CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016815
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-binding cassette sub-family A member 5 
Protein Synonyms/Alias
  
Gene Name
 Abca5 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
1438KKLPAGIKRKLCFALacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 May play a role in the processing of autolysosomes (By similarity). 
Sequence Annotation
 DOMAIN 478 713 ABC transporter 1.
 DOMAIN 1290 1533 ABC transporter 2.
 NP_BIND 514 521 ATP 1 (Potential).
 NP_BIND 1333 1340 ATP 2 (Potential).
 CARBOHYD 86 86 N-linked (GlcNAc...) (Potential).
 CARBOHYD 190 190 N-linked (GlcNAc...) (Potential).
 CARBOHYD 458 458 N-linked (GlcNAc...) (Potential).
 CARBOHYD 919 919 N-linked (GlcNAc...) (Potential).
 CARBOHYD 996 996 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Endosome; Glycoprotein; Golgi apparatus; Lysosome; Membrane; Nucleotide-binding; Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1642 AA 
Protein Sequence
MATAIRDVGV WRQTRTLLLK NYLVKCRTKK SSVQEILFPL FFLFWLILIS MMHPNKKYEE 60
VSDIELSPMD KSILSNLILG YTPVTNTTSS VMQRVSTDHL PDVLVTEEYA SEKELLASSL 120
SKPSNFVGVV FKDVMSYELR FFPDMVPVSS VYMDSRAGCS KSCDAAQYWS SGFTALQASI 180
DAAIIQLKTN VSLWRELEST KAVIMGEAAV VEIDTFPRGV ILIYLVIAFS PFGYFLAIHI 240
VAEKEKRLKE FLKIMGLHDT AFWLSWVLLY TSLIFLMSLL MAVIATASSL FPQSSSIVIF 300
LLFFLYGLSS VFFALMLTPL FKKSKHVGVV EFFVTVVFGF VGLLIVLVES FPRSLVWLFS 360
PLCQCAFLIG IAQVMHLEDF NEGALFSSLT EGPYPLIITL TMLALDSVFY ALLAVYLDQV 420
IPGEFGLRRS SLYFLKPSYW SKNKRNYKEL SEGNINGNIS LNEIVEPVSS EFIGKEAIRI 480
SGIQKAYRKK NETVEALRNL SFDIYEGQIT ALLGHSGTGK STLMNILCGL CPPSDGFASI 540
YGHRVSEIDE MFEARKMIGI CPQSDMNFDV LTVEENLSIL ASVKGIPANN IIQEVQKVLL 600
DLDMQAIKDN QAKKLSGGQK RKLSLGIAVL GNPKILLLDE PTAGMDPCSR HIVWNLLKYR 660
KANRVTVFST HFMDEADILA DRKAVISQGM LKCVGSSIFL KSKWGIGYRL SMYIDRYCAT 720
ESLSSLVRQH IPAAALLQQN DQQIVYSLPF KDMDKFSGLF SALDIHSNLG VISYGVSMTT 780
LEDVFLKLEV EAEIDQADYS VFTQQPREEE TDSKSFDEME QSLLILSETK ASLVSTMSLW 840
KQQVSTIAKF HFLSLKRESK SVRSVLLLLL IFFAVQIFMF LVHHSFKNAV VPIKLVPDLY 900
FLKPGDKPHK YKTSLLLQNS TDSDINDLID FFTQQNIIVA MFNDSDYVSA APHSAALNVV 960
QSEKDYVFTA VFNSTMVYSL PVMMNIISNY YLYHLNVTDT IQIWSTPFIQ EITDIVFKVE 1020
LYFQAALLGI IVTAMPPYFA MENAENHKIK AYTQLKLSGL LPSAYWIGQA VVDIPLFFVV 1080
LTLMLGSLFA FHHGLYFYPV KFLAVVFCLI AYVPSVILFT YIASFTFKKI LNTKEFWSFI 1140
YSVTALACVA VTEITFFLGY GVTAVFHYTF CIAIPIYPLL GCLISFIKGS WKNIPKTENA 1200
YNPWDRLLVA VIMPYLQCVL WIFLLQHYEK KHGGRSIRKD PLFRALSQKA KHKKFPEPPI 1260
NEDEDEDVKA ERLKVKELMG CQCCEEKPAI MVYNLHKEYD DKKDFLHSRK TTKVATKYVS 1320
FCVKKGEILG LLGPNGAGKS TIINILVGDV EPTSGKIFLG DYGSHSNEDD ESTKCMGYCP 1380
QTNPLWPDIT LQEHFEIYGA VKGMSSGDMK EVISRITKAL DLKEHLQKTV KKLPAGIKRK 1440
LCFALSMLGN PQVTLLDEPS TGMDPRAKQH MWRAIRTAFK NKKRAALLTT HYMEEAEAVC 1500
DRVAIMVSGQ LRCIGTVQHL KSKFGKGYFL EIKLKDWIEN LEIDRLQREI QYIFPNASRQ 1560
ESFSSILAYK IPKEDVQSLS QSFAKLEEAK HTFAIEEYSF SQATLEQVFV ELTKEQEEED 1620
NSCGTLNSTL WWERRQEDRV VF 1642 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:RGD.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
 GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016887; F:ATPase activity; IEA:InterPro.
 GO:0006200; P:ATP catabolic process; IEA:GOC.
 GO:0033344; P:cholesterol efflux; IEA:Compara.
 GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Compara.
 GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IEA:Compara.
 GO:0015918; P:sterol transport; NAS:RGD. 
Interpro
 IPR003593; AAA+_ATPase.
 IPR026082; ABC_A.
 IPR003439; ABC_transporter-like.
 IPR017871; ABC_transporter_CS.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00005; ABC_tran 
SMART
 SM00382; AAA 
PROSITE
 PS00211; ABC_TRANSPORTER_1
 PS50893; ABC_TRANSPORTER_2 
PRINTS