ABCA12

Protein identityUniProt · HPA

UniProt accession

Q86UK0

Gene

ABCA12

Ensembl

ENSG00000144452

Chromosome

2

Canonical length

2595 aa

Protein class

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

Subcellular location

Nucleoli,Vesicles,Plasma membrane,Cytosol

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, and White). This encoded protein is a member of the ABC1 subfamily, which is the only major ABC subfamily found exclusively in multicellular eukaryotes. Alternative splicing of this gene results in multiple transcript variants. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

2595 residues, UniProt reviewed canonical sequence.

>Q86UK0|ABCA12
     1  MASLFHQLQI LVWKNWLGVK RQPLWTLVLI LWPVIIFIIL AITRTKFPPT AKPTCYLAPR
    61  NLPSTGFFPF LQTLLCDTDS KCKDTPYGPQ DLLRRKGIDD ALFKDSEILR KSSNLDKDSS
   121  LSFQSTQVPE RRHASLATVF PSPSSDLEIP GTYTFNGSQV LARILGLEKL LKQNSTSEDI
   181  RRELCDSYSG YIVDDAFSWT FLGRNVFNKF CLSNMTLLES SLQELNKQFS QLSSDPNNQK
   241  IVFQEIVRML SFFSQVQEQK AVWQLLSSFP NVFQNDTSLS NLFDVLRKAN SVLLVVQKVY
   301  PRFATNEGFR TLQKSVKHLL YTLDSPAQGD SDNITHVWNE DDGQTLSPSS LAAQLLILEN
   361  FEDALLNISA NSPYIPYLAC VRNVTDSLAR GSPENLRLLQ STIRFKKSFL RNGSYEDYFP
   421  PVPEVLKSKL SQLRNLTELL CESETFSLIE KSCQLSDMSF GSLCEESEFD LQLLEAAELG
   481  TEIAASLLYH DNVISKKVRD LLTGDPSKIN LNMDQFLEQA LQMNYLENIT QLIPIIEAML
   541  HVNNSADASE KPGQLLEMFK NVEELKEDLR RTTGMSNRTI DKLLAIPIPD NRAEIISQVF
   601  WLHSCDTNIT TPKLEDAMKE FCNLSLSERS RQSYLIGLTL LHYLNIYNFT YKVFFPRKDQ
   661  KPVEKMMELF IRLKEILNQM ASGTHPLLDK MRSLKQMHLP RSVPLTQAMY RSNRMNTPQG
   721  SFSTISQALC SQGITTEYLT AMLPSSQRPK GNHTKDFLTY KLTKEQIASK YGIPINSTPF
   781  CFSLYKDIIN MPAGPVIWAF LKPMLLGRIL YAPYNPVTKA IMEKSNVTLR QLAELREKSQ
   841  EWMDKSPLFM NSFHLLNQAI PMLQNTLRNP FVQVFVKFSV GLDAVELLKQ IDELDILRLK
   901  LENNIDIIDQ LNTLSSLTVN ISSCVLYDRI QAAKTIDEME REAKRLYKSN ELFGSVIFKL
   961  PSNRSWHRGY DSGNVFLPPV IKYTIRMSLK TAQTTRSLRT KIWAPGPHNS PSHNQIYGRA
  1021  FIYLQDSIER AIIELQTGRN SQEIAVQVQA IPYPCFMKDN FLTSVSYSLP IVLMVAWVVF
  1081  IAAFVKKLVY EKDLRLHEYM KMMGVNSCSH FFAWLIESVG FLLVTIVILI IILKFGNILP
  1141  KTNGFILFLY FSDYSFSVIA MSYLISVFFN NTNIAALIGS LIYIIAFFPF IVLVTVENEL
  1201  SYVLKVFMSL LSPTAFSYAS QYIARYEEQG IGLQWENMYT SPVQDDTTSF GWLCCLILAD
  1261  SFIYFLIAWY VRNVFPGTYG MAAPWYFPIL PSYWKERFGC AEVKPEKSNG LMFTNIMMQN
  1321  TNPSASPEYM FSSNIEPEPK DLTVGVALHG VTKIYGSKVA VDNLNLNFYE GHITSLLGPN
  1381  GAGKTTTISM LTGLFGASAG TIFVYGKDIK TDLHTVRKNM GVCMQHDVLF SYLTTKEHLL
  1441  LYGSIKVPHW TKKQLHEEVK RTLKDTGLYS HRHKRVGTLS GGMKRKLSIS IALIGGSRVV
  1501  ILDEPSTGVD PCSRRSIWDV ISKNKTARTI ILSTHHLDEA EVLSDRIAFL EQGGLRCCGS
  1561  PFYLKEAFGD GYHLTLTKKK SPNLNANAVC DTMAVTAMIQ SHLPEAYLKE DIGGELVYVL
  1621  PPFSTKVSGA YLSLLRALDN GMGDLNIGCY GISDTTVEEV FLNLTKESQK NSAMSLEHLT
  1681  QKKIGNSNAN GISTPDDLSV SSSNFTDRDD KILTRGERLD GFGLLLKKIM AILIKRFHHT
  1741  RRNWKGLIAQ VILPIVFVTT AMGLGTLRNS SNSYPEIQIS PSLYGTSEQT AFYANYHPST
  1801  EALVSAMWDF PGIDNMCLNT SDLQCLNKDS LEKWNTSGEP ITNFGVCSCS ENVQECPKFN
  1861  YSPPHRRTYS SQVIYNLTGQ RVENYLISTA NEFVQKRYGG WSFGLPLTKD LRFDITGVPA
  1921  NRTLAKVWYD PEGYHSLPAY LNSLNNFLLR VNMSKYDAAR HGIIMYSHPY PGVQDQEQAT
  1981  ISSLIDILVA LSILMGYSVT TASFVTYVVR EHQTKAKQLQ HISGIGVTCY WVTNFIYDMV
  2041  FYLVPVAFSI GIIAIFKLPA FYSENNLGAV SLLLLLFGYA TFSWMYLLAG LFHETGMAFI
  2101  TYVCVNLFFG INSIVSLSVV YFLSKEKPND PTLELISETL KRIFLIFPQF CFGYGLIELS
  2161  QQQSVLDFLK AYGVEYPNET FEMNKLGAMF VALVSQGTMF FSLRLLINES LIKKLRLFFR
  2221  KFNSSHVRET IDEDEDVRAE RLRVESGAAE FDLVQLYCLT KTYQLIHKKI IAVNNISIGI
  2281  PAGECFGLLG VNGAGKTTIF KMLTGDIIPS SGNILIRNKT GSLGHVDSHS SLVGYCPQED
  2341  ALDDLVTVEE HLYFYARVHG IPEKDIKETV HKLLRRLHLM PFKDRATSMC SYGTKRKLST
  2401  ALALIGKPSI LLLDEPSSGM DPKSKRHLWK IISEEVQNKC SVILTSHSME ECEALCTRLA
  2461  IMVNGKFQCI GSLQHIKSRF GRGFTVKVHL KNNKVTMETL TKFMQLHFPK TYLKDQHLSM
  2521  LEYHVPVTAG GVANIFDLLE TNKTALNITN FLVSQTTLEE VFINFAKDQK SYETADTSSQ
  2581  GSTISVDSQD DQMES

