Q8IZY2 (ABCA7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-binding cassette sub-family A member 7

Alternative name(s):
ABCA-SSN
Autoantigen SS-N
Macrophage ABC transporter

Gene names

Name:

ABCA7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2146 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.7 Ref.8 Ref.9 Ref.10
Subcellular location	Cell membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein. 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. Isoform 2 may localize to the endoplasmic reticulum. Ref.7 Ref.8 Ref.10
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. Ref.1 Ref.4 Ref.7
Developmental stage	Expressed in fetal tissues. Strongly expressed in fetal liver. Ref.1 Ref.4
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. Ref.1 Ref.9
Sequence similarities	Belongs to the ABC transporter superfamily. ABCA family. Contains 2 ABC transporter domains.

Ontologies

Keywords
Biological process	Phagocytosis Transport
Cellular component	Cell membrane Endosome Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC phagocytosis Inferred from electronic annotation. Source: UniProtKB-KW phospholipid efflux Inferred from electronic annotation. Source: Compara transmembrane transport Traceable author statement. Source: Reactome
Cellular_component	ATP-binding cassette (ABC) transporter complex Traceable author statement Ref.1. Source: ProtInc Golgi apparatus Inferred from direct assay. Source: HPA Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell apical plasma membrane Inferred from electronic annotation. Source: Compara endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Traceable author statement Ref.1. Source: ProtInc plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Traceable author statement Ref.1. Source: ProtInc ATPase activity Inferred from electronic annotation. Source: InterPro phospholipid transporter activity Inferred from electronic annotation. Source: Compara transporter activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8IZY2-1)

Also known as: Type 1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8IZY2-2)

Also known as: Type 2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: Missing.
     139-166: AQPQPTKQSPLEPPMLDVAELLTSLLRT → MVCLGTGQSAGPLVSVQNHCPPCGLSPQ

