARUK-UCL.
DR GO; GO:0071806; P:protein transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISO:MGI.
DR GO; GO:0034616; P:response to laminar fluid shear stress; ISO:MGI.
DR GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL.
DR GO; GO:0023061; P:signal release; IMP:ARUK-UCL.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR030365; ABCA1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR PANTHER; PTHR19229:SF34; PTHR19229:SF34; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; Endosome; Glycoprotein;
KW Lipoprotein; Membrane; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..2261
FT /note="Phospholipid-transporting ATPase ABCA1"
FT /id="PRO_0000093289"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..639
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 683..703
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 745..765
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 777..797
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 827..847
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 941..961
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1351..1371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1372..1656
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1657..1677
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1703..1723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1735..1755
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1768..1788
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1802..1822
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1852..1872
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 899..1131
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1912..2144
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1285..1310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1285..1308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 933..940
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1946..1953
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 1042
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O95477"
FT MOD_RES 1296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2054
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O95477"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 23
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 1110
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 1111
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2044
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..309
FT /evidence="ECO:0000250"
FT DISULFID 1463..1477
FT /evidence="ECO:0000250"
FT CONFLICT 1567..1568
FT /note="Missing (in Ref. 2; AAG39073)"
FT /evidence="ECO:0000305"
FT CONFLICT 1568
FT /note="S -> T (in Ref. 1; CAA53530)"
FT /evidence="ECO:0000305"
FT CONFLICT 2024
FT /note="V -> F (in Ref. 1; CAA53530)"
FT /evidence="ECO:0000305"
FT CONFLICT 2024
FT /note="Missing (in Ref. 2; AAG39073)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2261 AA; 253912 MW; E041DA4FA73C2660 CRC64;
MACWPQLRLL LWKNLTFRRR QTCQLLLEVA WPLFIFLILI SVRLSYPPYE QHECHFPNKA
MPSAGTLPWV QGIICNANNP CFRYPTPGEA PGVVGNFNKS IVSRLFSDAQ RLLLYSQRDT
SIKDMHKVLR MLRQIKHPNS NLKLQDFLVD NETFSGFLQH NLSLPRSTVD SLLQANVGLQ
KVFLQGYQLH LASLCNGSKL EEIIQLGDAE VSALCGLPRK KLDAAERVLR YNMDILKPVV
TKLNSTSHLP TQHLAEATTV LLDSLGGLAQ ELFSTKSWSD MRQEVMFLTN VNSSSSSTQI
YQAVSRIVCG HPEGGGLKIK SLNWYEDNNY KALFGGNNTE EDVDTFYDNS TTPYCNDLMK
NLESSPLSRI IWKALKPLLV GKILYTPDTP ATRQVMAEVN KTFQELAVFH DLEGMWEELS
PQIWTFMENS QEMDLVRTLL DSRGNDQFWE QKLDGLDWTA QDIMAFLAKN PEDVQSPNGS
VYTWREAFNE TNQAIQTISR FMECVNLNKL EPIPTEVRLI NKSMELLDER KFWAGIVFTG
ITPDSVELPH HVKYKIRMDI DNVERTNKIK DGYWDPGPRA DPFEDMRYVW GGFAYLQDVV
EQAIIRVLTG SEKKTGVYVQ QMPYPCYVDD IFLRVMSRSM PLFMTLAWIY SVAVIIKSIV
YEKEARLKET MRIMGLDNGI LWFSWFVSSL IPLLVSAGLL VVILKLGNLL PYSDPSVVFV
FLSVFAMVTI LQCFLISTLF SRANLAAACG GIIYFTLYLP YVLCVAWQDY VGFSIKIFAS
LLSPVAFGFG CEYFALFEEQ GIGVQWDNLF ESPVEEDGFN LTTAVSMMLF DTFLYGVMTW
YIEAVFPGQY GIPRPWYFPC TKSYWFGEEI DEKSHPGSSQ KGVSEICMEE EPTHLRLGVS
IQNLVKVYRD GMKVAVDGLA LNFYEGQITS FLGHNGAGKT TTMSILTGLF PPTSGTAYIL
GKDIRSEMSS IRQNLGVCPQ HNVLFDMLTV EEHIWFYARL KGLSEKHVKA EMEQMALDVG
LPPSKLKSKT SQLSGGMQRK LSVALAFVGG SKVVILDEPT AGVDPYSRRG IWELLLKYRQ
GRTIILSTHH MDEADILGDR IAIISHGKLC CVGSSLFLKN QLGTGYYLTL VKKDVESSLS
SCRNSSSTVS CLKKEDSVSQ SSSDAGLGSD HESDTLTIDV SAISNLIRKH VSEARLVEDI
GHELTYVLPY EAAKEGAFVE LFHEIDDRLS DLGISSYGIS ETTLEEIFLK VAEESGVDAE
TSDGTLPARR NRRAFGDKQS CLHPFTEDDA VDPNDSDIDP ESRETDLLSG MDGKGSYQLK
GWKLTQQQFV ALLWKRLLIA RRSRKGFFAQ IVLPAVFVCI ALVFSLIVPP FGKYPSLELQ
PWMYNEQYTF VSNDAPEDMG TQELLNALTK DPGFGTRCME GNPIPDTPCL AGEEDWTISP
VPQSIVDLFQ NGNWTMKNPS PACQCSSDKI KKMLPVCPPG AGGLPPPQRK QKTADILQNL
TGRNISDYLV KTYVQIIAKS LKNKIWVNEF RYGGFSLGVS NSQALPPSHE VNDAIKQMKK
LLKLTKDSSA DRFLSSLGRF MAGLDTKNNV KVWFNNKGWH AISSFLNVIN NAILRANLQK
GENPSQYGIT AFNHPLNLTK QQLSEVALMT TSVDVLVSIC VIFAMSFVPA SFVVFLIQER
VSKAKHLQFI SGVKPVIYWL SNFVWDMCNY VVPATLVIII FICFQQKSYV SSTNLPVLAL
LLLLYGWSIT PLMYPASFVF KIPSTAYVVL TSVNLFIGIN GSVATFVLEL FTNNKLNDIN
DILKSVFLIF PHFCLGRGLI DMVKNQAMAD ALERFGENRF VSPLSWDLVG RNLFAMAVEG
VVFFLITVLI QYRFFIRPRP VKAKLPPLND EDEDVRRERQ RILDGGGQND ILEIKELTKI
YRRKRKPAVD RICIGIPPGE CFGLLGVNGA GKSTTFKMLT GDTPVTRGDA FLNKNSILSN
IHEVHQNMGY CPQFDAITEL LTGREHVEFF ALLRGVPEKE VGKVGEWAIR KLGLVKYGEK
YASNYSGGNK RKLSTAMALI GGPPVVFLDE PTTGMDPKAR RFLWNCALSI VKEGRSVVLT
SHSMEECEAL CTRMAIMVNG RFRCLGSVQH LKNRFGDGYT IVVRIAGSNP DLKPVQEFFG
LAFPGSVLKE KHRNMLQYQL PSSLSSLARI FSILSQSKKR LHIEDYSVSQ TTLDQVFVNF
AKDQSDDDHL KDLSLHKNQT VVDVAVLTSF LQDEKVKESY V
