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P05165

- PCCA_HUMAN

UniProt

P05165 - PCCA_HUMAN

Protein

Propionyl-CoA carboxylase alpha chain, mitochondrial

Gene

PCCA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 4 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA.

    Cofactori

    Biotin.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei177 – 1771ATPBy similarity
    Binding sitei261 – 2611ATPBy similarity
    Binding sitei296 – 2961ATPBy similarity
    Active sitei353 – 3531By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. biotin binding Source: ProtInc
    3. biotin carboxylase activity Source: InterPro
    4. enzyme binding Source: UniProtKB
    5. metal ion binding Source: InterPro
    6. propionyl-CoA carboxylase activity Source: ProtInc

    GO - Biological processi

    1. biotin metabolic process Source: Reactome
    2. cellular lipid metabolic process Source: Reactome
    3. fatty acid beta-oxidation Source: Reactome
    4. short-chain fatty acid catabolic process Source: Reactome
    5. small molecule metabolic process Source: Reactome
    6. vitamin metabolic process Source: Reactome
    7. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Biotin, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000175198-MONOMER.
    RETL1328306-WGS:GSTH-2235-MONOMER.
    ReactomeiREACT_11153. Biotin transport and metabolism.
    REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
    REACT_993. Propionyl-CoA catabolism.
    SABIO-RKP05165.
    UniPathwayiUPA00945; UER00908.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Propionyl-CoA carboxylase alpha chain, mitochondrial (EC:6.4.1.3)
    Short name:
    PCCase subunit alpha
    Alternative name(s):
    Propanoyl-CoA:carbon dioxide ligase subunit alpha
    Gene namesi
    Name:PCCA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:8653. PCCA.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Propionic acidemia type I (PA-1) [MIM:606054]: Life-threatening disease characterized by episodic vomiting, lethargy and ketosis, neutropenia, periodic thrombocytopenia, hypogammaglobulinemia, developmental retardation, and intolerance to protein.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti75 – 751A → P in PA-1. 1 Publication
    VAR_009087
    Natural varianti77 – 771R → W in PA-1. 2 Publications
    VAR_009088
    Natural varianti138 – 1381A → T in PA-1. 1 Publication
    VAR_009089
    Natural varianti164 – 1641I → T in PA-1. 1 Publication
    VAR_009090
    Natural varianti197 – 1971G → E in PA-1. 1 Publication
    VAR_023843
    Natural varianti229 – 2291M → K in PA-1. 1 Publication
    VAR_009091
    Natural varianti297 – 2971Q → R in PA-1. 1 Publication
    VAR_009092
    Natural varianti368 – 3681D → G in PA-1. 1 Publication
    VAR_009093
    Natural varianti373 – 3731M → K in PA-1; unstable protein. 1 Publication
    VAR_009094
    Natural varianti379 – 3791G → V in PA-1. 1 Publication
    VAR_009095
    Natural varianti398 – 3981C → R in PA-1. 1 Publication
    VAR_023844
    Natural varianti399 – 3991R → Q in PA-1. 1 Publication
    VAR_009096
    Natural varianti423 – 4231P → L in PA-1. 1 Publication
    VAR_009097
    Natural varianti532 – 5321Missing in PA-1. 1 Publication
    VAR_023845
    Natural varianti559 – 5591W → L in PA-1. 1 Publication
    Corresponds to variant rs118169528 [ dbSNP | Ensembl ].
    VAR_009099
    Natural varianti631 – 6311G → R in PA-1. 1 Publication
    VAR_009100
    Natural varianti668 – 6681G → R in PA-1. 1 Publication
    VAR_009101
    Natural varianti712 – 7121Missing in PA-1. 1 Publication
    VAR_009102