Note: Inactive for apoA-I-mediated lipid release.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2146	2146	ATP-binding cassette sub-family A member 7		PRO_0000250674
Regions
	Transmembrane	22 – 42	21	Helical; Potential
	Topological domain	43 – 549	507	Extracellular By similarity
	Transmembrane	550 – 570	21	Helical; Potential
	Transmembrane	593 – 613	21	Helical; Potential
	Transmembrane	626 – 646	21	Helical; Potential
	Transmembrane	655 – 675	21	Helical; Potential
	Transmembrane	687 – 707	21	Helical; Potential
	Transmembrane	727 – 747	21	Helical; Potential
	Transmembrane	849 – 869	21	Helical; Potential
	Transmembrane	1243 – 1263	21	Helical; Potential
	Topological domain	1264 – 1537	274	Extracellular By similarity
	Transmembrane	1538 – 1558	21	Helical; Potential
	Transmembrane	1584 – 1604	21	Helical; Potential
	Transmembrane	1621 – 1641	21	Helical; Potential
	Transmembrane	1649 – 1669	21	Helical; Potential
	Transmembrane	1683 – 1703	21	Helical; Potential
	Transmembrane	1729 – 1749	21	Helical; Potential
	Domain	807 – 1038	232	ABC transporter 1
	Domain	1793 – 2025	233	ABC transporter 2
	Nucleotide binding	841 – 848	8	ATP 1 Potential
	Nucleotide binding	1827 – 1834	8	ATP 2 Potential
Amino acid modifications
	Glycosylation	312	1	N-linked (GlcNAc...) Potential
	Disulfide bond	75 ↔ 225		By similarity
	Disulfide bond	1345 ↔ 1359		By similarity
Natural variations
	Alternative sequence	1 – 138	138	Missing in isoform 2.		VSP_020701
	Alternative sequence	139 – 166	28	AQPQP…SLLRT → MVCLGTGQSAGPLVSVQNHC PPCGLSPQ in isoform 2.		VSP_020702
	Natural variant	188	1	E → G. Ref.4 Ref.11 Corresponds to variant rs3764645 [ dbSNP | Ensembl ].		VAR_027581
	Natural variant	319	1	T → A. Ref.11 Corresponds to variant rs3752232 [ dbSNP | Ensembl ].		VAR_027582
	Natural variant	395	1	H → R. Ref.11 Corresponds to variant rs3764647 [ dbSNP | Ensembl ].		VAR_027583
	Natural variant	463	1	R → H. Ref.11 Corresponds to variant rs3752233 [ dbSNP | Ensembl ].		VAR_027584
	Natural variant	676	1	A → T. Corresponds to variant rs59851484 [ dbSNP | Ensembl ].		VAR_060985
	Natural variant	718	1	N → T. Ref.11 Corresponds to variant rs3752239 [ dbSNP | Ensembl ].		VAR_027585
	Natural variant	1349	1	R → Q. Ref.1 Ref.3 Ref.11 Corresponds to variant rs3745842 [ dbSNP | Ensembl ].		VAR_027586
	Natural variant	1527	1	G → A. Ref.1 Ref.2 Ref.3 Ref.4 Corresponds to variant rs3752246 [ dbSNP | Ensembl ].		VAR_027587
	Natural variant	1686	1	Q → R. Ref.11 Corresponds to variant rs4147918 [ dbSNP | Ensembl ].		VAR_027588
	Natural variant	2045	1	A → S. Ref.1 Ref.3 Ref.4 Ref.11 Corresponds to variant rs4147934 [ dbSNP | Ensembl ].		VAR_027589
Experimental info
	Sequence conflict	1503	1	P → R in AAF85794. Ref.1
	Sequence conflict	1503	1	P → R in BAB62294. Ref.3
	Sequence conflict	1525	1	S → F in AAF85794. Ref.1
	Sequence conflict	1525	1	S → F in AAN04657. Ref.2
	Sequence conflict	1525	1	S → F in BAB62294. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Type 1) [UniParc]. Last modified December 4, 2007. Version 3. Checksum: 6EA624088E74FEE6	FASTA	2,146	234,350
