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3.A.1.211.10
ABCA7. Regulates cellular efflux of phospholipids but not cholesterol, to apo A-1 (Voloshyna and Reiss, 2011).  Associated with late-onset Alzheimer's disease, possibly by influencing amyloid-β (Abeta) accumulation (Zhao et al. 2014).  Known functions of ABCA7 are summarized in Zhao et al. 2014 and Sakamoto et al. 2019.

Accession Number:Q8IZY2
Protein Name:ATP-binding cassette sub-family A member 7
Length:2146
Molecular Weight:234350.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:13
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate phospholipids

Cross database links:

Genevestigator: Q8IZY2
eggNOG: COG1131
HEGENOM: HOG000231547
Entrez Gene ID: 10347   
Pfam: PF00005   
KEGG: hsa:10347   

Gene Ontology

GO:0016324 C:apical plasma membrane
GO:0043190 C:ATP-binding cassette (ABC) transporter complex
GO:0010008 C:endosome membrane
GO:0000139 C:Golgi membrane
GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0005524 F:ATP binding
GO:0016887 F:ATPase activity
GO:0005548 F:phospholipid transporter activity
GO:0005215 F:transporter activity
GO:0006200 P:ATP catabolic process
GO:0006909 P:phagocytosis
GO:0033700 P:phospholipid efflux
GO:0055085 P:transmembrane transport

References (10)

[1] “Identification of a novel human sterol-sensitive ATP-binding cassette transporter (ABCA7).”  Kaminski W.E.et.al.   10873640
[2] “Genomic organization of the human cholesterol-responsive ABC transporter ABCA7: tandem linkage with the minor histocompatibility antigen HA-1 gene.”  Kaminski W.E.et.al.   11095984
[3] “Human ABCA1 contains a large amino-terminal extracellular domain homologous to an epitope of Sjogren's Syndrome.”  Tanaka A.R.et.al.   11355874
[4] “Comparative analysis of the promoter structure and genomic organization of the human and mouse ABCA7 gene encoding a novel ABCA transporter.”  Broccardo C.et.al.   11435699
[5] “The DNA sequence and biology of human chromosome 19.”  Grimwood J.et.al.   15057824
[6] “Posttranscriptional regulation of human ABCA7 and its function for the apoA-I-dependent lipid release.”  Ikeda Y.et.al.   14592415
[7] “ATP-binding cassette transporter A7 (ABCA7) binds apolipoprotein A-I and mediates cellular phospholipid but not cholesterol efflux.”  Wang N.et.al.   12917409
[8] “Adenosine triphosphate binding cassette (ABC) transporters are expressed and regulated during terminal keratinocyte differentiation: a potential role for ABCA7 in epidermal lipid reorganization.”  Kielar D.et.al.   12925201
[9] “Human ABCA7 supports apolipoprotein-mediated release of cellular cholesterol and phospholipid to generate high density lipoprotein.”  Abe-Dohmae S.et.al.   14570867
[10] “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.”  Iida A.et.al.   12111378

External Searches:

