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ATP-binding cassette sub-family A member 7

 ABCA7_MOUSE             Reviewed;        2159 AA.
Q91V24; Q9JL36;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
07-NOV-2018, entry version 129.
RecName: Full=ATP-binding cassette sub-family A member 7;
Name=Abca7;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
STRAIN=DBA/2J; TISSUE=Lymphoma;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1920-2159.
STRAIN=C57BL/6J;
PubMed=10708515; DOI=10.1006/geno.1999.6102;
Schriml L.M., Dean M.;
"Identification of 18 mouse ABC genes and characterization of the ABC
superfamily in Mus musculus.";
Genomics 64:24-31(2000).
[3]
FUNCTION, TISSUE SPECIFICITY, 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).
[4]
INDUCTION.
PubMed=16445568; DOI=10.1111/j.1440-1681.2005.04301.x;
Wakaumi M., Ishibashi K., Ando H., Kasanuki H., Tsuruoka S.;
"Acute digoxin loading reduces ABCA8A mRNA expression in the mouse
liver.";
Clin. Exp. Pharmacol. Physiol. 32:1034-1041(2005).
[5]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=15550377; DOI=10.1074/jbc.M412602200;
Kim W.S., Fitzgerald M.L., Kang K., Okuhira K., Bell S.A.,
Manning J.J., Koehn S.L., Lu N., Moore K.J., Freeman M.W.;
"Abca7 null mice retain normal macrophage phosphatidylcholine and
cholesterol efflux activity despite alterations in adipose mass and
serum cholesterol levels.";
J. Biol. Chem. 280:3989-3995(2005).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=16908670; DOI=10.1083/jcb.200601030;
Jehle A.W., Gardai S.J., Li S., Linsel-Nitschke P., Morimoto K.,
Janssen W.J., Vandivier R.W., Wang N., Greenberg S., Dale B.M.,
Qin C., Henson P.M., Tall A.R.;
"ATP-binding cassette transporter A7 enhances phagocytosis of
apoptotic cells and associated ERK signaling in macrophages.";
J. Cell Biol. 174:547-556(2006).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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:15550377, ECO:0000269|PubMed:16908670}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12917409};
Multi-pass membrane protein {ECO:0000255}. Golgi apparatus
membrane {ECO:0000269|PubMed:16908670}; Multi-pass membrane
protein {ECO:0000255}. Early endosome membrane
{ECO:0000269|PubMed:16908670}; 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 (PubMed:16908670). Localizes to the apical
brush border of cells in the proximal tubules of kidney
(Probable). {ECO:0000269|PubMed:16908670, ECO:0000305}.
-!- TISSUE SPECIFICITY: Widely expressed with higher expression in
brain, lung, adrenal gland and spleen (at protein level). Highly
expressed in spleen and hematopoietic tissues.
{ECO:0000269|PubMed:11435699, ECO:0000269|PubMed:12917409,
ECO:0000269|PubMed:15550377}.
-!- DEVELOPMENTAL STAGE: Widely expressed during embryogenesis.
{ECO:0000269|PubMed:11435699}.
-!- INDUCTION: Down-regulated by digoxin.
{ECO:0000269|PubMed:16445568}.
-!- DISRUPTION PHENOTYPE: According to PubMed:16908670, mice are not
viable and heterozygous knockout mice display impaired
phagocytosis of apoptotic cells. Depletion of Abca7 in macrophages
by RNAi reduces phagocytosis of apoptotic cells. According to
PubMed:15550377, mice are viable and females have less visceral
fat and lower total serum and high density lipoprotein cholesterol
level. {ECO:0000269|PubMed:15550377, ECO:0000269|PubMed:16908670}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF31434.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF287141; AAK56862.1; -; mRNA.
EMBL; AF287142; AAK56863.1; -; Genomic_DNA.
EMBL; AF213395; AAF31434.1; ALT_FRAME; mRNA.
CCDS; CCDS24004.1; -.
RefSeq; NP_038878.1; NM_013850.1.
RefSeq; XP_017169446.1; XM_017313957.1.
UniGene; Mm.103351; -.
ProteinModelPortal; Q91V24; -.
SMR; Q91V24; -.
IntAct; Q91V24; 1.
STRING; 10090.ENSMUSP00000043090; -.
iPTMnet; Q91V24; -.
PhosphoSitePlus; Q91V24; -.
SwissPalm; Q91V24; -.
EPD; Q91V24; -.
MaxQB; Q91V24; -.
PaxDb; Q91V24; -.
PRIDE; Q91V24; -.
Ensembl; ENSMUST00000043866; ENSMUSP00000043090; ENSMUSG00000035722.
Ensembl; ENSMUST00000132517; ENSMUSP00000115111; ENSMUSG00000035722.
GeneID; 27403; -.
KEGG; mmu:27403; -.
UCSC; uc007gba.1; mouse.
CTD; 10347; -.