	10 20 30 40 50 60 MAFWTQLMLL LWKNFMYRRR QPVQLLVELL WPLFLFFILV AVRHSHPPLE HHECHFPNKP 70 80 90 100 110 120 LPSAGTVPWL QGLICNVNNT CFPQLTPGEE PGRLSNFNDS LVSRLLADAR TVLGGASAHR 130 140 150 160 170 180 TLAGLGKLIA TLRAARSTAQ PQPTKQSPLE PPMLDVAELL TSLLRTESLG LALGQAQEPL 190 200 210 220 230 240 HSLLEAAEDL AQELLALRSL VELRALLQRP RGTSGPLELL SEALCSVRGP SSTVGPSLNW 250 260 270 280 290 300 YEASDLMELV GQEPESALPD SSLSPACSEL IGALDSHPLS RLLWRRLKPL ILGKLLFAPD 310 320 330 340 350 360 TPFTRKLMAQ VNRTFEELTL LRDVREVWEM LGPRIFTFMN DSSNVAMLQR LLQMQDEGRR 370 380 390 400 410 420 QPRPGGRDHM EALRSFLDPG SGGYSWQDAH ADVGHLVGTL GRVTECLSLD KLEAAPSEAA 430 440 450 460 470 480 LVSRALQLLA EHRFWAGVVF LGPEDSSDPT EHPTPDLGPG HVRIKIRMDI DVVTRTNKIR 490 500 510 520 530 540 DRFWDPGPAA DPLTDLRYVW GGFVYLQDLV ERAAVRVLSG ANPRAGLYLQ QMPYPCYVDD 550 560 570 580 590 600 VFLRVLSRSL PLFLTLAWIY SVTLTVKAVV REKETRLRDT MRAMGLSRAV LWLGWFLSCL 610 620 630 640 650 660 GPFLLSAALL VLVLKLGDIL PYSHPGVVFL FLAAFAVATV TQSFLLSAFF SRANLAAACG 670 680 690 700 710 720 GLAYFSLYLP YVLCVAWRDR LPAGGRVAAS LLSPVAFGFG CESLALLEEQ GEGAQWHNVG 730 740 750 760 770 780 TRPTADVFSL AQVSGLLLLD AALYGLATWY LEAVCPGQYG IPEPWNFPFR RSYWCGPRPP 790 800 810 820 830 840 KSPAPCPTPL DPKVLVEEAP PGLSPGVSVR SLEKRFPGSP QPALRGLSLD FYQGHITAFL 850 860 870 880 890 900 GHNGAGKTTT LSILSGLFPP SGGSAFILGH DVRSSMAAIR PHLGVCPQYN VLFDMLTVDE 910 920 930 940 950 960 HVWFYGRLKG LSAAVVGPEQ DRLLQDVGLV SKQSVQTRHL SGGMQRKLSV AIAFVGGSQV 970 980 990 1000 1010 1020 VILDEPTAGV DPASRRGIWE LLLKYREGRT LILSTHHLDE AELLGDRVAV VAGGRLCCCG 1030 1040 1050 1060 1070 1080 SPLFLRRHLG SGYYLTLVKA RLPLTTNEKA DTDMEGSVDT RQEKKNGSQG SRVGTPQLLA 1090 1100 1110 1120 1130 1140 LVQHWVPGAR LVEELPHELV LVLPYTGAHD GSFATLFREL DTRLAELRLT GYGISDTSLE 1150 1160 1170 1180 1190 1200 EIFLKVVEEC AADTDMEDGS CGQHLCTGIA GLDVTLRLKM PPQETALENG EPAGSAPETD 1210 1220 1230 1240 1250 1260 QGSGPDAVGR VQGWALTRQQ LQALLLKRFL LARRSRRGLF AQIVLPALFV GLALVFSLIV 1270 1280 1290 1300 1310 1320 PPFGHYPALR LSPTMYGAQV SFFSEDAPGD PGRARLLEAL LQEAGLEEPP VQHSSHRFSA 1330 1340 1350 1360 1370 1380 PEVPAEVAKV LASGNWTPES PSPACQCSRP GARRLLPDCP AAAGGPPPPQ AVTGSGEVVQ 1390 1400 1410 1420 1430 1440 NLTGRNLSDF LVKTYPRLVR QGLKTKKWVN EVRYGGFSLG GRDPGLPSGQ ELGRSVEELW 1450 1460 1470 1480 1490 1500 ALLSPLPGGA LDRVLKNLTA WAHSLDAQDS LKIWFNNKGW HSMVAFVNRA SNAILRAHLP 1510 1520 1530 1540 1550 1560 PGPARHAHSI TTLNHPLNLT KEQLSEGALM ASSVDVLVSI CVVFAMSFVP ASFTLVLIEE 1570 1580 1590 1600 1610 1620 RVTRAKHLQL MGGLSPTLYW LGNFLWDMCN YLVPACIVVL IFLAFQQRAY VAPANLPALL 1630 1640 1650 1660 1670 1680 LLLLLYGWSI TPLMYPASFF FSVPSTAYVV LTCINLFIGI NGSMATFVLE LFSDQKLQEV 1690 1700 1710 1720 1730 1740 SRILKQVFLI FPHFCLGRGL IDMVRNQAMA DAFERLGDRQ FQSPLRWEVV GKNLLAMVIQ 1750 1760 1770 1780 1790 1800 GPLFLLFTLL LQHRSQLLPQ PRVRSLPLLG EEDEDVARER ERVVQGATQG DVLVLRNLTK 1810 1820 1830 1840 1850 1860 VYRGQRMPAV DRLCLGIPPG ECFGLLGVNG AGKTSTFRMV TGDTLASRGE AVLAGHSVAR 1870 1880 1890 1900 1910 1920 EPSAAHLSMG YCPQSDAIFE LLTGREHLEL LARLRGVPEA QVAQTAGSGL ARLGLSWYAD 1930 1940 1950 1960 1970 1980 RPAGTYSGGN KRKLATALAL VGDPAVVFLD EPTTGMDPSA RRFLWNSLLA VVREGRSVML 1990 2000 2010 2020 2030 2040 TSHSMEECEA LCSRLAIMVN GRFRCLGSPQ HLKGRFAAGH TLTLRVPAAR SQPAAAFVAA 2050 2060 2070 2080 2090 2100 EFPGAELREA HGGRLRFQLP PGGRCALARV FGELAVHGAE HGVEDFSVSQ TMLEEVFLYF 2110 2120 2130 2140 SKDQGKDEDT EEQKEAGVGV DPAPGLQHPK RVSQFLDDPS TAETVL