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  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MAFWTQLMLL LWKNFMYRRR QPVQLLVELL WPLFLFFILV AVRHSHPPLE HHECHFPNKP 
61:	LPSAGTVPWL QGLICNVNNT CFPQLTPGEE PGRLSNFNDS LVSRLLADAR TVLGGASAHR 
121:	TLAGLGKLIA TLRAARSTAQ PQPTKQSPLE PPMLDVAELL TSLLRTESLG LALGQAQEPL 
181:	HSLLEAAEDL AQELLALRSL VELRALLQRP RGTSGPLELL SEALCSVRGP SSTVGPSLNW 
241:	YEASDLMELV GQEPESALPD SSLSPACSEL IGALDSHPLS RLLWRRLKPL ILGKLLFAPD 
301:	TPFTRKLMAQ VNRTFEELTL LRDVREVWEM LGPRIFTFMN DSSNVAMLQR LLQMQDEGRR 
361:	QPRPGGRDHM EALRSFLDPG SGGYSWQDAH ADVGHLVGTL GRVTECLSLD KLEAAPSEAA 
421:	LVSRALQLLA EHRFWAGVVF LGPEDSSDPT EHPTPDLGPG HVRIKIRMDI DVVTRTNKIR 
481:	DRFWDPGPAA DPLTDLRYVW GGFVYLQDLV ERAAVRVLSG ANPRAGLYLQ QMPYPCYVDD 
541:	VFLRVLSRSL PLFLTLAWIY SVTLTVKAVV REKETRLRDT MRAMGLSRAV LWLGWFLSCL 
601:	GPFLLSAALL VLVLKLGDIL PYSHPGVVFL FLAAFAVATV TQSFLLSAFF SRANLAAACG 
661:	GLAYFSLYLP YVLCVAWRDR LPAGGRVAAS LLSPVAFGFG CESLALLEEQ GEGAQWHNVG 
721:	TRPTADVFSL AQVSGLLLLD AALYGLATWY LEAVCPGQYG IPEPWNFPFR RSYWCGPRPP 
781:	KSPAPCPTPL DPKVLVEEAP PGLSPGVSVR SLEKRFPGSP QPALRGLSLD FYQGHITAFL 
841:	GHNGAGKTTT LSILSGLFPP SGGSAFILGH DVRSSMAAIR PHLGVCPQYN VLFDMLTVDE 
901:	HVWFYGRLKG LSAAVVGPEQ DRLLQDVGLV SKQSVQTRHL SGGMQRKLSV AIAFVGGSQV 
961:	VILDEPTAGV DPASRRGIWE LLLKYREGRT LILSTHHLDE AELLGDRVAV VAGGRLCCCG 
1021:	SPLFLRRHLG SGYYLTLVKA RLPLTTNEKA DTDMEGSVDT RQEKKNGSQG SRVGTPQLLA 
1081:	LVQHWVPGAR LVEELPHELV LVLPYTGAHD GSFATLFREL DTRLAELRLT GYGISDTSLE 
1141:	EIFLKVVEEC AADTDMEDGS CGQHLCTGIA GLDVTLRLKM PPQETALENG EPAGSAPETD 
1201:	QGSGPDAVGR VQGWALTRQQ LQALLLKRFL LARRSRRGLF AQIVLPALFV GLALVFSLIV 
1261:	PPFGHYPALR LSPTMYGAQV SFFSEDAPGD PGRARLLEAL LQEAGLEEPP VQHSSHRFSA 
1321:	PEVPAEVAKV LASGNWTPES PSPACQCSRP GARRLLPDCP AAAGGPPPPQ AVTGSGEVVQ 
1381:	NLTGRNLSDF LVKTYPRLVR QGLKTKKWVN EVRYGGFSLG GRDPGLPSGQ ELGRSVEELW 
1441:	ALLSPLPGGA LDRVLKNLTA WAHSLDAQDS LKIWFNNKGW HSMVAFVNRA SNAILRAHLP 
1501:	PGPARHAHSI TTLNHPLNLT KEQLSEGALM ASSVDVLVSI CVVFAMSFVP ASFTLVLIEE 
1561:	RVTRAKHLQL MGGLSPTLYW LGNFLWDMCN YLVPACIVVL IFLAFQQRAY VAPANLPALL 
1621:	LLLLLYGWSI TPLMYPASFF FSVPSTAYVV LTCINLFIGI NGSMATFVLE LFSDQKLQEV 
1681:	SRILKQVFLI FPHFCLGRGL IDMVRNQAMA DAFERLGDRQ FQSPLRWEVV GKNLLAMVIQ 
1741:	GPLFLLFTLL LQHRSQLLPQ PRVRSLPLLG EEDEDVARER ERVVQGATQG DVLVLRNLTK 
1801:	VYRGQRMPAV DRLCLGIPPG ECFGLLGVNG AGKTSTFRMV TGDTLASRGE AVLAGHSVAR 
1861:	EPSAAHLSMG YCPQSDAIFE LLTGREHLEL LARLRGVPEA QVAQTAGSGL ARLGLSWYAD 
1921:	RPAGTYSGGN KRKLATALAL VGDPAVVFLD EPTTGMDPSA RRFLWNSLLA VVREGRSVML 
1981:	TSHSMEECEA LCSRLAIMVN GRFRCLGSPQ HLKGRFAAGH TLTLRVPAAR SQPAAAFVAA 
2041:	EFPGAELREA HGGRLRFQLP PGGRCALARV FGELAVHGAE HGVEDFSVSQ TMLEEVFLYF 
2101:	SKDQGKDEDT EEQKEAGVGV DPAPGLQHPK RVSQFLDDPS TAETVL