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against ABCA12 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

20 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about ABCA12.

Disease | AllUniProt

Conditions ABCA12 is implicated in, by any mechanism.

• Ichthyosis, congenital, autosomal recessive 4A (ARCI4A) MIM:601277
• Ichthyosis, congenital, autosomal recessive 4B (ARCI4B) MIM:242500

Disease | GeneticClinVar

210 pathogenic / likely-pathogenic of 1,824 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Autosomal recessive congenital ichthyosis 4B
• Autosomal recessive congenital ichthyosis 4A
• Lamellar ichthyosis
• Ichthyosis
• ABCA12-related disorder

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)

0.48

gnomAD pLI

0

gnomAD missense Z

1.63

DepMap mean gene effect

0

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

• cellular homeostasis
• ceramide metabolic process
• ceramide transport
• cholesterol efflux
• corneocyte desquamation
• establishment of skin barrier
• intracellular protein transport
• keratinization
• lipid homeostasis
• lipid transport
• lung alveolus development
• phospholipid efflux
• positive regulation of cholesterol efflux
• positive regulation of protein localization to cell surface
• protein localization to plasma membrane
• regulated exocytosis
• regulation of insulin secretion involved in cellular response to glucose stimulus
• regulation of keratinocyte differentiation
• secretion by cell
• surfactant homeostasis
• positive regulation of intracellular lipid transport

Molecular functions

• ABC-type transporter activity
• apolipoprotein A-I receptor binding
• ATP binding
• ATP hydrolysis activity
• ATPase-coupled intramembrane lipid transporter activity
• ATPase-coupled lipid transmembrane transporter activity
• ATPase-coupled transmembrane transporter activity
• lipid transporter activity
• signaling receptor binding

Cellular components

• cytoplasm
• cytosol
• epidermal lamellar body
• Golgi membrane
• membrane
• plasma membrane
• transport vesicle membrane
• epidermal lamellar body 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
• Cytoplasmic vesicle
• Glycoprotein
• Golgi apparatus
• Ichthyosis
• Lipid transport
• Membrane
• Nucleotide-binding
• Repeat
• Translocase
• Transmembrane
• Transmembrane helix
• Transport

InteractionsUniProt · HPA

Protein binding partners of ABCA12 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• ABCA1
• NR1H2