ABCA7_RAT
ID ABCA7_RAT Reviewed; 2170 AA.
AC Q7TNJ2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=ATP-binding cassette sub-family A member 7;
GN Name=Abca7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Platelet;
RX PubMed=12727224; DOI=10.1016/s0006-291x(03)00659-4;
RA Sasaki M., Shoji A., Kubo Y., Nada S., Yamaguchi A.;
RT "Cloning of rat ABCA7 and its preferential expression in platelets.";
RL Biochem. Biophys. Res. Commun. 304:777-782(2003).
CC -!- FUNCTION: ATP-binding cassette (ABC) transporter that plays a role in
CC lipid homeostasis and macrophage-mediated phagocytosis (By similarity).
CC Binds APOA1 and may function in apolipoprotein-mediated phospholipid
CC efflux from cells (By similarity). May also mediate cholesterol efflux
CC (By similarity). May regulate cellular ceramide homeostasis during
CC keratinocyte differentiation (By similarity). Involved in lipid raft
CC organization and CD1D localization on thymocytes and antigen-presenting
CC cells, which plays an important role in natural killer T-cell
CC development and activation (By similarity). Plays a role in
CC phagocytosis of apoptotic cells by macrophages (By similarity).
CC Macrophage phagocytosis is stimulated by APOA1 or APOA2, probably by
CC stabilization of ABCA7 (By similarity). Also involved in phagocytic
CC clearance of amyloid-beta by microglia cells and macrophages (By
CC similarity). Further limits amyloid-beta production by playing a role
CC in the regulation of amyloid-beta A4 precursor protein (APP)
CC endocytosis and/or processing (By similarity).
CC {ECO:0000250|UniProtKB:Q8IZY2, ECO:0000250|UniProtKB:Q91V24}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12727224};
CC Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:12727224}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q91V24};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, ruffle
CC membrane {ECO:0000250|UniProtKB:Q91V24}. Cell projection, phagocytic
CC cup {ECO:0000250|UniProtKB:Q91V24}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q91V24}. Note=Localizes to cell membrane ruffles
CC and phagocytic cups of macrophages stimulated with C1q or apoptotic
CC cells. Localizes to the cytoplasm of resting macrophages, probably in
CC Golgi and endosomes. Localizes to the apical brush border of cells in
CC the proximal tubules of kidney. {ECO:0000250|UniProtKB:Q91V24}.
CC -!- TISSUE SPECIFICITY: Expressed in blood cells. Also detected in brain
CC and ovary tissues (at protein level). Expressed in platelet.
CC {ECO:0000269|PubMed:12727224}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q91V24}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
CC -!- CAUTION: There are conflicting results concerning the role of ABCA7 in
CC lipid transport. ABCA7 was described to play a role in apolipoprotein-
CC mediated phospholipid and cholesterol efflux when expressed in HEK293
CC cells (By similarity). However, another report shows that ABCA7
CC deficiency does not influence cholesterol and phospholipid efflux in
CC mouse primary macrophages, but leads to lower serum HDL cholesterol
CC levels and a reduction in fat mass in female mice (By similarity).
CC {ECO:0000250|UniProtKB:Q8IZY2, ECO:0000250|UniProtKB:Q91V24}.
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DR EMBL; AB097814; BAC81426.1; -; mRNA.
DR RefSeq; NP_997481.1; NM_207598.1.
DR AlphaFoldDB; Q7TNJ2; -.
DR SMR; Q7TNJ2; -.
DR BioGRID; 256273; 1.
DR IntAct; Q7TNJ2; 1.
DR MINT; Q7TNJ2; -.
DR STRING; 10116.ENSRNOP00000063805; -.
DR GlyGen; Q7TNJ2; 1 site.
DR iPTMnet; Q7TNJ2; -.
DR PhosphoSitePlus; Q7TNJ2; -.
DR PaxDb; Q7TNJ2; -.
DR PRIDE; Q7TNJ2; -.
DR GeneID; 299609; -.
DR KEGG; rno:299609; -.
