ABCA5_RAT
ID ABCA5_RAT Reviewed; 1642 AA.
AC Q8CF82; Q80Z07;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cholesterol transporter ABCA5 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:Q8K448};
DE AltName: Full=ATP-binding cassette sub-family A member 5 {ECO:0000305};
GN Name=Abca5 {ECO:0000312|RGD:628661};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=Wistar;
RX PubMed=12504089; DOI=10.1016/s0006-291x(02)02827-9;
RA Petry F., Kotthaus A., Hirsch-Ernst K.I.;
RT "Cloning of human and rat ABCA5/Abca5 and detection of a human splice
RT variant.";
RL Biochem. Biophys. Res. Commun. 300:343-350(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=Wistar; TISSUE=Testis;
RX PubMed=16162093; DOI=10.1042/bj20050808;
RA Petry F., Ritz V., Meineke C., Middel P., Kietzmann T., Schmitz-Salue C.,
RA Hirsch-Ernst K.I.;
RT "Subcellular localization of rat Abca5, a rat ATP-binding-cassette
RT transporter expressed in Leydig cells, and characterization of its splice
RT variant apparently encoding a half-transporter.";
RL Biochem. J. 393:79-87(2006).
CC -!- FUNCTION: Cholesterol efflux transporter in macrophages that is
CC responsible for APOAI/high-density lipoproteins (HDL) formation at the
CC plasma membrane under high cholesterol levels and participates in
CC reverse cholesterol transport. May play a role in the processing of
CC autolysosomes. {ECO:0000250|UniProtKB:Q8K448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q8K448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000250|UniProtKB:Q8K448};
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16162093};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16162093}. Late
CC endosome membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Golgi apparatus membrane {ECO:0000269|PubMed:16162093};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16162093}. Cell
CC membrane {ECO:0000250|UniProtKB:Q8K448}. Note=Localized at cell
CC membrane under high cholesterol levels. {ECO:0000250|UniProtKB:Q8K448}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CF82-1; Sequence=Displayed;
CC Name=2; Synonyms=V20+16;
CC IsoId=Q8CF82-2; Sequence=VSP_020693, VSP_020694;
CC -!- TISSUE SPECIFICITY: Expressed in testis, epididymis, lung and brain.
CC {ECO:0000269|PubMed:12504089, ECO:0000269|PubMed:16162093}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
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DR EMBL; AJ426052; CAD19800.2; -; mRNA.
DR EMBL; AJ550165; CAD80052.1; -; mRNA.
DR RefSeq; NP_775429.1; NM_173307.1. [Q8CF82-1]
DR AlphaFoldDB; Q8CF82; -.
DR STRING; 10116.ENSRNOP00000005848; -.
DR CarbonylDB; Q8CF82; -.
DR GlyGen; Q8CF82; 5 sites.
DR iPTMnet; Q8CF82; -.
DR PhosphoSitePlus; Q8CF82; -.
DR PaxDb; Q8CF82; -.
DR PRIDE; Q8CF82; -.
DR Ensembl; ENSRNOT00000005848; ENSRNOP00000005848; ENSRNOG00000004378. [Q8CF82-1]
DR GeneID; 286970; -.
DR KEGG; rno:286970; -.
DR CTD; 23461; -.
DR RGD; 628661; Abca5.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000158172; -.
DR HOGENOM; CLU_000604_19_1_1; -.
DR InParanoid; Q8CF82; -.
DR PhylomeDB; Q8CF82; -.
DR TreeFam; TF105192; -.
DR Reactome; R-RNO-1369062; ABC transporters in lipid homeostasis.
DR PRO; PR:Q8CF82; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000004378; Expressed in lung and 16 other tissues.
DR ExpressionAtlas; Q8CF82; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0005886; C:plasma 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:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; ISO:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; ISO:RGD.
DR GO; GO:1903064; P:positive regulation of reverse cholesterol transport; ISS:UniProtKB.
DR GO; GO:0010874; P:regulation of cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0015918; P:sterol transport; NAS:RGD.