	Isoform 2 (Type 2) [UniParc]. Checksum: 2B52CABF87220A7B	FASTA	2,008	218,497
	10 20 30 40 50 60 MVCLGTGQSA GPLVSVQNHC PPCGLSPQES LGLALGQAQE PLHSLLEAAE DLAQELLALR 70 80 90 100 110 120 SLVELRALLQ RPRGTSGPLE LLSEALCSVR GPSSTVGPSL NWYEASDLME LVGQEPESAL 130 140 150 160 170 180 PDSSLSPACS ELIGALDSHP LSRLLWRRLK PLILGKLLFA PDTPFTRKLM AQVNRTFEEL 190 200 210 220 230 240 TLLRDVREVW EMLGPRIFTF MNDSSNVAML QRLLQMQDEG RRQPRPGGRD HMEALRSFLD 250 260 270 280 290 300 PGSGGYSWQD AHADVGHLVG TLGRVTECLS LDKLEAAPSE AALVSRALQL LAEHRFWAGV 310 320 330 340 350 360 VFLGPEDSSD PTEHPTPDLG PGHVRIKIRM DIDVVTRTNK IRDRFWDPGP AADPLTDLRY 370 380 390 400 410 420 VWGGFVYLQD LVERAAVRVL SGANPRAGLY LQQMPYPCYV DDVFLRVLSR SLPLFLTLAW 430 440 450 460 470 480 IYSVTLTVKA VVREKETRLR DTMRAMGLSR AVLWLGWFLS CLGPFLLSAA LLVLVLKLGD 490 500 510 520 530 540 ILPYSHPGVV FLFLAAFAVA TVTQSFLLSA FFSRANLAAA CGGLAYFSLY LPYVLCVAWR 550 560 570 580 590 600 DRLPAGGRVA ASLLSPVAFG FGCESLALLE EQGEGAQWHN VGTRPTADVF SLAQVSGLLL 610 620 630 640 650 660 LDAALYGLAT WYLEAVCPGQ YGIPEPWNFP FRRSYWCGPR PPKSPAPCPT PLDPKVLVEE 670 680 690 700 710 720 APPGLSPGVS VRSLEKRFPG SPQPALRGLS LDFYQGHITA FLGHNGAGKT TTLSILSGLF 730 740 750 760 770 780 PPSGGSAFIL GHDVRSSMAA IRPHLGVCPQ YNVLFDMLTV DEHVWFYGRL KGLSAAVVGP 790 800 810 820 830 840 EQDRLLQDVG LVSKQSVQTR HLSGGMQRKL SVAIAFVGGS QVVILDEPTA GVDPASRRGI 850 860 870 880 890 900 WELLLKYREG RTLILSTHHL DEAELLGDRV AVVAGGRLCC CGSPLFLRRH LGSGYYLTLV 910 920 930 940 950 960 KARLPLTTNE KADTDMEGSV DTRQEKKNGS QGSRVGTPQL LALVQHWVPG ARLVEELPHE 970 980 990 1000 1010 1020 LVLVLPYTGA HDGSFATLFR ELDTRLAELR LTGYGISDTS LEEIFLKVVE ECAADTDMED 1030 1040 1050 1060 1070 1080 GSCGQHLCTG IAGLDVTLRL KMPPQETALE NGEPAGSAPE TDQGSGPDAV GRVQGWALTR 1090 1100 1110 1120 1130 1140 QQLQALLLKR FLLARRSRRG LFAQIVLPAL FVGLALVFSL IVPPFGHYPA LRLSPTMYGA 1150 1160 1170 1180 1190 1200 QVSFFSEDAP GDPGRARLLE ALLQEAGLEE PPVQHSSHRF SAPEVPAEVA KVLASGNWTP 1210 1220 1230 1240 1250 1260 ESPSPACQCS RPGARRLLPD CPAAAGGPPP PQAVTGSGEV VQNLTGRNLS DFLVKTYPRL 1270 1280 1290 1300 1310 1320 VRQGLKTKKW VNEVRYGGFS LGGRDPGLPS GQELGRSVEE LWALLSPLPG GALDRVLKNL 1330 1340 1350 1360 1370 1380 TAWAHSLDAQ DSLKIWFNNK GWHSMVAFVN RASNAILRAH LPPGPARHAH SITTLNHPLN 1390 1400 1410 1420 1430 1440 LTKEQLSEGA LMASSVDVLV SICVVFAMSF VPASFTLVLI EERVTRAKHL QLMGGLSPTL 1450 1460 1470 1480 1490 1500 YWLGNFLWDM CNYLVPACIV VLIFLAFQQR AYVAPANLPA LLLLLLLYGW SITPLMYPAS 1510 1520 1530 1540 1550 1560 FFFSVPSTAY VVLTCINLFI GINGSMATFV LELFSDQKLQ EVSRILKQVF LIFPHFCLGR 1570 1580 1590 1600 1610 1620 GLIDMVRNQA MADAFERLGD RQFQSPLRWE VVGKNLLAMV IQGPLFLLFT LLLQHRSQLL 1630 1640 1650 1660 1670 1680 PQPRVRSLPL LGEEDEDVAR ERERVVQGAT QGDVLVLRNL TKVYRGQRMP AVDRLCLGIP 1690 1700 1710 1720 1730 1740 PGECFGLLGV NGAGKTSTFR MVTGDTLASR GEAVLAGHSV AREPSAAHLS MGYCPQSDAI 1750 1760 1770 1780 1790 1800 FELLTGREHL ELLARLRGVP EAQVAQTAGS GLARLGLSWY ADRPAGTYSG GNKRKLATAL 1810 1820 1830 1840 1850 1860 ALVGDPAVVF LDEPTTGMDP SARRFLWNSL LAVVREGRSV MLTSHSMEEC EALCSRLAIM 1870 1880 1890 1900 1910 1920 VNGRFRCLGS PQHLKGRFAA GHTLTLRVPA ARSQPAAAFV AAEFPGAELR EAHGGRLRFQ 1930 1940 1950 1960 1970 1980 LPPGGRCALA RVFGELAVHG AEHGVEDFSV SQTMLEEVFL YFSKDQGKDE DTEEQKEAGV 1990 2000 GVDPAPGLQH PKRVSQFLDD PSTAETVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel human sterol-sensitive ATP-binding cassette transporter (ABCA7)." Kaminski W.E., Orso E., Diederich W., Klucken J., Drobnik W., Schmitz G. Biochem. Biophys. Res. Commun. 273:532-538(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-1349; ALA-1527 AND SER-2045, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION. Tissue: Macrophage.
