ID A2AJ26_MOUSE Unreviewed; 2433 AA.
AC A2AJ26;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE SubName: Full=ATP-binding cassette, sub-family A (ABC1), member 2 {ECO:0000313|Ensembl:ENSMUSP00000099983.4};
GN Name=Abca2 {ECO:0000313|Ensembl:ENSMUSP00000099983.4,
GN ECO:0000313|MGI:MGI:99606};
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 {ECO:0000313|Ensembl:ENSMUSP00000099983.4, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:19144319}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [2] {ECO:0000313|Ensembl:ENSMUSP00000099983.4, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000099983.4,
RC ECO:0000313|Proteomes:UP000000589};
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 [3] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [4] {ECO:0000313|Ensembl:ENSMUSP00000099983.4}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000099983.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; NP_031405.2; NM_007379.2.
DR SMR; A2AJ26; -.
DR EPD; A2AJ26; -.
DR MaxQB; A2AJ26; -.
DR PeptideAtlas; A2AJ26; -.
DR ProteomicsDB; 341520; -.
DR Antibodypedia; 32309; 246 antibodies from 27 providers.
DR DNASU; 11305; -.
DR Ensembl; ENSMUST00000102919.4; ENSMUSP00000099983.4; ENSMUSG00000026944.19.
DR GeneID; 11305; -.
DR UCSC; uc008isc.1; mouse.
DR AGR; MGI:99606; -.
DR CTD; 20; -.
DR MGI; MGI:99606; Abca2.
DR VEuPathDB; HostDB:ENSMUSG00000026944; -.
DR GeneTree; ENSGT00940000158560; -.
DR HOGENOM; CLU_000604_19_0_1; -.
DR OMA; QYFDSMC; -.
DR OrthoDB; 6951at2759; -.
DR PhylomeDB; A2AJ26; -.
DR TreeFam; TF105191; -.
DR BioGRID-ORCS; 11305; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Abca2; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000026944; Expressed in superior frontal gyrus and 169 other cell types or tissues.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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:0099038; F:ceramide floppase activity; IEA:Ensembl.
DR GO; GO:0061135; F:endopeptidase regulator activity; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0090156; P:intracellular sphingolipid homeostasis; IEA:Ensembl.
DR GO; GO:0090370; P:negative regulation of cholesterol efflux; IEA:Ensembl.
DR GO; GO:0071072; P:negative regulation of phospholipid biosynthetic process; IEA:Ensembl.
DR GO; GO:1905601; P:negative regulation of receptor-mediated endocytosis involved in cholesterol transport; IEA:Ensembl.
DR GO; GO:0090155; P:negative regulation of sphingolipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0042986; P:positive regulation of amyloid precursor protein biosynthetic process; IEA:Ensembl.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IEA:Ensembl.
DR GO; GO:0032805; P:positive regulation of low-density lipoprotein particle receptor catabolic process; IEA:Ensembl.
DR GO; GO:1901873; P:regulation of post-translational protein modification; IEA:Ensembl.
DR GO; GO:0019218; P:regulation of steroid metabolic process; IEA:Ensembl.
DR GO; GO:0070723; P:response to cholesterol; IEA:Ensembl.
DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR GO; GO:0046512; P:sphingosine biosynthetic process; IEA:Ensembl.
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; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229:SF225; ATP-BINDING CASSETTE SUB-FAMILY A MEMBER 2; 1.
DR PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR Pfam; PF12698; ABC2_membrane_3; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proteomics identification {ECO:0007829|EPD:A2AJ26,
KW ECO:0007829|MaxQB:A2AJ26};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 705..727