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi606054. phenotype.
    Orphaneti35. Propionic acidemia.
    PharmGKBiPA32992.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5252Mitochondrion1 PublicationAdd
    BLAST
    Chaini53 – 728676Propionyl-CoA carboxylase alpha chain, mitochondrialPRO_0000002837Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei65 – 651N6-acetyllysine; alternateBy similarity
    Modified residuei65 – 651N6-succinyllysine; alternateBy similarity
    Modified residuei119 – 1191N6-succinyllysineBy similarity
    Modified residuei150 – 1501N6-acetyllysine; alternateBy similarity
    Modified residuei150 – 1501N6-succinyllysine; alternateBy similarity
    Modified residuei200 – 2001N6-acetyllysine; alternateBy similarity
    Modified residuei200 – 2001N6-succinyllysine; alternateBy similarity
    Modified residuei252 – 2521PhosphoserineBy similarity
    Modified residuei262 – 2621N6-succinyllysineBy similarity
    Modified residuei328 – 3281N6-acetyllysine; alternateBy similarity
    Modified residuei328 – 3281N6-succinyllysine; alternateBy similarity
    Modified residuei385 – 3851N6-succinyllysineBy similarity
    Modified residuei407 – 4071N6-succinyllysineBy similarity
    Modified residuei496 – 4961N6-acetyllysineBy similarity
    Modified residuei502 – 5021N6-succinyllysineBy similarity
    Modified residuei513 – 5131N6-succinyllysineBy similarity
    Modified residuei648 – 6481N6-succinyllysineBy similarity
    Modified residuei694 – 6941N6-biotinyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP05165.
    PaxDbiP05165.
    PRIDEiP05165.

    PTM databases

    PhosphoSiteiP05165.

    Expressioni

    Gene expression databases

    ArrayExpressiP05165.
    BgeeiP05165.
    CleanExiHS_PCCA.
    GenevestigatoriP05165.

    Organism-specific databases

    HPAiHPA041716.
    HPA047792.

    Interactioni

    Subunit structurei

    Probably a dodecamer composed of six biotin-containing alpha subunits and six beta subunits.

    Protein-protein interaction databases

    BioGridi111128. 5 interactions.
    DIPiDIP-57493N.
    IntActiP05165. 7 interactions.
    STRINGi9606.ENSP00000365462.

    Structurei

    Secondary structure

    1
    728
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi199 – 2013
    Helixi202 – 21211
    Beta strandi214 – 2207
    Turni226 – 2283
    Beta strandi230 – 2345
    Helixi235 – 25218
    Beta strandi258 – 2625
    Beta strandi265 – 2684
    Beta strandi665 – 6673
    Beta strandi669 – 6735
    Beta strandi688 – 6914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CQYNMR-A176-270[»]
    2JKUX-ray1.50A658-728[»]
    ProteinModelPortaliP05165.
    SMRiP05165. Positions 63-728.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05165.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini62 – 509448Biotin carboxylationAdd
    BLAST
    Domaini181 – 378198ATP-graspPROSITE-ProRule annotationAdd
    BLAST
    Domaini660 – 72768Biotinyl-bindingAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
    Contains 1 biotin carboxylation domain.Curated
    Contains 1 biotinyl-binding domain.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG4770.
    HOGENOMiHOG000008989.
    HOVERGENiHBG000555.
    KOiK01965.
    OMAiHTVVASN.
    OrthoDBiEOG7RZ5PH.
    PhylomeDBiP05165.
    TreeFamiTF354220.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    InterProiIPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view]
    SMARTiSM00878. Biotin_carb_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P05165-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAGFWVGTAP LVAAGRRGRW PPQQLMLSAA LRTLKHVLYY SRQCLMVSRN    50
    LGSVGYDPNE KTFDKILVAN RGEIACRVIR TCKKMGIKTV AIHSDVDASS 100
    VHVKMADEAV CVGPAPTSKS YLNMDAIMEA IKKTRAQAVH PGYGFLSENK 150
    EFARCLAAED VVFIGPDTHA IQAMGDKIES KLLAKKAEVN TIPGFDGVVK 200
    DAEEAVRIAR EIGYPVMIKA SAGGGGKGMR IAWDDEETRD GFRLSSQEAA 250
    SSFGDDRLLI EKFIDNPRHI EIQVLGDKHG NALWLNEREC SIQRRNQKVV 300
    EEAPSIFLDA ETRRAMGEQA VALARAVKYS SAGTVEFLVD SKKNFYFLEM 350
    NTRLQVEHPV TECITGLDLV QEMIRVAKGY PLRHKQADIR INGWAVECRV 400
    YAEDPYKSFG LPSIGRLSQY QEPLHLPGVR VDSGIQPGSD ISIYYDPMIS 450
    KLITYGSDRT EALKRMADAL DNYVIRGVTH NIALLREVII NSRFVKGDIS 500
    TKFLSDVYPD GFKGHMLTKS EKNQLLAIAS SLFVAFQLRA QHFQENSRMP 550
    VIKPDIANWE LSVKLHDKVH TVVASNNGSV FSVEVDGSKL NVTSTWNLAS 600
    PLLSVSVDGT QRTVQCLSRE AGGNMSIQFL GTVYKVNILT RLAAELNKFM 650
    LEKVTEDTSS VLRSPMPGVV VAVSVKPGDA VAEGQEICVI EAMKMQNSMT 700
    AGKTGTVKSV HCQAGDTVGE GDLLVELE 728
    Length:728
    Mass (Da):80,059
    Last modified:October 5, 2010 - v4
    Checksum:i065F64186A0B8CCC
    GO
    Isoform 2 (identifier: P05165-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         36-61: Missing.