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; IPR030367; ABCA5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR PANTHER; PTHR19229:SF100; PTHR19229:SF100; 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 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell membrane; Endosome; Glycoprotein;
KW Golgi apparatus; Lipid transport; Lysosome; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1642
FT /note="Cholesterol transporter ABCA5"
FT /id="PRO_0000250671"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 967..987
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1021..1041
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1071..1091
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1102..1122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1139..1159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1164..1184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1207..1227
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 1290..1533
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 1333..1340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 919
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 922..925
FT /note="DSDI -> GESV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16162093"
FT /id="VSP_020693"
FT VAR_SEQ 926..1642
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16162093"
FT /id="VSP_020694"
SQ SEQUENCE 1642 AA; 185811 MW; 3592F1D90ABCB81F CRC64;
MATAIRDVGV WRQTRTLLLK NYLVKCRTKK SSVQEILFPL FFLFWLILIS MMHPNKKYEE
VSDIELSPMD KSILSNLILG YTPVTNTTSS VMQRVSTDHL PDVLVTEEYA SEKELLASSL
SKPSNFVGVV FKDVMSYELR FFPDMVPVSS VYMDSRAGCS KSCDAAQYWS SGFTALQASI
DAAIIQLKTN VSLWRELEST KAVIMGEAAV VEIDTFPRGV ILIYLVIAFS PFGYFLAIHI
VAEKEKRLKE FLKIMGLHDT AFWLSWVLLY TSLIFLMSLL MAVIATASSL FPQSSSIVIF
LLFFLYGLSS VFFALMLTPL FKKSKHVGVV EFFVTVVFGF VGLLIVLVES FPRSLVWLFS
PLCQCAFLIG IAQVMHLEDF NEGALFSSLT EGPYPLIITL TMLALDSVFY ALLAVYLDQV
IPGEFGLRRS SLYFLKPSYW SKNKRNYKEL SEGNINGNIS LNEIVEPVSS EFIGKEAIRI
SGIQKAYRKK NETVEALRNL SFDIYEGQIT ALLGHSGTGK STLMNILCGL CPPSDGFASI
YGHRVSEIDE MFEARKMIGI CPQSDMNFDV LTVEENLSIL ASVKGIPANN IIQEVQKVLL
DLDMQAIKDN QAKKLSGGQK RKLSLGIAVL GNPKILLLDE PTAGMDPCSR HIVWNLLKYR
KANRVTVFST HFMDEADILA DRKAVISQGM LKCVGSSIFL KSKWGIGYRL SMYIDRYCAT
ESLSSLVRQH IPAAALLQQN DQQIVYSLPF KDMDKFSGLF SALDIHSNLG VISYGVSMTT
LEDVFLKLEV EAEIDQADYS VFTQQPREEE TDSKSFDEME QSLLILSETK ASLVSTMSLW
KQQVSTIAKF HFLSLKRESK SVRSVLLLLL IFFAVQIFMF LVHHSFKNAV VPIKLVPDLY
FLKPGDKPHK YKTSLLLQNS TDSDINDLID FFTQQNIIVA MFNDSDYVSA APHSAALNVV
QSEKDYVFTA VFNSTMVYSL PVMMNIISNY YLYHLNVTDT IQIWSTPFIQ EITDIVFKVE
LYFQAALLGI IVTAMPPYFA MENAENHKIK AYTQLKLSGL LPSAYWIGQA VVDIPLFFVV
LTLMLGSLFA FHHGLYFYPV KFLAVVFCLI AYVPSVILFT YIASFTFKKI LNTKEFWSFI
YSVTALACVA VTEITFFLGY GVTAVFHYTF CIAIPIYPLL GCLISFIKGS WKNIPKTENA
YNPWDRLLVA VIMPYLQCVL WIFLLQHYEK KHGGRSIRKD PLFRALSQKA KHKKFPEPPI
NEDEDEDVKA ERLKVKELMG CQCCEEKPAI MVYNLHKEYD DKKDFLHSRK TTKVATKYVS
FCVKKGEILG LLGPNGAGKS TIINILVGDV EPTSGKIFLG DYGSHSNEDD ESTKCMGYCP
QTNPLWPDIT LQEHFEIYGA VKGMSSGDMK EVISRITKAL DLKEHLQKTV KKLPAGIKRK
LCFALSMLGN PQVTLLDEPS TGMDPRAKQH MWRAIRTAFK NKKRAALLTT HYMEEAEAVC
DRVAIMVSGQ LRCIGTVQHL KSKFGKGYFL EIKLKDWIEN LEIDRLQREI QYIFPNASRQ
ESFSSILAYK IPKEDVQSLS QSFAKLEEAK HTFAIEEYSF SQATLEQVFV ELTKEQEEED
NSCGTLNSTL WWERRQEDRV VF