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 748..770
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 782..804
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 811..832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 889..912
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1792..1814
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1848..1866
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1878..1897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1903..1925
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 989..1220
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 2050..2285
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 300..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1585..1608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1585..1599
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2433 AA; 270525 MW; D5E92BDFA06C0AF6 CRC64;
MGFLHQLQLL LWKNVTLKRR SPWVLAFEIF IPLVLFFILL GLRQKKPTIS VKEAFYTAAP
LTSAGILPVM QSLCPDGQRD EFGFLQYANS TVTQLLERLH RVVEEGNLFD PVRPSLGSEL
EALRQRLEAL SSGPGTWESH SARPAVSSFS LDSVARDQRE LWRFLMQNLS LPNSTAQALL
AARVDPSEVY RLLFGPLPDL DGKLGFLRKQ EPWSRLGSNP LLQMEELLLA PALLEQLTCA
PGSGELGRIL TMPEGHQVDL QGYRDAVCSG QATARAQRFS DLAAELRNQL DTAKIAQQLG
FDVPNGSDPQ PQAPSPQSLP ALLGDLLDAQ KLLQDVDVLS ALALLLPQGA CAGQASAPQA
SSLNGLANST GIGANSGSNT TVEEGTQSPV SPASPDTLQG QCSAFVQLWA GLQPILCGNN
RTIEPEALRR GNMSSLGFTS KEQRNLGLLV HLMTSNPKIL YAPVGSEADR VILKANETFA
FVGNVTHYAQ VWLNISTEIR SFLEQGRLQQ HLQWLQQYVA DLQLHPEAMN LSLEELPPAL
RQDFSLPNGT ALLQQLDTID NAACGWIQFM SKVSVDIFKG FPDEESIVNY TLNQAYQDNV
TVFASVIFQT RKDGSLPPHV HYKIRQNSSF TEKTNEIRRA YWRPGPNTGG RFYFLYGFVW
IQDMMERAII NTFVGHDVVE PGNYVQMFPY PCYTRDDFLF VIEHMMPLCM VISWVYSVAM
TIQHIVAEKE HRLKEVMKTM GLNNAVHWVA WFITGFVQLS ISVTALTAIL KYGQVLMHSH
VLIIWLFLAV YAVATIMFCF LVSVLYSKAK LASACGGIIY FLSYVPYMYV AIREEVAHDK
ITAFEKCIAS LMSTTAFGLG SKYFALYEVA GVGIQWHTFS QSPVEGDDFN LLLAVTMLMV
DTVVYGVLTW YIEAVHPGMY GLPRPWYFPL QKSYWLGSGR TEAWEWSWPW AHTPRLSVME
EDQACAMESR HFEETRGMEE EPTHLPLVVC VDKLTKVYKN DKKMALNKLS LNLYENQVVS
FLGHNGAGKT TTMSILTGLF PPTSGSATIY GHDIRTEMDE IRKNLGMCPQ HNVLFDRLTV
EEHLWFYSRL KSMAQEEIRK ETDKMIEDLE LSNKRHSLVQ TLSGGMKRKL SVAIAFVGGS
RAIILDEPTA GVDPYARRAI WDLILKYKPG RTILLSTHHM DEADLLGDRI AIISHGKLKC
CGSPLFLKGA YGDGYRLTLV KQPAEPGTSQ EPGLASSPSG CPRLSSCSEP QVSQFIRKHV
ASSLLVSDTS TELSYILPSE AVKKGAFERL FQQLEHSLDA LHLSSFGLMD TTLEEVFLKV
SEEDQSLENS EADVKESRKD VLPGAEGLTA VGGQAGNLAR CSELAQSQAS LQSASSVGSA
RGEEGTGYSD GYGDYRPLFD NLQDPDNVSL QEAEMEALAQ VGQGSRKLEG WWLKMRQFHG
LLVKRFHCAR RNSKALCSQI LLPAFFVCVA MTVALSVPEI GDLPPLVLSP SQYHNYTQPR
GNFIPYANEE RQEYRLRLSP DASPQQLVST FRLPSGVGAT CVLKSPANGS LGPMLNLSSG
ESRLLAARFF DSMCLESFTQ GLPLSNFVPP PPSPAPSDSP VSPDEDSLQA WNMSLPPTAG
PETWTSAPSL PRLVHEPVRC TCSAQGTGFS CPSSVGGHPP QMRVVTGDIL TDITGHNVSE
YLLFTSDRFR LHRYGAITFG NVQKSIPASF GARVPPMVRK IAVRRVAQVL YNNKGYHSMP
TYLNSLNNAI LRANLPKSKG NPAAYGITVT NHPMNKTSAS LSLDYLLQGT DVVIAIFIIV
AMSFVPASFV VFLVAEKSTK AKHLQFVSGC NPVIYWLANY VWDMLNYLVP ATCCVIILFV
FDLPAYTSPT NFPAVLSLFL LYGWSITPIM YPASFWFEVP SSAYVFLIVI NLFIGITATV
ATFLLQLFEH DKDLKVVNSY LKSCFLIFPN YNLGHGLMEM AYNEYINEYY AKIGQFDKMK
SPFEWDIVTR GLVAMTVEGF VGFFLTIMCQ YNFLRQPQRL PVSTKPVEDD VDVASERQRV
LRGDADNDMV KIENLTKVYK SRKIGRILAV DRLCLGVRPG ECFGLLGVNG AGKTSTFKML
TGDESTTGGE AFVNGHSVLK DLLQVQQSLG YCPQFDALFD ELTAREHLQL YTRLRGIPWK
DEAQVVKWAL EKLELTKYAD KPAGTYSGGN KRKLSTAIAL IGYPAFIFLD EPTTGMDPKA
RRFLWNLILD LIKTGRSVVL TSHSMEECEA LCTRLAIMVN GRLRCLGSIQ HLKNRFGDGY
MITVRTKSSQ NVKDVVRFFN RNFPEAMLKE RHHTKVQYQL KSEHISLAQV FSKMEQVVGV
LGIEDYSVSQ TTLDNVFVNF AKKQSDNVEQ QEAEPSSLPS PLGLLSLLRP RPAPTELRAL
VADEPEDLDT EDEGLISFEE ERAQLSFNTD TLC
//
