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ATP-binding cassette sub-family A member 7 (ABCA-SSN) (Autoantigen SS-N) (Macrophage ABC transporter)

 ABCA7_HUMAN             Reviewed;        2146 AA.
Q8IZY2; Q96S58; Q9BZC4; Q9NR73; Q9UKP8;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 3.
25-OCT-2017, entry version 127.
RecName: Full=ATP-binding cassette sub-family A member 7;
AltName: Full=ABCA-SSN;
AltName: Full=Autoantigen SS-N;
AltName: Full=Macrophage ABC transporter;
Name=ABCA7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-1349; ALA-1527
AND SER-2045, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
TISSUE=Macrophage;
PubMed=10873640; DOI=10.1006/bbrc.2000.2954;
Kaminski W.E., Orso E., Diederich W., Klucken J., Drobnik W.,
Schmitz G.;
"Identification of a novel human sterol-sensitive ATP-binding cassette
transporter (ABCA7).";
Biochem. Biophys. Res. Commun. 273:532-538(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-1527.
PubMed=11095984; DOI=10.1006/bbrc.2000.3880;
Kaminski W.E., Piehler A., Schmitz G.;
"Genomic organization of the human cholesterol-responsive ABC
transporter ABCA7: tandem linkage with the minor histocompatibility
antigen HA-1 gene.";
Biochem. Biophys. Res. Commun. 278:782-789(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS GLN-1349;
ALA-1527 AND SER-2045.
TISSUE=Thymus;
PubMed=11355874; DOI=10.1006/bbrc.2001.4891;
Tanaka A.R., Ikeda Y., Abe-Dohmae S., Arakawa R., Sadanami K.,
Kidera A., Nakagawa S., Nagase T., Aoki R., Kioka N., Amachi T.,
Yokoyama S., Ueda K.;
"Human ABCA1 contains a large amino-terminal extracellular domain
homologous to an epitope of Sjogren's Syndrome.";
Biochem. Biophys. Res. Commun. 283:1019-1025(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLY-188; ALA-1527 AND
SER-2045, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=Spleen;
PubMed=11435699;
Broccardo C., Osorio J., Luciani M.-F., Schriml L.M., Prades C.,
Shulenin S., Arnould I., Naudin L., Lafargue C., Rosier M., Jordan B.,
Mattei M.-G., Dean M., Denefle P., Chimini G.;
"Comparative analysis of the promoter structure and genomic
organization of the human and mouse ABCA7 gene encoding a novel ABCA
transporter.";
Cytogenet. Cell Genet. 92:264-270(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 195-352 (ISOFORMS 1/2).
TISSUE=Cervix carcinoma;
Niwa M., Maruyama M., Fujimoto T., Dohi K., Maruyama I.N.;
"Isolation of autoantigen cDNAs by lambda phage surface display.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=14592415; DOI=10.1016/j.bbrc.2003.10.002;
Ikeda Y., Abe-Dohmae S., Munehira Y., Aoki R., Kawamoto S., Furuya A.,
Shitara K., Amachi T., Kioka N., Matsuo M., Yokoyama S., Ueda K.;
"Posttranscriptional regulation of human ABCA7 and its function for
the apoA-I-dependent lipid release.";
Biochem. Biophys. Res. Commun. 311:313-318(2003).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12917409; DOI=10.1074/jbc.M307831200;
Wang N., Lan D., Gerbod-Giannone M., Linsel-Nitschke P., Jehle A.W.,
Chen W., Martinez L.O., Tall A.R.;
"ATP-binding cassette transporter A7 (ABCA7) binds apolipoprotein A-I
and mediates cellular phospholipid but not cholesterol efflux.";
J. Biol. Chem. 278:42906-42912(2003).
[9]
FUNCTION, AND INDUCTION.
PubMed=12925201; DOI=10.1046/j.1523-1747.2003.12404.x;
Kielar D., Kaminski W.E., Liebisch G., Piehler A., Wenzel J.J.,
Moehle C., Heimerl S., Langmann T., Friedrich S.O., Boettcher A.,
Barlage S., Drobnik W., Schmitz G.;
"Adenosine triphosphate binding cassette (ABC) transporters are
expressed and regulated during terminal keratinocyte differentiation:
a potential role for ABCA7 in epidermal lipid reorganization.";
J. Invest. Dermatol. 121:465-474(2003).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14570867; DOI=10.1074/jbc.M309888200;
Abe-Dohmae S., Ikeda Y., Matsuo M., Hayashi M., Okuhira K., Ueda K.,
Yokoyama S.;
"Human ABCA7 supports apolipoprotein-mediated release of cellular
cholesterol and phospholipid to generate high density lipoprotein.";
J. Biol. Chem. 279:604-611(2004).
[11]
INVOLVEMENT IN AD9.
