ID ABCA6_MOUSE Reviewed; 1624 AA.
AC Q8K441; A2A6R3; Q8BGH0; Q8BPT1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 24-JAN-2024, entry version 145.
DE RecName: Full=ATP-binding cassette sub-family A member 6 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:Q8N139};
GN Name=Abca6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=12532264; DOI=10.1007/s00335-002-2229-9;
RA Annilo T., Chen Z.-Q., Shulenin S., Dean M.;
RT "Evolutionary analysis of a cluster of ATP-binding cassette (ABC) genes.";
RL Mamm. Genome 14:7-20(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Aorta, Cerebellum, Eye, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Probable transporter which may play a role in macrophage
CC lipid transport and homeostasis. {ECO:0000250|UniProtKB:Q8N139}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8N139}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8N139}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K441-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K441-2; Sequence=VSP_020699, VSP_020700;
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in heart,
CC lung, brain, spleen and testis. {ECO:0000269|PubMed:12532264}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis.
CC {ECO:0000269|PubMed:12532264}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
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DR EMBL; AF498361; AAM90907.1; -; mRNA.
DR EMBL; AK040652; BAC30657.1; -; mRNA.
DR EMBL; AK042934; BAC31409.1; -; mRNA.
DR EMBL; AK053384; BAC35372.1; -; mRNA.
DR EMBL; AL603792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132417; AAI32418.1; -; mRNA.
DR EMBL; BC132419; AAI32420.1; -; mRNA.
DR CCDS; CCDS25590.1; -. [Q8K441-1]
DR RefSeq; NP_001160028.1; NM_001166556.1. [Q8K441-2]
DR RefSeq; NP_001160029.1; NM_001166557.1.
DR RefSeq; NP_671751.2; NM_147218.2. [Q8K441-1]
DR RefSeq; XP_006534476.1; XM_006534413.1. [Q8K441-1]
DR RefSeq; XP_006534477.1; XM_006534414.2. [Q8K441-1]
DR AlphaFoldDB; Q8K441; -.
DR SMR; Q8K441; -.
DR BioGRID; 218010; 13.
DR STRING; 10090.ENSMUSP00000035458; -.
DR GlyCosmos; Q8K441; 3 sites, No reported glycans.
DR GlyGen; Q8K441; 3 sites.
DR iPTMnet; Q8K441; -.
DR PhosphoSitePlus; Q8K441; -.
DR SwissPalm; Q8K441; -.
DR CPTAC; non-CPTAC-3441; -.
DR jPOST; Q8K441; -.
DR MaxQB; Q8K441; -.
DR PaxDb; 10090-ENSMUSP00000035458; -.
DR PeptideAtlas; Q8K441; -.
DR ProteomicsDB; 285744; -. [Q8K441-1]
DR ProteomicsDB; 285745; -. [Q8K441-2]
DR Antibodypedia; 31832; 180 antibodies from 27 providers.
DR DNASU; 76184; -.
DR Ensembl; ENSMUST00000044003.14; ENSMUSP00000035458.8; ENSMUSG00000044749.14. [Q8K441-1]
DR GeneID; 76184; -.
DR KEGG; mmu:76184; -.
DR UCSC; uc007mdj.3; mouse. [Q8K441-1]
DR UCSC; uc007mdk.2; mouse. [Q8K441-2]
DR AGR; MGI:1923434; -.
DR CTD; 23460; -.
DR MGI; MGI:1923434; Abca6.
DR VEuPathDB; HostDB:ENSMUSG00000044749; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000162244; -.
DR HOGENOM; CLU_000604_19_1_1; -.
DR InParanoid; Q8K441; -.
DR OMA; ITSQIVF; -.
DR OrthoDB; 6951at2759; -.
DR PhylomeDB; Q8K441; -.
DR TreeFam; TF105192; -.
DR Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR BioGRID-ORCS; 76184; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Abca6; mouse.
DR PRO; PR:Q8K441; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K441; Protein.
DR Bgee; ENSMUSG00000044749; Expressed in lumbar dorsal root ganglion and 49 other cell types or tissues.
DR Genevisible; Q8K441; MM.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR CDD; cd03263; ABC_subfamily_A; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229:SF13; ATP-BINDING CASSETTE SUB-FAMILY A MEMBER 6; 1.
DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR Pfam; PF12698; ABC2_membrane_3; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Glycoprotein; Golgi apparatus; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1624
FT /note="ATP-binding cassette sub-family A member 6"
FT /id="PRO_0000250673"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..874
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 971..991
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1005..1025
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1058..1078
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1094..1114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1130..1150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1154..1174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1194..1214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 478..713
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1282..1520
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 514..521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1320..1327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 375..388
FT /note="IFQDYNLNGVVFPD -> NTEVITDASNGINP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020699"
FT VAR_SEQ 389..1624
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020700"
FT CONFLICT 331
FT /note="I -> V (in Ref. 3; BAC35372)"
FT /evidence="ECO:0000305"
FT CONFLICT 1020
FT /note="I -> T (in Ref. 1; AAM90907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1624 AA; 183283 MW; 90C077C465B5F79C CRC64;
MKELSVHVRQ QTRALLHKIL LKKWRRKRES LLEWSIPIII GLHMGLFSYL ARNIQVLEVP
PQDLGSLNEF NGSSLVVVYT PISNITQQIM NKTTFAPTMK GTRIIGVPSI EDLDEVLLHN
IPDALGVIFN DSFSYQLKVL RMYGNPFLKE DLLAHCWDTH SQAFCSLSKY WERGFVALQT
AINAGIIEVT TNHSVMEELM SIDGINMKTL PFIPRDLSDY EIFILFCLLY FSSFIYFASS
NVTKERKQCK EVMKVMGLQD SAFWLSWGLI YVGFIFIISI FIAIIITSTQ IIMMTGFLVI
FTLFFLYGLS LIAVTFLMAV LLQKAVLTNL IVLFFTLFWG CVGFTVLHKE LPPSLEWVLS
IFSPFAFTSG MAKVIFQDYN LNGVVFPDPS GESYVMIAVF FILAFDSLLY LVLALYFDKI
LLYGAEHRSA PLFFLNPTSC FRKTANRNKV IERDLDPELP SDEYFEPVDP EYQGKEAIRI
RNIKKEYKGK SGKVKALKGL FLDIYESQIT AILGHSGAGK SSLLNILSGL YVPTAGSVTV
YNKNLSDMQD LKEIRKAIGV CPQHNVQFDA LTVKENLTLF AKIKGILPQD VEQEVQQILS
ELDMQNIRDD LAEHLSEGQK RKLTFGIATV GDPQILLLDE PTVGLDPFSR QRIWGFLKER
RADHVILFST QFMDEADILA DRKVLIANGA LKCTGSSVFL KRKWGLGYHL SLFMDETCDS
ERLTSFINHH IPYAKLKAKT KEKLVYILPL ERTSEFPEFF SDLDKYSGQG LMSYEVSMST
LNDVFLNLEG EPSTKQDFEK RETATDSESL NDMEVAYPSL SQVQETVSTM SLWRMQVCAI
ARLRILKLKR ERKAFLIILL LLGIALLPLV IEYVANALLE VKNNWEFKTD LYFLSPGQLP
QGLRTSLLVI NNTESNIEDF LQSLKHQNIV LEVDDFENRN ATNSLSYNGA IIVSGRQKDY
RFSAVCNTKR LHCFPILMNV ISNGILHMLN HTQYIRIKED IFSPFIVLVW TGIQETCLFI
LCVICSLSPH IAMSSVSDYK KKADSQLWIS GLYPSAYWCG QAVVDISLFS GMLLTSYFTS
YTSKLLNIDM TSEIVFSVIV LALGCAASLV FLTYVISFVF GKRKKNSTLW SICFLLVIAI
TFEKVANGPF NEALVISATM LVPSFALNGL LVVLEMRAYQ YYIEFEEIKH GLSAVDLLLC
LIPYIHTLLF IFVLRCLELK YGKNVVRRDP IFRIAPQSLK AQPNPEEPID EDENVQAERL
RTSDALSTPN LDEKPVIIAS CLHKEYAGQK KHCCSRRTRN MAVRNVSFCV NKGEILGLLG
PDGAGKSSSI RMIAGITKPT AGQVELKRLS SAVGHQGDSR AEFGYCPQEN GLWPNLTVKE
HLELYAAVKG LRKEDAVVAI SRLVNALKLH DQLNVQVQNL VAGATRKLCF VLSILGNSPV
LILDEPSTGL DVSGKHQVWQ AIQAVVKDNE KGVLLSTHDL AEAEALCDRA AIMVSGRLRC
IGPIQHLKRK FGQDYVLELR VKDVSQEPLV HREILKLFPQ AARQDRCFSL LTYKLPVTDV
HPLSQAFHKL EAVKHGFDLE DYSLSQCTLD RVILELSKEQ ELGTVYEEAD MTLGRKLLPP
SDEL
//