[2]	"Genomic organization of the human cholesterol-responsive ABC transporter ABCA7: tandem linkage with the minor histocompatibility antigen HA-1 gene." Kaminski W.E., Piehler A., Schmitz G. Biochem. Biophys. Res. Commun. 278:782-789(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-1527.
[3]	"Human ABCA1 contains a large amino-terminal extracellular domain homologous to an epitope of Sjogren's Syndrome." 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. Biochem. Biophys. Res. Commun. 283:1019-1025(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS GLN-1349; ALA-1527 AND SER-2045. Tissue: Thymus.
[4]	"Comparative analysis of the promoter structure and genomic organization of the human and mouse ABCA7 gene encoding a novel ABCA transporter." 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. Cytogenet. Cell Genet. 92:264-270(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLY-188; ALA-1527 AND SER-2045, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Spleen.
[5]	"The DNA sequence and biology of human chromosome 19." 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. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Isolation of autoantigen cDNAs by lambda phage surface display." Niwa M., Maruyama M., Fujimoto T., Dohi K., Maruyama I.N. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 195-352 (ISOFORMS 1/2). Tissue: Cervix carcinoma.
[7]	"Posttranscriptional regulation of human ABCA7 and its function for the apoA-I-dependent lipid release." 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. Biochem. Biophys. Res. Commun. 311:313-318(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[8]	"ATP-binding cassette transporter A7 (ABCA7) binds apolipoprotein A-I and mediates cellular phospholipid but not cholesterol efflux." Wang N., Lan D., Gerbod-Giannone M., Linsel-Nitschke P., Jehle A.W., Chen W., Martinez L.O., Tall A.R. J. Biol. Chem. 278:42906-42912(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]	"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., 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. J. Invest. Dermatol. 121:465-474(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[10]	"Human ABCA7 supports apolipoprotein-mediated release of cellular cholesterol and phospholipid to generate high density lipoprotein." Abe-Dohmae S., Ikeda Y., Matsuo M., Hayashi M., Okuhira K., Ueda K., Yokoyama S. J. Biol. Chem. 279:604-611(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"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., Saito S., Sekine A., Mishima C., Kitamura Y., Kondo K., Harigae S., Osawa S., Nakamura Y. J. Hum. Genet. 47:285-310(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLY-188; ALA-319; ARG-395; HIS-463; THR-718; GLN-1349; ARG-1686 AND SER-2045.
+	Additional computationally mapped references.