PubMed=26141617; DOI=10.1016/S1474-4422(15)00133-7;
Cuyvers E., De Roeck A., Van den Bossche T., Van Cauwenberghe C.,
Bettens K., Vermeulen S., Mattheijssens M., Peeters K.,
Engelborghs S., Vandenbulcke M., Vandenberghe R., De Deyn P.P.,
Van Broeckhoven C., Sleegers K.;
"Mutations in ABCA7 in a Belgian cohort of Alzheimer's disease
patients: a targeted resequencing study.";
Lancet Neurol. 14:814-822(2015).
[12]
INVOLVEMENT IN AD9.
PubMed=25807283; DOI=10.1038/ng.3246;
DemGene;
Steinberg S., Stefansson H., Jonsson T., Johannsdottir H., Ingason A.,
Helgason H., Sulem P., Magnusson O.T., Gudjonsson S.A.,
Unnsteinsdottir U., Kong A., Helisalmi S., Soininen H., Lah J.J.,
Aarsland D., Fladby T., Ulstein I.D., Djurovic S., Sando S.B.,
White L.R., Knudsen G.P., Westlye L.T., Selbaek G., Giegling I.,
Hampel H., Hiltunen M., Levey A.I., Andreassen O.A., Rujescu D.,
Jonsson P.V., Bjornsson S., Snaedal J., Stefansson K.;
"Loss-of-function variants in ABCA7 confer risk of Alzheimer's
disease.";
Nat. Genet. 47:445-447(2015).
[13]
VARIANTS GLY-188; ALA-319; ARG-395; HIS-463; THR-718; GLN-1349;
ARG-1686 AND SER-2045.
PubMed=12111378; DOI=10.1007/s100380200041;
Iida A., Saito S., Sekine A., Mishima C., Kitamura Y., Kondo K.,
Harigae S., Osawa S., Nakamura Y.;
"Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes
encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8,
ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and
ABCG8.";
J. Hum. Genet. 47:285-310(2002).
-!- FUNCTION: Plays a role in phagocytosis by macrophages of apoptotic
cells. Binds APOA1 and may function in apolipoprotein-mediated
phospholipid efflux from cells. May also mediate cholesterol
efflux. May regulate cellular ceramide homeostasis during
keratinocytes differentiation. {ECO:0000269|PubMed:12917409,
ECO:0000269|PubMed:12925201, ECO:0000269|PubMed:14570867,
ECO:0000269|PubMed:14592415}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12917409,
ECO:0000269|PubMed:14592415}; Multi-pass membrane protein
{ECO:0000255}. Golgi apparatus membrane
{ECO:0000250|UniProtKB:Q91V24}; Multi-pass membrane protein
{ECO:0000255}. Early endosome membrane
{ECO:0000250|UniProtKB:Q91V24}; Multi-pass membrane protein
{ECO:0000255}. Note=Localizes to cell membrane ruffles and
phagocytic cups of macrophages stimulated with C1q or apoptotic
cells. Localizes to the cytoplasm of resting macrophages, probably
in Golgi and endosomes. Localizes to the apical brush border of
cells in the proximal tubules of kidney (By similarity). Isoform 2
may localize to the endoplasmic reticulum (PubMed:14592415).
{ECO:0000250|UniProtKB:Q91V24, ECO:0000269|PubMed:14592415}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Type 1;
IsoId=Q8IZY2-1; Sequence=Displayed;
Name=2; Synonyms=Type 2;
IsoId=Q8IZY2-2; Sequence=VSP_020701, VSP_020702;
Note=Inactive for apoA-I-mediated lipid release.;
-!- TISSUE SPECIFICITY: Expressed in leukocytes (at protein level).
Widely expressed. Highly expressed in myelo-lymphatic tissues
including peripheral leukocytes, thymus, spleen and bone marrow.