DR UCSC; RGD:1303134; rat.
DR CTD; 10347; -.
DR RGD; 1303134; Abca7.
DR eggNOG; KOG0059; Eukaryota.
DR InParanoid; Q7TNJ2; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; Q7TNJ2; -.
DR Reactome; R-RNO-1369062; ABC transporters in lipid homeostasis.
DR PRO; PR:Q7TNJ2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097386; C:glial cell projection; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0001891; C:phagocytic cup; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0034188; F:apolipoprotein A-I receptor activity; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0140328; F:floppase activity; ISO:RGD.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; ISO:RGD.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; ISO:RGD.
DR GO; GO:0005548; F:phospholipid transporter activity; ISO:RGD.
DR GO; GO:0150094; P:amyloid-beta clearance by cellular catabolic process; ISS:UniProtKB.
DR GO; GO:0034205; P:amyloid-beta formation; ISS:UniProtKB.
DR GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0033344; P:cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0007613; P:memory; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISS:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; ISO:RGD.
DR GO; GO:1903898; P:negative regulation of PERK-mediated unfolded protein response; ISO:RGD.
DR GO; GO:0018149; P:peptide cross-linking; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:0033700; P:phospholipid efflux; ISS:UniProtKB.
DR GO; GO:0045332; P:phospholipid translocation; ISO:RGD.
DR GO; GO:0044857; P:plasma membrane raft organization; ISS:UniProtKB.
DR GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:1902995; P:positive regulation of phospholipid efflux; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:1902991; P:regulation of amyloid precursor protein catabolic process; ISS:UniProtKB.
DR GO; GO:0019216; P:regulation of lipid metabolic process; ISO:RGD.
DR GO; GO:0008542; P:visual learning; ISO:RGD.
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; IPR030369; ABCA7.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR PANTHER; PTHR19229:SF49; PTHR19229:SF49; 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; Cell projection; Cytoplasm; Disulfide bond;
KW Endosome; Glycoprotein; Golgi apparatus; Lipid transport; Membrane;
KW Nucleotide-binding; Phagocytosis; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..2170
FT /note="ATP-binding cassette sub-family A member 7"
FT /id="PRO_0000250676"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..547
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 624..644
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 653..673
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 733..753
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 847..867
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1257..1277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1278..1562
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1563..1583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1609..1629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1646..1666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1674..1694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1708..1728
