ABCA9_MOUSE
ID ABCA9_MOUSE Reviewed; 1623 AA.
AC Q8K449; A2A6R5; Q8C114;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=ATP-binding cassette sub-family A member 9 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:Q8IUA7};
GN Name=Abca9;
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], AND TISSUE SPECIFICITY.
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 654-1623.
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [5]
RP INDUCTION.
RX PubMed=16445568; DOI=10.1111/j.1440-1681.2005.04301.x;
RA Wakaumi M., Ishibashi K., Ando H., Kasanuki H., Tsuruoka S.;
RT "Acute digoxin loading reduces ABCA8A mRNA expression in the mouse liver.";
RL Clin. Exp. Pharmacol. Physiol. 32:1034-1041(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and Spleen;
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 [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=29520568; DOI=10.1007/s12565-018-0435-0;
RA Tachikawa M., Toki H., Watanabe M., Tomi M., Hosoya K.I., Terasaki T.;
RT "Gene expression of A6-like subgroup of ATP-binding cassette transporters
RT in mouse brain parenchyma and microvessels.";
RL Anat. Sci. Int. 93:456-463(2018).
CC -!- FUNCTION: Transporter that may play a role in monocyte differentiation
CC and lipid transport and homeostasis. {ECO:0000250|UniProtKB:Q8IUA7}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and to lower extent in
CC kidney, brain and spleen (PubMed:12532264). Weakly expressed in
CC developing and adult brains (PubMed:29520568). Weakly expressed in the
CC cerebellar granular layer at P14 and P21 (PubMed:29520568).
CC {ECO:0000269|PubMed:12532264, ECO:0000269|PubMed:29520568}.
CC -!- DEVELOPMENTAL STAGE: Detected along the outer surface of the brain or
CC along the fissure of cerebellar lobules at 13 dpc to P21.
CC {ECO:0000269|PubMed:29520568}.
CC -!- INDUCTION: Down-regulated by digoxin. {ECO:0000269|PubMed:16445568}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
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DR EMBL; AF491299; AAM90894.1; -; mRNA.
DR EMBL; AL603792; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34378.1; -; Genomic_DNA.
DR EMBL; AK029256; BAC26358.1; -; mRNA.
DR CCDS; CCDS25589.1; -.
DR RefSeq; NP_671753.2; NM_147220.2.
DR RefSeq; XP_017169975.1; XM_017314486.1.
DR AlphaFoldDB; Q8K449; -.
DR SMR; Q8K449; -.
DR BioGRID; 229876; 2.
DR STRING; 10090.ENSMUSP00000036338; -.
DR GlyGen; Q8K449; 1 site.
DR iPTMnet; Q8K449; -.
DR PhosphoSitePlus; Q8K449; -.
DR jPOST; Q8K449; -.
DR MaxQB; Q8K449; -.
DR PaxDb; Q8K449; -.
DR PeptideAtlas; Q8K449; -.
DR PRIDE; Q8K449; -.
DR ProteomicsDB; 286041; -.
DR Antibodypedia; 31822; 180 antibodies from 31 providers.
DR DNASU; 217262; -.
DR Ensembl; ENSMUST00000044850; ENSMUSP00000036338; ENSMUSG00000041797.
DR GeneID; 217262; -.
DR KEGG; mmu:217262; -.
DR UCSC; uc007mdh.1; mouse.
DR CTD; 10350; -.
DR MGI; MGI:2386796; Abca9.
DR VEuPathDB; HostDB:ENSMUSG00000041797; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000162444; -.
DR HOGENOM; CLU_000604_19_1_1; -.
DR InParanoid; Q8K449; -.
DR OMA; YFEEHTS; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; Q8K449; -.
DR TreeFam; TF105192; -.
DR Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR BioGRID-ORCS; 217262; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Abca9; mouse.
DR PRO; PR:Q8K449; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K449; protein.
DR Bgee; ENSMUSG00000041797; Expressed in sciatic nerve and 190 other tissues.
DR Genevisible; Q8K449; MM.