MGI; MGI:1351646; Abca7.
eggNOG; KOG0059; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00760000118965; -.
HOVERGEN; HBG050436; -.
InParanoid; Q91V24; -.
KO; K05645; -.
Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
PRO; PR:Q91V24; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000035722; Expressed in 215 organ(s), highest expression level in dorsal pancreas.
ExpressionAtlas; Q91V24; baseline and differential.
Genevisible; Q91V24; MM.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0009986; C:cell surface; IDA:Alzheimers_University_of_Toronto.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0001891; C:phagocytic cup; IDA:Alzheimers_University_of_Toronto.
GO; GO:0005886; C:plasma membrane; ISS:Alzheimers_University_of_Toronto.
GO; GO:0032587; C:ruffle membrane; IDA:Alzheimers_University_of_Toronto.
GO; GO:0034188; F:apolipoprotein A-I receptor activity; IDA:Alzheimers_University_of_Toronto.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISO:MGI.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0090554; F:phosphatidylcholine-translocating ATPase activity; ISO:MGI.
GO; GO:0090556; F:phosphatidylserine-translocating ATPase activity; ISO:MGI.
GO; GO:0005548; F:phospholipid transporter activity; IDA:MGI.
GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IDA:Alzheimers_University_of_Toronto.
GO; GO:0033344; P:cholesterol efflux; ISS:Alzheimers_University_of_Toronto.
GO; GO:0034380; P:high-density lipoprotein particle assembly; ISS:Alzheimers_University_of_Toronto.
GO; GO:0006869; P:lipid transport; IBA:GO_Central.
GO; GO:0007613; P:memory; IMP:Alzheimers_University_of_Toronto.
GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IDA:Alzheimers_University_of_Toronto.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; IDA:Alzheimers_University_of_Toronto.
GO; GO:0018149; P:peptide cross-linking; IDA:Alzheimers_University_of_Toronto.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:0033700; P:phospholipid efflux; IDA:MGI.
GO; GO:0045332; P:phospholipid translocation; ISO:MGI.
GO; GO:1900223; P:positive regulation of amyloid-beta clearance; IMP:Alzheimers_University_of_Toronto.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IMP:Alzheimers_University_of_Toronto.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:Alzheimers_University_of_Toronto.
GO; GO:0050766; P:positive regulation of phagocytosis; IMP:Alzheimers_University_of_Toronto.
GO; GO:1902995; P:positive regulation of phospholipid efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:0034504; P:protein localization to nucleus; IDA:Alzheimers_University_of_Toronto.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR026082; ABCA.
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;
ATP-binding; Cell membrane; Complete proteome; Disulfide bond;
Endosome; Glycoprotein; Golgi apparatus; Membrane; Nucleotide-binding;
Phagocytosis; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 2159 ATP-binding cassette sub-family A member
7.
/FTId=PRO_0000250675.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TOPO_DOM 43 546 Extracellular. {ECO:0000250}.
TRANSMEM 547 567 Helical. {ECO:0000255}.
TRANSMEM 590 610 Helical. {ECO:0000255}.
TRANSMEM 623 643 Helical. {ECO:0000255}.
TRANSMEM 652 672 Helical. {ECO:0000255}.
TRANSMEM 678 698 Helical. {ECO:0000255}.
TRANSMEM 732 752 Helical. {ECO:0000255}.
TRANSMEM 846 866 Helical. {ECO:0000255}.
TRANSMEM 1246 1266 Helical. {ECO:0000255}.
TOPO_DOM 1267 1551 Extracellular. {ECO:0000250}.
TRANSMEM 1552 1572 Helical. {ECO:0000255}.
TRANSMEM 1598 1618 Helical. {ECO:0000255}.
TRANSMEM 1635 1655 Helical. {ECO:0000255}.
TRANSMEM 1663 1683 Helical. {ECO:0000255}.
TRANSMEM 1743 1763 Helical. {ECO:0000255}.
DOMAIN 804 1035 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 1807 2039 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 838 845 ATP 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 1841 1848 ATP 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 75 222 {ECO:0000250}.
DISULFID 1359 1373 {ECO:0000250}.
CONFLICT 1944 1944 N -> D (in Ref. 2; AAF31434).
{ECO:0000305}.
CONFLICT 2004 2004 A -> R (in Ref. 2; AAF31434).
{ECO:0000305}.
CONFLICT 2069 2069 L -> M (in Ref. 2; AAF31434).
{ECO:0000305}.