Isoform 2 is more abundant in lymph node, spleen, thymus and
trachea than isoform 1 which is more strongly expressed in brain
and bone marrow. {ECO:0000269|PubMed:10873640,
ECO:0000269|PubMed:11435699, ECO:0000269|PubMed:14592415}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal tissues. Strongly
expressed in fetal liver. {ECO:0000269|PubMed:10873640,
ECO:0000269|PubMed:11435699}.
-!- INDUCTION: Up-regulated in macrophages upon cholesterol uptake and
inversely regulated upon cholesterol deloading from the cells (at
protein level). Up-regulated in keratinocytes during terminal
differentiation. {ECO:0000269|PubMed:10873640,
ECO:0000269|PubMed:12925201}.
-!- DISEASE: Alzheimer disease 9 (AD9) [MIM:608907]: A familial, late-
onset form of Alzheimer disease. Alzheimer disease is a
neurodegenerative disorder characterized by progressive dementia,
loss of cognitive abilities, and deposition of fibrillar amyloid
proteins as intraneuronal neurofibrillary tangles, extracellular
amyloid plaques and vascular amyloid deposits. The major
constituents of these plaques are neurotoxic amyloid-beta protein
40 and amyloid-beta protein 42, that are produced by the
proteolysis of the transmembrane APP protein. The cytotoxic C-
terminal fragments (CTFs) and the caspase-cleaved products, such
as C31, are also implicated in neuronal death.
{ECO:0000269|PubMed:25807283, ECO:0000269|PubMed:26141617}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC
proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q8IZY2";
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EMBL; AF250238; AAF85794.1; -; mRNA.
EMBL; AF311102; AAN04657.1; -; Genomic_DNA.
EMBL; AF311058; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311059; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311060; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311061; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311062; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311063; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311064; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311065; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311066; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311067; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311068; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311057; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311069; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311070; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311071; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311072; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311073; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311074; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311075; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311076; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311077; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311078; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311079; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311080; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311081; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311082; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311083; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311084; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311085; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311086; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311087; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311088; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311089; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311090; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311091; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311092; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311093; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311094; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311095; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311096; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311097; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311098; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311099; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311100; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AF311101; AAN04657.1; JOINED; Genomic_DNA.
EMBL; AB055390; BAB62294.1; -; mRNA.
EMBL; AF328787; AAK00959.1; -; mRNA.
EMBL; AC011558; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF140342; AAF06727.1; -; mRNA.
CCDS; CCDS12055.1; -. [Q8IZY2-1]
RefSeq; NP_061985.2; NM_019112.3. [Q8IZY2-1]
RefSeq; XP_011525930.1; XM_011527628.2. [Q8IZY2-1]
UniGene; Hs.134514; -.
ProteinModelPortal; Q8IZY2; -.
SMR; Q8IZY2; -.
BioGrid; 115629; 8.
IntAct; Q8IZY2; 8.
STRING; 9606.ENSP00000263094; -.
SwissLipids; SLP:000000346; -.
TCDB; 3.A.1.211.10; the atp-binding cassette (abc) superfamily.
iPTMnet; Q8IZY2; -.
PhosphoSitePlus; Q8IZY2; -.
BioMuta; ABCA7; -.
DMDM; 161784300; -.
MaxQB; Q8IZY2; -.
PaxDb; Q8IZY2; -.
PeptideAtlas; Q8IZY2; -.
PRIDE; Q8IZY2; -.
DNASU; 10347; -.
Ensembl; ENST00000263094; ENSP00000263094; ENSG00000064687. [Q8IZY2-1]
Ensembl; ENST00000433129; ENSP00000414062; ENSG00000064687. [Q8IZY2-1]
Ensembl; ENST00000435683; ENSP00000465322; ENSG00000064687. [Q8IZY2-2]
GeneID; 10347; -.
KEGG; hsa:10347; -.
UCSC; uc002lqw.5; human. [Q8IZY2-1]
CTD; 10347; -.
DisGeNET; 10347; -.
EuPathDB; HostDB:ENSG00000064687.12; -.
GeneCards; ABCA7; -.
H-InvDB; HIX0014569; -.
HGNC; HGNC:37; ABCA7.
HPA; HPA041564; -.
MIM; 605414; gene.
MIM; 608907; phenotype.
neXtProt; NX_Q8IZY2; -.
