ABCA2

Protein identityUniProt · HPA

UniProt accession

Q9BZC7

Gene

ABCA2

Ensembl

ENSG00000107331

Chromosome

9

Canonical length

2435 aa

Protein class

Disease related genes, Human disease related genes, Plasma proteins, Potential drug targets, Predicted intracellular proteins, Predicted membrane proteins, Transporters

Subcellular location

Vesicles

OverviewNCBI Gene

The membrane-associated protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intracellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the ABC1 subfamily. Members of the ABC1 subfamily comprise the only major ABC subfamily found exclusively in multicellular eukaryotes. This protein is highly expressed in brain tissue and may play a role in macrophage lipid metabolism and neural development. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

2435 residues, UniProt reviewed canonical sequence.

>Q9BZC7|ABCA2
     1  MGFLHQLQLL LWKNVTLKRR SPWVLAFEIF IPLVLFFILL GLRQKKPTIS VKEAFYTAAP
    61  LTSAGILPVM QSLCPDGQRD EFGFLQYANS TVTQLLERLD RVVEEGNLFD PARPSLGSEL
   121  EALRQHLEAL SAGPGTSGSH LDRSTVSSFS LDSVARNPQE LWRFLTQNLS LPNSTAQALL
   181  AARVDPPEVY HLLFGPSSAL DSQSGLHKGQ EPWSRLGGNP LFRMEELLLA PALLEQLTCT
   241  PGSGELGRIL TVPESQKGAL QGYRDAVCSG QAAARARRFS GLSAELRNQL DVAKVSQQLG
   301  LDAPNGSDSS PQAPPPRRLQ ALLGDLLDAQ KVLQDVDVLS ALALLLPQGA CTGRTPGPPA
   361  SGAGGAANGT GAGAVMGPNA TAEEGAPSAA ALATPDTLQG QCSAFVQLWA GLQPILCGNN
   421  RTIEPEALRR GNMSSLGFTS KEQRNLGLLV HLMTSNPKIL YAPAGSEVDR VILKANETFA
   481  FVGNVTHYAQ VWLNISAEIR SFLEQGRLQQ HLRWLQQYVA ELRLHPEALN LSLDELPPAL
   541  RQDNFSLPSG MALLQQLDTI DNAACGWIQF MSKVSVDIFK GFPDEESIVN YTLNQAYQDN
   601  VTVFASVIFQ TRKDGSLPPH VHYKIRQNSS FTEKTNEIRR AYWRPGPNTG GRFYFLYGFV
   661  WIQDMMERAI IDTFVGHDVV EPGSYVQMFP YPCYTRDDFL FVIEHMMPLC MVISWVYSVA
   721  MTIQHIVAEK EHRLKEVMKT MGLNNAVHWV AWFITGFVQL SISVTALTAI LKYGQVLMHS
   781  HVVIIWLFLA VYAVATIMFC FLVSVLYSKA KLASACGGII YFLSYVPYMY VAIREEVAHD
   841  KITAFEKCIA SLMSTTAFGL GSKYFALYEV AGVGIQWHTF SQSPVEGDDF NLLLAVTMLM
   901  VDAVVYGILT WYIEAVHPGM YGLPRPWYFP LQKSYWLGSG RTEAWEWSWP WARTPRLSVM
   961  EEDQACAMES RRFEETRGME EEPTHLPLVV CVDKLTKVYK DDKKLALNKL SLNLYENQVV
  1021  SFLGHNGAGK TTTMSILTGL FPPTSGSATI YGHDIRTEMD EIRKNLGMCP QHNVLFDRLT
  1081  VEEHLWFYSR LKSMAQEEIR REMDKMIEDL ELSNKRHSLV QTLSGGMKRK LSVAIAFVGG
  1141  SRAIILDEPT AGVDPYARRA IWDLILKYKP GRTILLSTHH MDEADLLGDR IAIISHGKLK
  1201  CCGSPLFLKG TYGDGYRLTL VKRPAEPGGP QEPGLASSPP GRAPLSSCSE LQVSQFIRKH
  1261  VASCLLVSDT STELSYILPS EAAKKGAFER LFQHLERSLD ALHLSSFGLM DTTLEEVFLK
  1321  VSEEDQSLEN SEADVKESRK DVLPGAEGPA SGEGHAGNLA RCSELTQSQA SLQSASSVGS
  1381  ARGDEGAGYT DVYGDYRPLF DNPQDPDNVS LQEVEAEALS RVGQGSRKLD GGWLKVRQFH
  1441  GLLVKRFHCA RRNSKALFSQ ILLPAFFVCV AMTVALSVPE IGDLPPLVLS PSQYHNYTQP
  1501  RGNFIPYANE ERREYRLRLS PDASPQQLVS TFRLPSGVGA TCVLKSPANG SLGPTLNLSS
  1561  GESRLLAARF FDSMCLESFT QGLPLSNFVP PPPSPAPSDS PASPDEDLQA WNVSLPPTAG
  1621  PEMWTSAPSL PRLVREPVRC TCSAQGTGFS CPSSVGGHPP QMRVVTGDIL TDITGHNVSE
  1681  YLLFTSDRFR LHRYGAITFG NVLKSIPASF GTRAPPMVRK IAVRRAAQVF YNNKGYHSMP
  1741  TYLNSLNNAI LRANLPKSKG NPAAYGITVT NHPMNKTSAS LSLDYLLQGT DVVIAIFIIV
  1801  AMSFVPASFV VFLVAEKSTK AKHLQFVSGC NPIIYWLANY VWDMLNYLVP ATCCVIILFV
  1861  FDLPAYTSPT NFPAVLSLFL LYGWSITPIM YPASFWFEVP SSAYVFLIVI NLFIGITATV
  1921  ATFLLQLFEH DKDLKVVNSY LKSCFLIFPN YNLGHGLMEM AYNEYINEYY AKIGQFDKMK
  1981  SPFEWDIVTR GLVAMAVEGV VGFLLTIMCQ YNFLRRPQRM PVSTKPVEDD VDVASERQRV
  2041  LRGDADNDMV KIENLTKVYK SRKIGRILAV DRLCLGVRPG ECFGLLGVNG AGKTSTFKML
  2101  TGDESTTGGE AFVNGHSVLK ELLQVQQSLG YCPQCDALFD ELTAREHLQL YTRLRGISWK
  2161  DEARVVKWAL EKLELTKYAD KPAGTYSGGN KRKLSTAIAL IGYPAFIFLD EPTTGMDPKA
  2221  RRFLWNLILD LIKTGRSVVL TSHSMEECEA LCTRLAIMVN GRLRCLGSIQ HLKNRFGDGY
  2281  MITVRTKSSQ SVKDVVRFFN RNFPEAMLKE RHHTKVQYQL KSEHISLAQV FSKMEQVSGV
  2341  LGIEDYSVSQ TTLDNVFVNF AKKQSDNLEQ QETEPPSALQ SPLGCLLSLL RPRSAPTELR
  2401  ALVADEPEDL DTEDEGLISF EEERAQLSFN TDTLC

