P05165 (PCCA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Propionyl-CoA carboxylase alpha chain, mitochondrial
Short name=PCCase subunit alpha
EC=6.4.1.3

Alternative name(s):
Propanoyl-CoA:carbon dioxide ligase subunit alpha

Gene names

Name:

PCCA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	728 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA.
Cofactor	Biotin.
Pathway	Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3.
Subunit structure	Probably a dodecamer composed of six biotin-containing alpha subunits and six beta subunits.
Subcellular location	Mitochondrion matrix Ref.8.
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.16 Ref.17 Ref.18
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain.
Sequence caution	The sequence AAA60035.1 differs from that shown. Reason: Frameshift at positions 374, 378, 380 and 395. 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. The sequence CAA32763.1 differs from that shown. Reason: Frameshift at position 23.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Ligand	ATP-binding Biotin Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid beta-oxidation Traceable author statement. Source: Reactome short-chain fatty acid catabolic process Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW biotin binding Traceable author statement Ref.10. Source: ProtInc biotin carboxylase activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: InterPro propionyl-CoA carboxylase activity Traceable author statement Ref.10. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P05165-1)

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.

Isoform 2 (identifier: P05165-2)

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

Isoform 3 (identifier: P05165-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 52

52

Mitochondrion Ref.8

Chain

53 – 728

676

Propionyl-CoA carboxylase alpha chain, mitochondrial

PRO_0000002837

Regions

Domain

62 – 509

448

Biotin carboxylation

Domain

181 – 378

198

ATP-grasp

Domain

660 – 727

68

Biotinyl-binding

Sites

Active site

353

1

By similarity

Binding site

177

1

ATP By similarity

Binding site

261

1

ATP By similarity

Binding site

296

1

ATP By similarity

Amino acid modifications

Modified residue

694

1

N6-biotinyllysine By similarity

Natural variations

Alternative sequence

36 – 61

26

Missing in isoform 2.

VSP_039857

Alternative sequence

634 – 680

47

Missing in isoform 3.

VSP_044458

Natural variant

75

1

A → P in PA-1. Ref.18

VAR_009087

Natural variant

77

1

R → W in PA-1. Ref.15 Ref.17

VAR_009088

Natural variant

138

1

A → T in PA-1. Ref.15

VAR_009089

Natural variant

164

1

I → T in PA-1. Ref.15

VAR_009090

Natural variant

197

1

G → E in PA-1. Ref.17

VAR_023843

Natural variant

229

1

M → K in PA-1. Ref.18

VAR_009091

Natural variant

297

1

Q → R in PA-1. Ref.17

VAR_009092

Natural variant

368

1

D → G in PA-1. Ref.18

VAR_009093

Natural variant

373

1

M → K in PA-1; unstable protein. Ref.15

VAR_009094

Natural variant

379

1

G → V in PA-1. Ref.18

VAR_009095

Natural variant

398

1

C → R in PA-1. Ref.17

VAR_023844

Natural variant

399

1

R → Q in PA-1. Ref.17

VAR_009096

Natural variant

423

1

P → L in PA-1. Ref.17

VAR_009097

Natural variant

475

1

I → V.
Corresponds to variant rs35719359 [ dbSNP | Ensembl ].

VAR_009098

Natural variant

532

1

Missing in PA-1. Ref.16

VAR_023845

Natural variant

551

1

V → F. Ref.16

VAR_023846

Natural variant

559

1

W → L in PA-1. Ref.17

VAR_009099

Natural variant

631

1

G → R in PA-1. Ref.15

VAR_009100

Natural variant

668

1

G → R in PA-1. Ref.18

VAR_009101

Natural variant

712

1

Missing in PA-1. Ref.18

VAR_009102

Experimental info

Sequence conflict

61

1

K → E in BAG60571. Ref.2

Sequence conflict

93

1

H → Y in BAG59350. Ref.4

Sequence conflict

373

1

M → R in AAA60035. Ref.10

Sequence conflict

378 – 379

2

KG → RS in AAA60035. Ref.10

Sequence conflict

558

1

N → H in AAA60035. Ref.10

Sequence conflict

610

1

T → A in BAG59350. Ref.4

Sequence conflict

679

1

D → A in AAA36424. Ref.11

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

728

Helix Strand Turn

Details...