OpenTargets; ENSG00000064687; -.
PharmGKB; PA24382; -.
eggNOG; KOG0059; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00760000118965; -.
HOGENOM; HOG000231547; -.
HOVERGEN; HBG050436; -.
InParanoid; Q8IZY2; -.
KO; K05645; -.
OMA; RPHLGVC; -.
OrthoDB; EOG091G007E; -.
PhylomeDB; Q8IZY2; -.
TreeFam; TF105191; -.
Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
ChiTaRS; ABCA7; human.
GeneWiki; ABCA7; -.
GenomeRNAi; 10347; -.
PRO; PR:Q8IZY2; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000064687; -.
CleanEx; HS_ABCA7; -.
ExpressionAtlas; Q8IZY2; baseline and differential.
Genevisible; Q8IZY2; HS.
GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; TAS:ProtInc.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0009986; C:cell surface; ISS:Alzheimers_University_of_Toronto.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0001891; C:phagocytic cup; ISS:Alzheimers_University_of_Toronto.
GO; GO:0005886; C:plasma membrane; IDA:Alzheimers_University_of_Toronto.
GO; GO:0032587; C:ruffle membrane; ISS:Alzheimers_University_of_Toronto.
GO; GO:0034188; F:apolipoprotein A-I receptor activity; IDA:Alzheimers_University_of_Toronto.
GO; GO:0005524; F:ATP binding; TAS:ProtInc.
GO; GO:0016887; F:ATPase activity; IDA:BHF-UCL.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0090554; F:phosphatidylcholine-translocating ATPase activity; IDA:BHF-UCL.
GO; GO:0090556; F:phosphatidylserine-translocating ATPase activity; IDA:BHF-UCL.
GO; GO:0005215; F:transporter activity; TAS:ProtInc.
GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IDA:Alzheimers_University_of_Toronto.
GO; GO:0033344; P:cholesterol efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:0034380; P:high-density lipoprotein particle assembly; IDA:Alzheimers_University_of_Toronto.
GO; GO:0007613; P:memory; ISS:Alzheimers_University_of_Toronto.
GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; ISS:Alzheimers_University_of_Toronto.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0018149; P:peptide cross-linking; ISS:Alzheimers_University_of_Toronto.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:0033700; P:phospholipid efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:0045332; P:phospholipid translocation; IDA:BHF-UCL.
GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISS:Alzheimers_University_of_Toronto.
GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:Alzheimers_University_of_Toronto.
GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; ISS:Alzheimers_University_of_Toronto.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:Alzheimers_University_of_Toronto.
GO; GO:0050766; P:positive regulation of phagocytosis; ISS:Alzheimers_University_of_Toronto.
GO; GO:1902995; P:positive regulation of phospholipid efflux; ISS:Alzheimers_University_of_Toronto.
GO; GO:0034504; P:protein localization to nucleus; ISS:Alzheimers_University_of_Toronto.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR026082; ABC_A.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR030369; ABCA7.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR19229; PTHR19229; 1.
PANTHER; PTHR19229:SF49; PTHR19229:SF49; 1.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
Alternative splicing; Alzheimer disease; Amyloidosis; ATP-binding;
Cell membrane; Complete proteome; Disulfide bond; Endosome;
Glycoprotein; Golgi apparatus; Membrane; Neurodegeneration;
Nucleotide-binding; Phagocytosis; Polymorphism; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 2146 ATP-binding cassette sub-family A member
7.
/FTId=PRO_0000250674.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TOPO_DOM 43 549 Extracellular. {ECO:0000250}.
TRANSMEM 550 570 Helical. {ECO:0000255}.
TRANSMEM 593 613 Helical. {ECO:0000255}.
TRANSMEM 626 646 Helical. {ECO:0000255}.
TRANSMEM 655 675 Helical. {ECO:0000255}.
TRANSMEM 687 707 Helical. {ECO:0000255}.
TRANSMEM 727 747 Helical. {ECO:0000255}.
TRANSMEM 849 869 Helical. {ECO:0000255}.
TRANSMEM 1243 1263 Helical. {ECO:0000255}.
TOPO_DOM 1264 1537 Extracellular. {ECO:0000250}.
TRANSMEM 1538 1558 Helical. {ECO:0000255}.
TRANSMEM 1584 1604 Helical. {ECO:0000255}.