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1754..1774
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 805..1036
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1818..2050
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1044..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2129..2170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 839..846
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1852..1859
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..222
FT /evidence="ECO:0000250"
FT DISULFID 1370..1384
FT /evidence="ECO:0000250"
SQ SEQUENCE 2170 AA; 237720 MW; 003C8DF70B8744CE CRC64;
MAFCTQLMLL LWKNYTYRRR QPIQLVVELL WPLFLFFILV AVRHSHPPLE HHECHFPNKP
LPSAGTVPWL QGLVCNVNNS CFQHPTPGEK PGVLSNFKDS LISRLLADAH TVLGGHSTQD
MLAALGKLIP VLRAVGSGAW PQESNQPAKQ GSVTELLEKI LQRASLETVL GQAQDSMRKF
SDATRTVAQE LLTLPSLVEL RALLRRPRGS AGSLELISEA LCSTKGPSSP GGLSLNWYEA
NQINEFMGPE LAPTLPDSSL SPACSEFVGA LDDHPVSRLL WRRLKPLILG KILFAPDTNF
TRKLMAQVNQ TFEELALLRD LHELWGVLGP QIFNFMNDST NVAMLQKLLD VEGTGWQQQT
PKGQKQLEAI RDFLDPSRGR YNWQEAHADM GRLAEILGQI LECVSLDKLE AVPSEEALVS
RALELLGERR LWAGIVFLSP EHPLDSSEPP SPTTTGPGHL RVKIRMDIDD VTRTNKIRDK
FWDPGPSADP LMDLRYVWGG FVYLQDLLEQ AAVRVLSGRD SRAGLYLQQM PHPCYVDDVF
LRVLSRSLPL FLTLAWIYSV ALTVKAVVRE KETRLRETMR AMGLSRAVLW LGWFLSCLGP
FLVSAALLVL VLKLGNILPY SHPVVVFLFL AAFAVATVAQ SFLLSAFFSR ANLAAACGGL
AYFALYLPYV LCVAWRERLP LGGLLAVSLL SPVAFGFGCE SLALLEEQGD GAQWHNLGTG
PAEDVFSLAQ VSAFLLLDAV IYGLALWYLE AVCPGQYGIP EPWNFPFRRS YWCGPGPPKS
SVLAPAPQDP KVLVEEPPPG LVPGVSIRGL KKHFRGSPQP ALRGLNLDFY EGHITAFLGH
NGAGKTTTLS ILSGLFPPSS GSASILGHDV QTNMAAIRPH LGICPQYNVL FDMLTVEEHV
WFYGRLKGVS AAAIDSEQEH LIRDVGLIPK RDTQTRHLSG GMQRKLSVAI AFVGGSRVVI
MDEPTAGVDP ASRRGIWELL LKYREGRTLI LSTHHLDEAE LLGDRVAMVA SGSLCCCGSP
LFLRRHLGCG YYLTLVKSSQ SLVTHDLKGD TEDPRREKKS GSEGKTADTV LTRDGPHRSS
QVPAPDAVPV TPSAALILEL VQRHVPGAQL VEELPHELVL ALPYAGALDG SFATVFQELD
QQLERLGLTG YGISDTNLEE IFLKVVEEAH AHGEGGDPRQ QQHLLTATPQ PHTGPEASVL
ENGELAKLVL DPQAPKGSAP TTAQVQGWTL TCQQLRALLH KRFLLARRSR RGLFAQIVLP
ALFVGLALFF TLIVPPFGQY PPLQLSPAMY GPQVSFFSED APADPNRMKL LEALLGEAGL
QDPSVQGKGS RGSECTHSLA CYFTVPEVPP DVASILASGN WTPDSPSPAC QCSQPGARRL
LPDCPAGAGG PPPPQAMAGF GEVVQNLTGR NVSDFLVKTY PSLVRRGLKT KKWVDEVRYG
GFSLGGRDPD LPSGREVVRT VAEMRALLSP QPGNTLDRIL NNLTQWALGL DARNSLKIWF
NNKGWHAMVA FVNRANNGLL RAFLPSGSVR HAHSITTLNH PLNLTKEQLS EATLIASSVD
VLVSICVVFA MSFVPASFTL VLIEERITRA KHLQLVSGLP QTLYWLGNFL WDMCNYLVAV
CIVVLIFLAF QQKAYVAPEN LPALLLLLLL YGWSITPLMY PASFFFSVPS TAYVVLTCIN
LFIGINSSMA TFVLELLSDQ NLQEVSRILK QVFLIFPHFC LGRGLIDMVR NQAMADAFER
LGDKQFQSPL RWDIIGKNLL AMVAQGPLFL LITLLLQHRN RLLPQPKSRL PPPLGEEDED
VVRERERVTK GATQGDVLVL RDLTKVYRGQ RSPAVDHLCL GIPPGECFGL LGVNGAGKTS
TFRMVTGDTL PSSGEAVLAG HNVAQEPSAA HRSMGYCPQS DAIFDLLTGR EHLELFARLR
GVPEAQVAQT ALSGLVRLGL PSYADRPAGT YSGGNKRKLA TALALVGDPA VVFLDEPTTG
MDPSARRFLW NNLLSVVREG RSVVLTSHSM EECEALCTRL AIMVNGRFRC LGSAQHLKSR
FGAGHTLTLR VPPDQPEPAI AFIVTTFPDA ELREVHGSRL RFQLPPGGGC TLARVFRELA
AQGKAHGVED FSVSQTTLEE VFLYFSKDQG EEEEGSGQET ETREVSTPGL QHPKRVSRFL
EDPSSVETVI