Beta strand

199 – 201

3

Helix

202 – 212

11

Beta strand

214 – 220

7

Turn

226 – 228

3

Beta strand

230 – 234

5

Helix

235 – 252

18

Beta strand

258 – 262

5

Beta strand

265 – 268

4

Beta strand

665 – 667

3

Beta strand

669 – 673

5

Beta strand

688 – 691

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 5, 2010. Version 4. Checksum: 065F64186A0B8CCC	FASTA	728	80,059
	10 20 30 40 50 60 MAGFWVGTAP LVAAGRRGRW PPQQLMLSAA LRTLKHVLYY SRQCLMVSRN LGSVGYDPNE 70 80 90 100 110 120 KTFDKILVAN RGEIACRVIR TCKKMGIKTV AIHSDVDASS VHVKMADEAV CVGPAPTSKS 130 140 150 160 170 180 YLNMDAIMEA IKKTRAQAVH PGYGFLSENK EFARCLAAED VVFIGPDTHA IQAMGDKIES 190 200 210 220 230 240 KLLAKKAEVN TIPGFDGVVK DAEEAVRIAR EIGYPVMIKA SAGGGGKGMR IAWDDEETRD 250 260 270 280 290 300 GFRLSSQEAA SSFGDDRLLI EKFIDNPRHI EIQVLGDKHG NALWLNEREC SIQRRNQKVV 310 320 330 340 350 360 EEAPSIFLDA ETRRAMGEQA VALARAVKYS SAGTVEFLVD SKKNFYFLEM NTRLQVEHPV 370 380 390 400 410 420 TECITGLDLV QEMIRVAKGY PLRHKQADIR INGWAVECRV YAEDPYKSFG LPSIGRLSQY 430 440 450 460 470 480 QEPLHLPGVR VDSGIQPGSD ISIYYDPMIS KLITYGSDRT EALKRMADAL DNYVIRGVTH 490 500 510 520 530 540 NIALLREVII NSRFVKGDIS TKFLSDVYPD GFKGHMLTKS EKNQLLAIAS SLFVAFQLRA 550 560 570 580 590 600 QHFQENSRMP VIKPDIANWE LSVKLHDKVH TVVASNNGSV FSVEVDGSKL NVTSTWNLAS 610 620 630 640 650 660 PLLSVSVDGT QRTVQCLSRE AGGNMSIQFL GTVYKVNILT RLAAELNKFM LEKVTEDTSS 670 680 690 700 710 720 VLRSPMPGVV VAVSVKPGDA VAEGQEICVI EAMKMQNSMT AGKTGTVKSV HCQAGDTVGE GDLLVELE
	Isoform 2 [UniParc]. Checksum: B75C63581796ED53	FASTA	702	77,048
	10 20 30 40 50 60 MAGFWVGTAP LVAAGRRGRW PPQQLMLSAA LRTLKTFDKI LVANRGEIAC RVIRTCKKMG 70 80 90 100 110 120 IKTVAIHSDV DASSVHVKMA DEAVCVGPAP TSKSYLNMDA IMEAIKKTRA QAVHPGYGFL 130 140 150 160 170 180 SENKEFARCL AAEDVVFIGP DTHAIQAMGD KIESKLLAKK AEVNTIPGFD GVVKDAEEAV 190 200 210 220 230 240 RIAREIGYPV MIKASAGGGG KGMRIAWDDE ETRDGFRLSS QEAASSFGDD RLLIEKFIDN 250 260 270 280 290 300 PRHIEIQVLG DKHGNALWLN ERECSIQRRN QKVVEEAPSI FLDAETRRAM GEQAVALARA 310 320 330 340 350 360 VKYSSAGTVE FLVDSKKNFY FLEMNTRLQV EHPVTECITG LDLVQEMIRV AKGYPLRHKQ 370 380 390 400 410 420 ADIRINGWAV ECRVYAEDPY KSFGLPSIGR LSQYQEPLHL PGVRVDSGIQ PGSDISIYYD 430 440 450 460 470 480 PMISKLITYG SDRTEALKRM ADALDNYVIR GVTHNIALLR EVIINSRFVK GDISTKFLSD 490 500 510 520 530 540 VYPDGFKGHM LTKSEKNQLL AIASSLFVAF QLRAQHFQEN SRMPVIKPDI ANWELSVKLH 550 560 570 580 590 600 DKVHTVVASN NGSVFSVEVD GSKLNVTSTW NLASPLLSVS VDGTQRTVQC LSREAGGNMS 610 620 630 640 650 660 IQFLGTVYKV NILTRLAAEL NKFMLEKVTE DTSSVLRSPM PGVVVAVSVK PGDAVAEGQE 670 680 690 700 ICVIEAMKMQ NSMTAGKTGT VKSVHCQAGD TVGEGDLLVE LE