TRANSMEM 1621 1641 Helical. {ECO:0000255}.
TRANSMEM 1649 1669 Helical. {ECO:0000255}.
TRANSMEM 1683 1703 Helical. {ECO:0000255}.
TRANSMEM 1729 1749 Helical. {ECO:0000255}.
DOMAIN 807 1038 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 1793 2025 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 841 848 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1827 1834 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
CARBOHYD 312 312 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 75 225 {ECO:0000250}.
DISULFID 1345 1359 {ECO:0000250}.
VAR_SEQ 1 138 Missing (in isoform 2).
{ECO:0000303|PubMed:11355874}.
/FTId=VSP_020701.
VAR_SEQ 139 166 AQPQPTKQSPLEPPMLDVAELLTSLLRT -> MVCLGTGQS
AGPLVSVQNHCPPCGLSPQ (in isoform 2).
{ECO:0000303|PubMed:11355874}.
/FTId=VSP_020702.
VARIANT 188 188 E -> G (in dbSNP:rs3764645).
{ECO:0000269|PubMed:11435699,
ECO:0000269|PubMed:12111378}.
/FTId=VAR_027581.
VARIANT 319 319 T -> A (in dbSNP:rs3752232).
{ECO:0000269|PubMed:12111378}.
/FTId=VAR_027582.
VARIANT 395 395 H -> R (in dbSNP:rs3764647).
{ECO:0000269|PubMed:12111378}.
/FTId=VAR_027583.
VARIANT 463 463 R -> H (in dbSNP:rs3752233).
{ECO:0000269|PubMed:12111378}.
/FTId=VAR_027584.
VARIANT 676 676 A -> T (in dbSNP:rs59851484).
/FTId=VAR_060985.
VARIANT 718 718 N -> T (in dbSNP:rs3752239).
{ECO:0000269|PubMed:12111378}.
/FTId=VAR_027585.
VARIANT 1349 1349 R -> Q (in dbSNP:rs3745842).
{ECO:0000269|PubMed:10873640,
ECO:0000269|PubMed:11355874,
ECO:0000269|PubMed:12111378}.
/FTId=VAR_027586.
VARIANT 1527 1527 G -> A (in dbSNP:rs3752246).
{ECO:0000269|PubMed:10873640,
ECO:0000269|PubMed:11095984,
ECO:0000269|PubMed:11355874,
ECO:0000269|PubMed:11435699}.
/FTId=VAR_027587.
VARIANT 1686 1686 Q -> R (in dbSNP:rs4147918).
{ECO:0000269|PubMed:12111378}.
/FTId=VAR_027588.
VARIANT 2045 2045 A -> S (in dbSNP:rs4147934).
{ECO:0000269|PubMed:10873640,
ECO:0000269|PubMed:11355874,
ECO:0000269|PubMed:11435699,
ECO:0000269|PubMed:12111378}.
/FTId=VAR_027589.
CONFLICT 1503 1503 P -> R (in Ref. 1; AAF85794 and 3;
BAB62294). {ECO:0000305}.
CONFLICT 1525 1525 S -> F (in Ref. 1; AAF85794, 2; AAN04657
and 3; BAB62294). {ECO:0000305}.