SEQUENCE 2159 AA; 236884 MW; CD2BE3FE0D8B822B CRC64;
MALGTQLMLL LWKNYTYRRR QPIQLLVELL WPLFLFFILV AVRHSHPPLE HHECHFPNKP
LPSAGTVPWL QGLVCNVNNS CFQHPTPGEK PGVLSNFKDS LISRLLADTR TVLGGHSIQD
MLDALGKLIP VLRAVGGGAR PQESDQPTSQ GSVTKLLEKI LQRASLDPVL GQAQDSMRKF
SDAIRDLAQE LLTLPSLMEL RALLRRPRGS AGSLELVSEA LCSTKGPSSP GGLSLNWYEA
NQLNEFMGPE VAPALPDNSL SPACSEFVGT LDDHPVSRLL WRRLKPLILG KILFAPDTNF
TRKLMAQVNQ TFEELALLRD LHELWGVLGP QIFNFMNDST NVAMLQRLLD VGGTGQRQQT
PRAQKKLEAI KDFLDPSRGG YSWREAHADM GRLAGILGQM MECVSLDKLE AVPSEEALVS
RALELLGERR LWAGIVFLSP EHPLDPSELS SPALSPGHLR FKIRMDIDDV TRTNKIRDKF
WDPGPSADPF MDLRYVWGGF VYLQDLLEQA AVRVLGGGNS RTGLYLQQMP HPCYVDDVFL
RVLSRSLPLF LTLAWIYSVA LTVKAVVREK ETRLRETMRA MGLSRAVLWL GWFLSCLGPF
LVSAALLVLV LKLGNILPYS HPVVIFLFLA AFAVATVAQS FLLSAFFSRA NLAAACGGLA
YFALYLPYVL CVAWRERLHL GGLLAASLLS PVAFGFGCES LALLEEQGDG AQWHNLGTGP
AEDVFSLAQV SAFLLLDAVI YGLALWYLEA VCPGQYGIPE PWNFPFRRSY WCGPGPPKSS
VLAPAPQDPK VLVEEPPLGL VPGVSIRGLK KHFRGCPQPA LQGLNLDFYE GHITAFLGHN
GAGKTTTLSI LSGLFPPSSG SASILGHDVQ TNMAAIRPHL GICPQYNVLF DMLTVEEHVW
FYGRLKGVSA AAMGPERERL IRDVGLTLKR DTQTRHLSGG MQRKLSVAIA FVGGSRVVIM
DEPTAGVDPA SRRGIWELLL KYREGRTLIL STHHLDEAEL LGDRVAMVAG GSLCCCGSPL
FLRRHLGCGY YLTLVKSSQS LVTHDAKGDS EDPRREKKSD GNGRTSDTAF TRGTSDKSNQ
APAPGAVPIT PSTARILELV QQHVPGAQLV EDLPHELLLV LPYAGALDGS FAMVFQELDQ
QLELLGLTGY GISDTNLEEI FLKVVEDAHR EGGDSRPQLH LRTCTPQPPT GPEASVLENG
ELAPQGLAPN AAQVQGWTLT CQQLRALLHK RFLLARRSRR GLFAQVVLPA LFVGLALFFS
LIVPPFGQYP PLQLSPAMYG PQVSFFSEDA PGDPNRMKLL EALLGEAGLQ EPSMQDKDAR
GSECTHSLAC YFTVPEVPPD VASILASGNW TPESPSPACQ CSQPGARRLL PDCPAGAGGP
PPPQAVAGLG EVVQNLTGRN VSDFLVKTYP SLVRRGLKTK KWVDEVRYGG FSLGGRDPDL
PTGHEVVRTL AEIRALLSPQ PGNALDRILN NLTQWALGLD ARNSLKIWFN NKGWHAMVAF
VNRANNGLLH ALLPSGPVRH AHSITTLNHP LNLTKEQLSE ATLIASSVDV LVSICVVFAM
SFVPASFTLV LIEERITRAK HLQLVSGLPQ TLYWLGNFLW DMCNYLVAVC IVVFIFLAFQ
QRAYVAPENL PALLLLLLLY GWSITPLMYP ASFFFSVPST AYVVLTCINL FIGINSSMAT
FVLELLSDQN LQEVSRILKQ VFLIFPHFCL GRGLIDMVRN QAMADAFERL GDKQFQSPLR
WDIIGKNLLA MMAQGPLFLL ITLLLQHRNR LLPQSKPRLL PPLGEEDEDV AQERERVTKG
ATQGDVLVLR DLTKVYRGQR NPAVDRLCLG IPPGECFGLL GVNGAGKTST FRMVTGDTLP
SSGEAVLAGH NVAQERSAAH RSMGYCPQSD AIFDLLTGRE HLELFARLRG VPEAQVAQTA
LSGLVRLGLP SYADRPAGTY SGGNKRKLAT ALALVGDPAV VFLDEPTTGM DPSARRFLWN
SLLSVVREGR SVVLTSHSME ECEALCTRLA IMVNGRFRCL GSSQHLKGRF GAGHTLTLRV
PPDQPEPAIA FIRITFPGAE LREVHGSRLR FQLPPGGRCT LTRVFRELAA QGRAHGVEDF
SVSQTTLEEV FLYFSKDQGE EEESSRQEAE EEEVSKPGRQ HPKRVSRFLE DPSSVETMI


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