MCCC1

Protein identityUniProt · HPA

UniProt accession

Q96RQ3

Gene

MCCC1

Ensembl

ENSG00000078070

Chromosome

3

Canonical length

725 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins

Subcellular location

Mitochondria

OverviewNCBI Gene

This gene encodes the large subunit of 3-methylcrotonyl-CoA carboxylase. This enzyme functions as a heterodimer and catalyzes the carboxylation of 3-methylcrotonyl-CoA to form 3-methylglutaconyl-CoA. Mutations in this gene are associated with 3-Methylcrotonylglycinuria, an autosomal recessive disorder of leucine catabolism. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

725 residues, UniProt reviewed canonical sequence.

>Q96RQ3|MCCC1
     1  MAAASAVSVL LVAAERNRWH RLPSLLLPPR TWVWRQRTMK YTTATGRNIT KVLIANRGEI
    61  ACRVMRTAKK LGVQTVAVYS EADRNSMHVD MADEAYSIGP APSQQSYLSM EKIIQVAKTS
   121  AAQAIHPGCG FLSENMEFAE LCKQEGIIFI GPPPSAIRDM GIKSTSKSIM AAAGVPVVEG
   181  YHGEDQSDQC LKEHARRIGY PVMIKAVRGG GGKGMRIVRS EQEFQEQLES ARREAKKSFN
   241  DDAMLIEKFV DTPRHVEVQV FGDHHGNAVY LFERDCSVQR RHQKIIEEAP APGIKSEVRK
   301  KLGEAAVRAA KAVNYVGAGT VEFIMDSKHN FCFMEMNTRL QVEHPVTEMI TGTDLVEWQL
   361  RIAAGEKIPL SQEEITLQGH AFEARIYAED PSNNFMPVAG PLVHLSTPRA DPSTRIETGV
   421  RQGDEVSVHY DPMIAKLVVW AADRQAALTK LRYSLRQYNI VGLHTNIDFL LNLSGHPEFE
   481  AGNVHTDFIP QHHKQLLLSR KAAAKESLCQ AALGLILKEK AMTDTFTLQA HDQFSPFSSS
   541  SGRRLNISYT RNMTLKDGKN NVAIAVTYNH DGSYSMQIED KTFQVLGNLY SEGDCTYLKC
   601  SVNGVASKAK LIILENTIYL FSKEGSIEID IPVPKYLSSV SSQETQGGPL APMTGTIEKV
   661  FVKAGDKVKA GDSLMVMIAM KMEHTIKSPK DGTVKKVFYR EGAQANRHTP LVEFEEEESD
   721  KRESE

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against MCCC1 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

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.28

Highest tissue expression

55 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about MCCC1.

Disease | AllUniProt

Conditions MCCC1 is implicated in, by any mechanism.

• 3-methylcrotonoyl-CoA carboxylase 1 deficiency (MCC1D) MIM:210200

Disease | GeneticClinVar

204 pathogenic / likely-pathogenic of 999 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• 3-methylcrotonyl-CoA carboxylase 1 deficiency
• Methylcrotonyl-CoA carboxylase deficiency
• MCCC1-related disorder
• Inborn genetic diseases
• Cervical cancer

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)

0.9

gnomAD pLI

0

gnomAD missense Z

0.54

DepMap mean gene effect

-0.03

DepMap dependency class

none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 12% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• biotin metabolic process
• branched-chain amino acid catabolic process
• L-leucine catabolic process

Molecular functions

• ATP binding
• biotin binding
• metal ion binding
• methylcrotonoyl-CoA carboxylase activity
• biotin carboxylase activity

Cellular components

• cytosol
• methylcrotonoyl-CoA carboxylase complex
• mitochondrial matrix
• mitochondrion

Protein domainsUniProt · Pfam · InterPro

• Biotin/lipoyl attachment
• Biotin-binding site
• Carbamoyl phosphate synthase, ATP-binding domain
• Biotin carboxylase-like, N-terminal domain
• Biotin carboxylase, C-terminal
• Single hybrid motif
• Rudiment single hybrid motif
• ATP-grasp fold
• Biotin carboxylation domain
• Pre-ATP-grasp domain superfamily
• Biotin-dependent Carboxylase Complex
• Biotin carboxylase, N-terminal domain
• Biotin-requiring enzyme
• Biotin carboxylase C-terminal domain
• Carbamoyl-phosphate synthase L chain, ATP binding domain

KeywordsUniProt

• Acetylation
• ATP-binding
• Biotin
• Ligase
• Mitochondrion
• Nucleotide-binding
• Transit peptide

InteractionsUniProt · HPA

Protein binding partners of MCCC1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• SIRT4
• MCCC2
• PCCB