SEQUENCE 2146 AA; 234350 MW; 6EA624088E74FEE6 CRC64;
MAFWTQLMLL LWKNFMYRRR QPVQLLVELL WPLFLFFILV AVRHSHPPLE HHECHFPNKP
LPSAGTVPWL QGLICNVNNT CFPQLTPGEE PGRLSNFNDS LVSRLLADAR TVLGGASAHR
TLAGLGKLIA TLRAARSTAQ PQPTKQSPLE PPMLDVAELL TSLLRTESLG LALGQAQEPL
HSLLEAAEDL AQELLALRSL VELRALLQRP RGTSGPLELL SEALCSVRGP SSTVGPSLNW
YEASDLMELV GQEPESALPD SSLSPACSEL IGALDSHPLS RLLWRRLKPL ILGKLLFAPD
TPFTRKLMAQ VNRTFEELTL LRDVREVWEM LGPRIFTFMN DSSNVAMLQR LLQMQDEGRR
QPRPGGRDHM EALRSFLDPG SGGYSWQDAH ADVGHLVGTL GRVTECLSLD KLEAAPSEAA
LVSRALQLLA EHRFWAGVVF LGPEDSSDPT EHPTPDLGPG HVRIKIRMDI DVVTRTNKIR
DRFWDPGPAA DPLTDLRYVW GGFVYLQDLV ERAAVRVLSG ANPRAGLYLQ QMPYPCYVDD
VFLRVLSRSL PLFLTLAWIY SVTLTVKAVV REKETRLRDT MRAMGLSRAV LWLGWFLSCL
GPFLLSAALL VLVLKLGDIL PYSHPGVVFL FLAAFAVATV TQSFLLSAFF SRANLAAACG
GLAYFSLYLP YVLCVAWRDR LPAGGRVAAS LLSPVAFGFG CESLALLEEQ GEGAQWHNVG
TRPTADVFSL AQVSGLLLLD AALYGLATWY LEAVCPGQYG IPEPWNFPFR RSYWCGPRPP
KSPAPCPTPL DPKVLVEEAP PGLSPGVSVR SLEKRFPGSP QPALRGLSLD FYQGHITAFL
GHNGAGKTTT LSILSGLFPP SGGSAFILGH DVRSSMAAIR PHLGVCPQYN VLFDMLTVDE
HVWFYGRLKG LSAAVVGPEQ DRLLQDVGLV SKQSVQTRHL SGGMQRKLSV AIAFVGGSQV
VILDEPTAGV DPASRRGIWE LLLKYREGRT LILSTHHLDE AELLGDRVAV VAGGRLCCCG
SPLFLRRHLG SGYYLTLVKA RLPLTTNEKA DTDMEGSVDT RQEKKNGSQG SRVGTPQLLA
LVQHWVPGAR LVEELPHELV LVLPYTGAHD GSFATLFREL DTRLAELRLT GYGISDTSLE
EIFLKVVEEC AADTDMEDGS CGQHLCTGIA GLDVTLRLKM PPQETALENG EPAGSAPETD
QGSGPDAVGR VQGWALTRQQ LQALLLKRFL LARRSRRGLF AQIVLPALFV GLALVFSLIV
PPFGHYPALR LSPTMYGAQV SFFSEDAPGD PGRARLLEAL LQEAGLEEPP VQHSSHRFSA
PEVPAEVAKV LASGNWTPES PSPACQCSRP GARRLLPDCP AAAGGPPPPQ AVTGSGEVVQ
NLTGRNLSDF LVKTYPRLVR QGLKTKKWVN EVRYGGFSLG GRDPGLPSGQ ELGRSVEELW
ALLSPLPGGA LDRVLKNLTA WAHSLDAQDS LKIWFNNKGW HSMVAFVNRA SNAILRAHLP
PGPARHAHSI TTLNHPLNLT KEQLSEGALM ASSVDVLVSI CVVFAMSFVP ASFTLVLIEE
RVTRAKHLQL MGGLSPTLYW LGNFLWDMCN YLVPACIVVL IFLAFQQRAY VAPANLPALL
LLLLLYGWSI TPLMYPASFF FSVPSTAYVV LTCINLFIGI NGSMATFVLE LFSDQKLQEV
SRILKQVFLI FPHFCLGRGL IDMVRNQAMA DAFERLGDRQ FQSPLRWEVV GKNLLAMVIQ
GPLFLLFTLL LQHRSQLLPQ PRVRSLPLLG EEDEDVARER ERVVQGATQG DVLVLRNLTK
VYRGQRMPAV DRLCLGIPPG ECFGLLGVNG AGKTSTFRMV TGDTLASRGE AVLAGHSVAR
EPSAAHLSMG YCPQSDAIFE LLTGREHLEL LARLRGVPEA QVAQTAGSGL ARLGLSWYAD
RPAGTYSGGN KRKLATALAL VGDPAVVFLD EPTTGMDPSA RRFLWNSLLA VVREGRSVML
TSHSMEECEA LCSRLAIMVN GRFRCLGSPQ HLKGRFAAGH TLTLRVPAAR SQPAAAFVAA
EFPGAELREA HGGRLRFQLP PGGRCALARV FGELAVHGAE HGVEDFSVSQ TMLEEVFLYF
SKDQGKDEDT EEQKEAGVGV DPAPGLQHPK RVSQFLDDPS TAETVL


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