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Database: UniProt
Entry: Q6AXE3_MOUSE
LinkDB: Q6AXE3_MOUSE
Original site: Q6AXE3_MOUSE 
ID   Q6AXE3_MOUSE            Unreviewed;      1449 AA.
AC   Q6AXE3;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   SubName: Full=ATP-binding cassette, sub-family A (ABC1), member 3 {ECO:0000313|Ensembl:ENSMUSP00000113538.2};
DE   SubName: Full=Abca3 protein {ECO:0000313|EMBL:AAH79617.1};
GN   Name=Abca3 {ECO:0000313|EMBL:AAH79617.1,
GN   ECO:0000313|Ensembl:ENSMUSP00000113538.2,
GN   ECO:0000313|MGI:MGI:1351617};
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|EMBL:AAH79617.1};
RN   [1] {ECO:0000313|EMBL:AAH79617.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6 {ECO:0000313|EMBL:AAH79617.1};
RC   TISSUE=Brain {ECO:0000313|EMBL:AAH79617.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   [2] {ECO:0000313|Ensembl:ENSMUSP00000113538.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000113538.2,
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:ENSMUSP00000113538.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000113538.2};
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   EMBL; BC079617; AAH79617.1; -; mRNA.
DR   RefSeq; NP_001034670.1; NM_001039581.2.
DR   RefSeq; NP_038883.2; NM_013855.3.
DR   ProteomicsDB; 331040; -.
DR   Antibodypedia; 1409; 99 antibodies from 19 providers.
DR   DNASU; 27410; -.
DR   Ensembl; ENSMUST00000117337.2; ENSMUSP00000113538.2; ENSMUSG00000024130.17.
DR   GeneID; 27410; -.
DR   KEGG; mmu:27410; -.
DR   UCSC; uc012amg.2; mouse.
DR   AGR; MGI:1351617; -.
DR   CTD; 21; -.
DR   MGI; MGI:1351617; Abca3.
DR   VEuPathDB; HostDB:ENSMUSG00000024130; -.
DR   GeneTree; ENSGT00940000155289; -.
DR   HOGENOM; CLU_000604_19_1_1; -.
DR   OrthoDB; 6951at2759; -.
DR   BioGRID-ORCS; 27410; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Abca3; mouse.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Bgee; ENSMUSG00000024130; Expressed in left lung lobe and 255 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   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; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR   PANTHER; PTHR19229:SF98; PHOSPHOLIPID-TRANSPORTING ATPASE ABCA3; 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:Q6AXE3,
KW   ECO:0007829|MaxQB:Q6AXE3};
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        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        303..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        345..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        371..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        845..866
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        886..914
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        926..948
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        960..980
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          530..763
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          1126..1359
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   1449 AA;  163479 MW;  25094B962B056FFB CRC64;
     MAVLRQLTLL LWKNYTLKKR KVLVTVLELF LPLLFSGILI WLRLKIQSEN VPNATVYPDQ
     SIQELPLFFS FPPPGGTWEL AYVPSHSDAA RTITETVKRE FMIKMRVHGF SSEKDFEDYI
     RYDNHSSSVL AAVVFEHSFN HSQDPLPLAV KYHLRFSYTR RNYMWTQTGN IFLKETEGWH
     TTSLFPLFPS PGPREPSSPD GGEPGYIREG FLAMQHAVDK AIMRYHANTS AQQLFQKLMV
     ITKRFPFPPY ISDPFLIAIQ YQLPLLLMLS FTYTSLTIIR AVVQEKEKKL KEYMRMMGLN
     SWLHWSAWFL MFFLFFLIVV SFMTLLFCVK VKKDIAVLSN SDPSLVLAFL LCFAISSISF
     SFMVSTFFSK ANIAAAVGGF LYFFTYTPYF FVAPRYNWMT LSQKLLSCLL SNVAMAMGAQ
     LIGKFEAKGT GIQWRDLLNP VNVDDNFCFG QVLGMLLLDS ALYGLVTWYV EAVFPGQFGV
     PQPWHFFLMP SYWCGNPRTV VGKEEEGSDP EKALRNEYFE AEPEDLVAGI KIKHLSKVFQ
     VGNKDKMGIR DLTLNLYEGQ ITVLLGHNGA GKTTTMSLLT GLFPPTSGHA YIHGYEISQD
     MAQIRKSLGL CPQHDVLFDN LTVAEHLYFY AQLKGLSLQK CPEEVKQMLH ILSLEDKRDL
     RSKFLSGGMK RKLSIGIALI AGSKVLMLDE PTSGMDAVSR RAIWDLLQQQ KSDRTVLLTT
     HFMDEADLLG DRIAILAKGE LQCCGSSLFL KQKYGAGYHM TLVKEPHCNP EGISQLVHHH
     VPNAMLESHA GAELSFILPK ESTHRFESLF AKLEKKQKEL GIASFGASVT TMEEVFLRGR
     KGFDIALNLL IAMAFLASTF SILAVSERAV QAKHVQFVSG VHVATFWFSA LLWDLISFLV
     PSLLLLVVFQ AFNVHAFTRD GHMADLLLLL MLYGWAIIPL MYLMSFFFSA ASTAYTRLTI
     FNILSGIATF IMVTIMRIPA VKLEELSRTL DHVFLVLPNH CLGMAVSNFY ENYETRRYCT
     SSELAAHYCK KYNIQYQESF YAWSTPGVGK FVTSMAASGG IYLTLLFLIE TNLLWRLRTF
     ICAFRRRWTL AELQNRTSVL PEDQDVAEER SRILVPSLDS MLDTPLIINE LSKVYDQRAP
     LLAVDRISLA VQKGECFGLL GFNGAGKTTT FKMLTGEETI TSGDAFVGGY SISSDIGKVR
     QRMGYCPQFD ALLDHMTGRE MLVMYARLRG IPERLINACV ENTLRGLLLE PHANKLVKTY
     SGGNKRKLST GIALIGEPAV IFLDEPSTGM DPVARRLLWD TVARARESGK AIVITSHSME
     ECEALCTRLA IMVQGQFKCL GSPQHLKSKF GSGYSLQAKV RSEGKQDALE EFKAFVDLTF
     PGSILEDEHQ DMVHYHLPGC DLSWAKVFGI LEKAKEKYGV DDYSVSQISL EQVFLSFAHL
     QPPTTEDGR
//
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