    Show »
    Length:702
    Mass (Da):77,048
    Checksum:iB75C63581796ED53
    GO
    Isoform 3 (identifier: P05165-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         634-680: Missing.

    Show »
    Length:681
    Mass (Da):75,002
    Checksum:iCF5795BE08D8BD5B
    GO

    Sequence cautioni

    The sequence AAA60035.1 differs from that shown. Reason: Frameshift at positions 374, 378, 380 and 395.
    The sequence CAA32763.1 differs from that shown. Reason: Frameshift at position 23.
    The sequence AAH00140.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAK61392.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611K → E in BAG60571. (PubMed:14702039)Curated
    Sequence conflicti93 – 931H → Y in BAG59350. 1 PublicationCurated
    Sequence conflicti373 – 3731M → R in AAA60035. (PubMed:3460076)Curated
    Sequence conflicti378 – 3792KG → RS in AAA60035. (PubMed:3460076)Curated
    Sequence conflicti558 – 5581N → H in AAA60035. (PubMed:3460076)Curated
    Sequence conflicti610 – 6101T → A in BAG59350. 1 PublicationCurated
    Sequence conflicti679 – 6791D → A in AAA36424. (PubMed:3555348)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti75 – 751A → P in PA-1. 1 Publication
    VAR_009087
    Natural varianti77 – 771R → W in PA-1. 2 Publications
    VAR_009088
    Natural varianti138 – 1381A → T in PA-1. 1 Publication
    VAR_009089
    Natural varianti164 – 1641I → T in PA-1. 1 Publication
    VAR_009090
    Natural varianti197 – 1971G → E in PA-1. 1 Publication
    VAR_023843
    Natural varianti229 – 2291M → K in PA-1. 1 Publication
    VAR_009091
    Natural varianti297 – 2971Q → R in PA-1. 1 Publication
    VAR_009092
    Natural varianti368 – 3681D → G in PA-1. 1 Publication
    VAR_009093
    Natural varianti373 – 3731M → K in PA-1; unstable protein. 1 Publication
    VAR_009094
    Natural varianti379 – 3791G → V in PA-1. 1 Publication
    VAR_009095
    Natural varianti398 – 3981C → R in PA-1. 1 Publication
    VAR_023844
    Natural varianti399 – 3991R → Q in PA-1. 1 Publication
    VAR_009096
    Natural varianti423 – 4231P → L in PA-1. 1 Publication
    VAR_009097
    Natural varianti475 – 4751I → V.
    Corresponds to variant rs35719359 [ dbSNP | Ensembl ].
    VAR_009098
    Natural varianti532 – 5321Missing in PA-1. 1 Publication
    VAR_023845
    Natural varianti551 – 5511V → F.1 Publication
    Corresponds to variant rs61749895 [ dbSNP | Ensembl ].
    VAR_023846
    Natural varianti559 – 5591W → L in PA-1. 1 Publication
    Corresponds to variant rs118169528 [ dbSNP | Ensembl ].
    VAR_009099
    Natural varianti631 – 6311G → R in PA-1. 1 Publication
    VAR_009100
    Natural varianti668 – 6681G → R in PA-1. 1 Publication
    VAR_009101
    Natural varianti712 – 7121Missing in PA-1. 1 Publication
    VAR_009102