Web resources

ABCMdb

Database for mutations in ABC proteins

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF250238 mRNA. Translation: AAF85794.1. AF311102 , AF311058, AF311059, AF311060, AF311061, AF311062, AF311063, AF311064, AF311065, AF311066, AF311067, AF311068, AF311057, AF311069, AF311070, AF311071, AF311072, AF311073, AF311074, AF311075, AF311076, AF311077, AF311078, AF311079, AF311080, AF311081, AF311082, AF311083, AF311084, AF311085, AF311086, AF311087, AF311088, AF311089, AF311090, AF311091, AF311092, AF311093, AF311094, AF311095, AF311096, AF311097, AF311098, AF311099, AF311100, AF311101 Genomic DNA. Translation: AAN04657.1. AB055390 mRNA. Translation: BAB62294.1. AF328787 mRNA. Translation: AAK00959.1. AC011558 Genomic DNA. No translation available. AF140342 mRNA. Translation: AAF06727.1.
IPI	IPI00020941. IPI00293895.
RefSeq	NP_061985.2. NM_019112.3.
UniGene	Hs.134514.
3D structure databases
ProteinModelPortal	Q8IZY2.
SMR	Q8IZY2. Positions 806-1032, 1792-2020.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8IZY2. 1 interaction.
STRING	9606.ENSP00000263094.
PTM databases
PhosphoSite	Q8IZY2.
Polymorphism databases
DMDM	161784300.
Proteomic databases
PaxDb	Q8IZY2.
PRIDE	Q8IZY2.
Protocols and materials databases
DNASU	10347.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263094; ENSP00000263094; ENSG00000064687. ENST00000433129; ENSP00000414062; ENSG00000064687. ENST00000435683; ENSP00000465322; ENSG00000064687.
GeneID	10347.
KEGG	hsa:10347.
UCSC	uc002lqw.4. human. uc010dsb.1. human.
Organism-specific databases
CTD	10347.
GeneCards	GC19P001040.
H-InvDB	HIX0014569.
HGNC	HGNC:37. ABCA7.
HPA	HPA041564.
MIM	605414. gene.
neXtProt	NX_Q8IZY2.
PharmGKB	PA24382.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1131.
HOGENOM	HOG000231547.
HOVERGEN	HBG050436.
InParanoid	Q8IZY2.
KO	K05645.
OMA	PGHVRIK.
OrthoDB	EOG4THVS5.
PhylomeDB	Q8IZY2.
Enzyme and pathway databases
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	Q8IZY2.
Bgee	Q8IZY2.
CleanEx	HS_ABCA7.
Genevestigator	Q8IZY2.
GermOnline	ENSG00000064687. Homo sapiens.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR026082. ABC_A. IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. [Graphical view]
PANTHER	PTHR19229. PTHR19229. 1 hit.
Pfam	PF00005. ABC_tran. 2 hits. [Graphical view]
SMART	SM00382. AAA. 2 hits. [Graphical view]
PROSITE	PS00211. ABC_TRANSPORTER_1. 1 hit. PS50893. ABC_TRANSPORTER_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ABCA7. human.
GenomeRNAi	10347.
NextBio	39239.
SOURCE	Search...

Entry information

Entry name

ABCA7_HUMAN

Accession

Primary (citable) accession number: Q8IZY2
Secondary accession number(s): Q96S58 , Q9BZC4, Q9NR73, Q9UKP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	December 4, 2007
Last modified:	May 1, 2013
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.