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against ABCA2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Other membrane

Secreted

No

Transmembrane segments

14

Mean surface accessibility (rSASA)

0.31

Highest tissue expression

178 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about ABCA2.

Disease | AllUniProt

Conditions ABCA2 is implicated in, by any mechanism.

• Intellectual developmental disorder with poor growth and with or without seizures or ataxia (IDPOGSA) MIM:618808

Disease | GeneticClinVar

15 pathogenic / likely-pathogenic of 678 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Intellectual developmental disorder with poor growth and with or without seizures or ataxia
• Ataxia with Dysarthria

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.17

gnomAD pLI

1

gnomAD missense Z

4.91

DepMap mean gene effect

0.04

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• central nervous system myelin formation
• ceramide translocation
• cholesterol homeostasis
• ganglioside metabolic process
• glycosphingolipid metabolic process
• intracellular sphingolipid homeostasis
• lipid metabolic process
• lipid transport
• locomotory behavior
• negative regulation of cholesterol efflux
• negative regulation of receptor-mediated endocytosis involved in cholesterol transport
• negative regulation of steroid metabolic process
• positive regulation of amyloid precursor protein biosynthetic process
• positive regulation of amyloid precursor protein catabolic process
• positive regulation of amyloid-beta formation
• positive regulation of low-density lipoprotein particle receptor catabolic process
• regulation of intracellular cholesterol transport
• regulation of post-translational protein modification
• regulation of protein localization to cell surface
• regulation of steroid metabolic process
• response to cholesterol
• response to steroid hormone
• response to xenobiotic stimulus
• sphingomyelin metabolic process
• sphingosine biosynthetic process
• transmembrane transport
• transport across blood-brain barrier
• negative regulation of intracellular cholesterol transport
• negative regulation of phospholipid biosynthetic process
• negative regulation of sphingolipid biosynthetic process
• regulation of protein localization to cell periphery

Molecular functions

• ABC-type transporter activity
• ATP binding
• ATP hydrolysis activity
• ATPase-coupled transmembrane transporter activity
• ceramide floppase activity
• lipid transporter activity
• nucleotide binding
• endopeptidase regulator activity

Cellular components

• ATP-binding cassette (ABC) transporter complex
• cytoplasmic vesicle
• endosome
• endosome membrane
• lysosomal membrane
• lysosome
• membrane
• microtubule organizing center
• plasma membrane

Protein domainsUniProt · Pfam · InterPro

• ABC transporter-like, ATP-binding domain
• AAA+ ATPase domain
• ABC-2 type transporter, transmembrane domain
• ABC transporter-like, conserved site
• ABC transporter A
• P-loop containing nucleoside triphosphate hydrolase
• ABCA1-4-like, C-terminal R2 regulatory domain
• ABC transporter
• ABC-2 family transporter protein
• ABCA1-like, C-terminal R1 regulatory domain

KeywordsUniProt

• ATP-binding
• Endosome
• Epilepsy
• Glycoprotein
• Intellectual disability
• Lysosome
• Membrane
• Methylation
• Nucleotide-binding
• Phosphoprotein
• Repeat
• Translocase
• Transmembrane
• Transmembrane helix
• Transport