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei36 – 6126Missing in isoform 2. 1 PublicationVSP_039857Add
    BLAST
    Alternative sequencei634 – 68047Missing in isoform 3. 1 PublicationVSP_044458Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF385926 mRNA. Translation: AAL66189.1.
    AY035808
    , AY035786, AY035787, AY035788, AY035789, AY035790, AY035791, AY035792, AY035793, AY035794, AY035795, AY035796, AY035797, AY035798, AY035799, AY035800, AY035801, AY035802, AY035803, AY035804, AY035805, AY035806, AY035807 Genomic DNA. Translation: AAK61392.1. Different initiation.
    AK296771 mRNA. Translation: BAG59350.1.
    AK298318 mRNA. Translation: BAG60571.1.
    AL355338
    , AL136526, AL353697, AL356575 Genomic DNA. Translation: CAH70370.2.
    AL356575
    , AL136526, AL353697, AL355338 Genomic DNA. Translation: CAH72681.2.
    AL136526
    , AL353697, AL355338, AL356575 Genomic DNA. Translation: CAI39557.2.
    AL353697
    , AL136526, AL355338, AL356575 Genomic DNA. Translation: CAI40434.2.
    CH471085 Genomic DNA. Translation: EAX09034.1.
    BC000140 mRNA. Translation: AAH00140.1. Different initiation.
    X14608 mRNA. Translation: CAA32763.1. Frameshift.
    S55656 mRNA. Translation: AAB25345.1.
    M13572 mRNA. Translation: AAA60035.1. Frameshift.
    M26121 mRNA. Translation: AAA36424.1.
    CCDSiCCDS45065.1. [P05165-2]
    CCDS53878.1. [P05165-3]
    CCDS9496.2. [P05165-1]
    PIRiS04613. A27883.
    RefSeqiNP_000273.2. NM_000282.3. [P05165-1]
    NP_001121164.1. NM_001127692.2. [P05165-2]
    NP_001171475.1. NM_001178004.1. [P05165-3]
    UniGeneiHs.80741.

    Genome annotation databases

    EnsembliENST00000376279; ENSP00000365456; ENSG00000175198. [P05165-3]
    ENST00000376285; ENSP00000365462; ENSG00000175198. [P05165-1]
    ENST00000376286; ENSP00000365463; ENSG00000175198. [P05165-2]
    GeneIDi5095.
    KEGGihsa:5095.
    UCSCiuc001voo.3. human. [P05165-1]
    uc010aga.3. human. [P05165-2]
    uc010tiz.2. human. [P05165-3]