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:0005739; C:mitochondrion; HDA: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: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 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; IPR030370; ABCA9.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR PANTHER; PTHR19229:SF120; PTHR19229:SF120; 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; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1623
FT /note="ATP-binding cassette sub-family A member 9"
FT /id="PRO_0000250681"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 863..883
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1025..1045
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1071..1091
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1107..1127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1135..1155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1163..1183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1199..1219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 481..716
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1287..1520
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 517..524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1325..1332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 57
FT /note="A -> T (in Ref. 1; AAM90894)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1623 AA; 183114 MW; 666E67039EDB2627 CRC64;
MRKRHLRLGQ QMWALLCKNW LRKFRMRRET LLEWLFSLLL ILFVYQLSSN LHQVHDAPEM
SVVDLGRVDN FNDSNYMMVF APESEATHEI MNKVASAPFM KGRTIVACPD EKSMNELDLN
YSIDAVRVIF KDTFSYHLKF SWGQRIPKTK EHKDHSAPCE PLNNKMICEN SAFWEKGFVA
FQAAINAGII EMITNHSVME ELMSVIGSNM KMPPFIAQGG VATDFFIFFC VISFSSLIYY
LSVNITQERQ YMTTLMAMMG LRESAFWLSW SLMYAGFILV VAVLMSLIVK SAQVVVLTGF
MVVFLLFLFY GLSLITLSFL MSVLIKKPFL TGLAIFILTV FWGSLGFTAL YKHLPAFVEW
TLCFLSPFAF TTGMAQLIHL DYDVNSNVNL NSPNNSYLIM ATLFMLVLDA LLYLVLALYF
DKITLSKYGH QRSPLFFLKS SYWFKRRGAS HVVLENEIDS DPSLNDSLEP VSPEFQGKEA
IRIKNLKKEY SGKHGKVEAL RGLGFDIYEG QITALLGHSG AGKTTLINTL SGLSPPTTGS
VTIYNQTVSE MDDSDAVLTI TGVCPQSNVQ FGFLTVRENL RLFAKIKGIL PHEVEQEVQQ
VLQDLEMENI QDILAQNLSG GQKRKLTLGI AILGDPQVLL LDEPTAGLDP LSRHRIWNLL
KERRAGRVIV FSTQFMDEAD ILADRKVFIS NGRLKCAGSS LFLKKKWGIG YHLSLHLNEA
CDPEGITSLV KKHISDARLT TQSEERLVYI LPLERTNKFP DLYRDLDRCS NQGIEDYGVS
MTTLNEVFLK LEGKSMADES DVGICGRLQS DGARDMESLV ELEQVLSLDS SGSSVSGMAL
WRQQLCAVAK VRFFKLKNER KSLMTVLLLF GISFVPQLLE HLVYKVYHKS YSWGLSPSMY
FLSPGQPPQD PLTHLLVINR TGSSIDNFVH ALRQQGIALD LDALGTRNGT EEALYNGAIT
VLGEEKALRF SVACNAKRLN CFPVLMDIIS NGLLGIFNSS ERIQTDRSTV FEEHMLYEYG
FMSNAFFWIP VAASLTPYIA MGSISDHKKK VLSQLWTSGL YPSAYWCGQA LVDIPIYFLI
LFLMQIMDSV FSSEEFISVM ESLLIQIPCS IGYASSLIFM TYVISFIFRN GRKNSGIWSF
FFLIVTIFFI IATDINEYGF LELLICTFLV PPFTLIGSLL IFSEVSYDSV DYLGTSESQL
VFLALLIPYL HFLLFFFILR CLERYLRKKS LRVDPVFRIS PRSCPAVPNP EEPGEEDEDV
QMERVRTTGA MATLQTDEKP VIIASCLRKE YIGRTKRCFS KMKKKIATRN ISFCVKKGEV
LGLLGHNGAG KSTTISMITG DTIPTAGQVF LKGSGGGAAL GFLGYCPQEN VLWPNLTVKE
HLELYAAVKG LKKKDAVVTI TRLVNALKLQ DHLKALVRTL SEGVKRKLCF VLSILGNPPV
VLLDEPSTGM DPEGQQQMWQ AIRATFTNTE RGALLTTHYM AEAEAVCDRV AIMVSGRLRC
IGSIQHLKSK FGKDYLLEMK VKTPSQVEPL NTEIMRLFPQ AARQERYSSL MVYKLPVEDV
RPLSEAFFKL ERLKENFDLE EYSLSQSTLE QVFLELSKEQ ELDDFGEEAN SSVKWKLLPQ
EEL