    Polymorphism databases

    DMDMi308153661.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF385926 mRNA. Translation: AAL66189.1 .
    AY035808
    , AY035786 , AY035787 , AY035788 , AY035789 , AY035790 , AY035791 , AY035792 , AY035793 , AY035794 , AY035795 , AY035796 , AY035797 , AY035798 , AY035799 , AY035800 , AY035801 , AY035802 , AY035803 , AY035804 , AY035805 , AY035806 , AY035807 Genomic DNA. Translation: AAK61392.1 . Different initiation.
    AK296771 mRNA. Translation: BAG59350.1 .
    AK298318 mRNA. Translation: BAG60571.1 .
    AL355338
    , AL136526 , AL353697 , AL356575 Genomic DNA. Translation: CAH70370.2 .
    AL356575
    , AL136526 , AL353697 , AL355338 Genomic DNA. Translation: CAH72681.2 .
    AL136526
    , AL353697 , AL355338 , AL356575 Genomic DNA. Translation: CAI39557.2 .
    AL353697
    , AL136526 , AL355338 , AL356575 Genomic DNA. Translation: CAI40434.2 .
    CH471085 Genomic DNA. Translation: EAX09034.1 .
    BC000140 mRNA. Translation: AAH00140.1 . Different initiation.
    X14608 mRNA. Translation: CAA32763.1 . Frameshift.
    S55656 mRNA. Translation: AAB25345.1 .
    M13572 mRNA. Translation: AAA60035.1 . Frameshift.
    M26121 mRNA. Translation: AAA36424.1 .
    CCDSi CCDS45065.1. [P05165-2 ]
    CCDS53878.1. [P05165-3 ]
    CCDS9496.2. [P05165-1 ]
    PIRi S04613. A27883.
    RefSeqi NP_000273.2. NM_000282.3. [P05165-1 ]
    NP_001121164.1. NM_001127692.2. [P05165-2 ]
    NP_001171475.1. NM_001178004.1. [P05165-3 ]
    UniGenei Hs.80741.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CQY NMR - A 176-270 [» ]
    2JKU X-ray 1.50 A 658-728 [» ]
    ProteinModelPortali P05165.
    SMRi P05165. Positions 63-728.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111128. 5 interactions.
    DIPi DIP-57493N.
    IntActi P05165. 7 interactions.
    STRINGi 9606.ENSP00000365462.

    Chemistry

    DrugBanki DB00121. Biotin.

    PTM databases

    PhosphoSitei P05165.

    Polymorphism databases

    DMDMi 308153661.

    Proteomic databases

    MaxQBi P05165.
    PaxDbi P05165.
    PRIDEi P05165.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376279 ; ENSP00000365456 ; ENSG00000175198 . [P05165-3 ]
    ENST00000376285 ; ENSP00000365462 ; ENSG00000175198 . [P05165-1 ]
    ENST00000376286 ; ENSP00000365463 ; ENSG00000175198 . [P05165-2 ]
    GeneIDi 5095.
    KEGGi hsa:5095.
    UCSCi uc001voo.3. human. [P05165-1 ]
    uc010aga.3. human. [P05165-2 ]
    uc010tiz.2. human. [P05165-3 ]

    Organism-specific databases

    CTDi 5095.
    GeneCardsi GC13P100741.
    GeneReviewsi PCCA.
    HGNCi HGNC:8653. PCCA.
    HPAi HPA041716.
    HPA047792.
    MIMi 232000. gene.
    606054. phenotype.
    neXtProti NX_P05165.
    Orphaneti 35. Propionic acidemia.
    PharmGKBi PA32992.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4770.
    HOGENOMi HOG000008989.
    HOVERGENi HBG000555.
    KOi K01965.
    OMAi HTVVASN.
    OrthoDBi EOG7RZ5PH.
    PhylomeDBi P05165.
    TreeFami TF354220.

    Enzyme and pathway databases

    UniPathwayi UPA00945 ; UER00908 .
    BioCyci MetaCyc:ENSG00000175198-MONOMER.
    RETL1328306-WGS:GSTH-2235-MONOMER.
    Reactomei REACT_11153. Biotin transport and metabolism.
    REACT_169312. Defective HLCS causes multiple carboxylase deficiency.
    REACT_993. Propionyl-CoA catabolism.
    SABIO-RK P05165.

    Miscellaneous databases

    ChiTaRSi PCCA. human.
    EvolutionaryTracei P05165.
    GenomeRNAii 5095.
    NextBioi 19656.
    PROi P05165.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05165.
    Bgeei P05165.
    CleanExi HS_PCCA.
    Genevestigatori P05165.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    InterProi IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view ]
    SMARTi SM00878. Biotin_carb_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the PCCA gene and distribution of mutations causing propionic acidemia."
      Campeau E., Desviat L.R., Leclerc D., Wu X., Perez B., Ugarte M., Gravel R.A.
      Mol. Genet. Metab. 74:238-247(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Tissue: Kidney and Tongue.
    3. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-728 (ISOFORM 1).
      Tissue: Placenta.
    6. "Human mitochondrial propionyl-CoA carboxylase: localization of the N-terminus of the pro- and mature alpha chains in the deduced primary sequence of a full-length cDNA."
      Lamhonwah A.-M., Mahuran D.J., Gravel R.A.
      Nucleic Acids Res. 17:4396-4396(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-728 (ISOFORM 1).
    7. Gravel R.A.
      Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    8. Cited for: PROTEIN SEQUENCE OF 53-58, SUBCELLULAR LOCATION.
      Tissue: Kidney.
    9. "Cloning of functional alpha propionyl CoA carboxylase and correction of enzyme deficiency in pccA fibroblasts."
      Stankovics J., Ledley F.D.
      Am. J. Hum. Genet. 52:144-151(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 364-392.
      Tissue: Liver.
    10. "Isolation of cDNA clones coding for the alpha and beta chains of human propionyl-CoA carboxylase: chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes."
      Lamhonwah A.-M., Barankiewicz T.J., Willard H.F., Mahuran D.J., Quan F., Gravel R.A.
      Proc. Natl. Acad. Sci. U.S.A. 83:4864-4868(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 369-561.
    11. "Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase."
      Lamhonwah A.-M., Quan F., Gravel R.A.
      Arch. Biochem. Biophys. 254:631-636(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 633-728.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Solution structure of B domain from human propionyl-CoA carboxylase alpha subunit."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 175-270.
    14. Cited for: REVIEW ON PA VARIANTS.
    15. "Genetic heterogeneity in propionic acidemia patients with alpha-subunit defects: identification of five novel mutations, one of them causing instability of the protein."
      Richard E., Desviat L.R., Perez B., Perez-Cerda C., Ugarte M.
      Biochim. Biophys. Acta 1453:351-358(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PA-1 TRP-77; THR-138; THR-164; LYS-373 AND ARG-631.
    16. "Propionic acidemia: identification of twenty-four novel mutations in Europe and North America."
      Perez B., Desviat L.R., Rodriguez-Pombo P., Clavero S., Navarrete R., Perez-Cerda C., Ugarte M.
      Mol. Genet. Metab. 78:59-67(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PHE-551, VARIANT PA-1 LEU-532 DEL.
    17. Cited for: VARIANTS PA-1 TRP-77; GLU-197; ARG-297; ARG-398; GLN-399; LEU-423 AND LEU-559.
    18. "Coding sequence mutations in the alpha subunit of propionyl-CoA carboxylase in patients with propionic acidemia."
      Campeau E., Dupuis L., Leon-Del-Rio A., Gravel R.
      Mol. Genet. Metab. 67:11-22(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PA-1 PRO-75; LYS-229; GLY-368; VAL-379; ARG-668 AND CYS-712 DEL.

    Entry informationi

    Entry nameiPCCA_HUMAN
    AccessioniPrimary (citable) accession number: P05165
    Secondary accession number(s): B4DKY8
    , B4DPF9, C9JPQ8, Q15979, Q8WXQ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 173 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3