	Isoform 3 [UniParc]. Checksum: CF5795BE08D8BD5B	FASTA	681	75,002
	10 20 30 40 50 60 MAGFWVGTAP LVAAGRRGRW PPQQLMLSAA LRTLKHVLYY SRQCLMVSRN LGSVGYDPNE 70 80 90 100 110 120 KTFDKILVAN RGEIACRVIR TCKKMGIKTV AIHSDVDASS VHVKMADEAV CVGPAPTSKS 130 140 150 160 170 180 YLNMDAIMEA IKKTRAQAVH PGYGFLSENK EFARCLAAED VVFIGPDTHA IQAMGDKIES 190 200 210 220 230 240 KLLAKKAEVN TIPGFDGVVK DAEEAVRIAR EIGYPVMIKA SAGGGGKGMR IAWDDEETRD 250 260 270 280 290 300 GFRLSSQEAA SSFGDDRLLI EKFIDNPRHI EIQVLGDKHG NALWLNEREC SIQRRNQKVV 310 320 330 340 350 360 EEAPSIFLDA ETRRAMGEQA VALARAVKYS SAGTVEFLVD SKKNFYFLEM NTRLQVEHPV 370 380 390 400 410 420 TECITGLDLV QEMIRVAKGY PLRHKQADIR INGWAVECRV YAEDPYKSFG LPSIGRLSQY 430 440 450 460 470 480 QEPLHLPGVR VDSGIQPGSD ISIYYDPMIS KLITYGSDRT EALKRMADAL DNYVIRGVTH 490 500 510 520 530 540 NIALLREVII NSRFVKGDIS TKFLSDVYPD GFKGHMLTKS EKNQLLAIAS SLFVAFQLRA 550 560 570 580 590 600 QHFQENSRMP VIKPDIANWE LSVKLHDKVH TVVASNNGSV FSVEVDGSKL NVTSTWNLAS 610 620 630 640 650 660 PLLSVSVDGT QRTVQCLSRE AGGNMSIQFL GTVVAEGQEI CVIEAMKMQN SMTAGKTGTV 670 680 KSVHCQAGDT VGEGDLLVEL E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"Mitochondrial targeting signals and mature peptides of 3-methylcrotonyl-CoA carboxylase." Stadler S.C., Polanetz R., Meier S., Mayerhofer P.U., Herrmann J.M., Anslinger K., Roscher A.A., Roschinger W., Holzinger A. Biochem. Biophys. Res. Commun. 334:939-946(2005) [PubMed] [Europe PMC] [Abstract] 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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]	"Overview of mutations in the PCCA and PCCB genes causing propionic acidemia." Ugarte M., Perez-Cerda C., Rodriguez-Pombo P., Desviat L.R., Perez B., Richard E., Muro S., Campeau E., Ohura T., Gravel R.A. Hum. Mutat. 14:275-282(1999) [PubMed] [Europe PMC] [Abstract] 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]	"Mutation spectrum of the PCCA and PCCB genes in Japanese patients with propionic acidemia." Yang X., Sakamoto O., Matsubara Y., Kure S., Suzuki Y., Aoki Y., Yamaguchi S., Takahashi Y., Nishikubo T., Kawaguchi C., Yoshioka A., Kimura T., Hayasaka K., Kohno Y., Iinuma K., Ohura T. Mol. Genet. Metab. 81:335-342(2004) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00552419.
IPI00744115.
IPI00895869.

PIR

A27883. S04613.

RefSeq

NP_000273.2. NM_000282.3.
NP_001121164.1. NM_001127692.2.
NP_001171475.1. NM_001178004.1.

UniGene

Hs.80741.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CQY	NMR	-	A	175-270	[»]
2JKU	X-ray	1.50	A	658-728	[»]

ProteinModelPortal

P05165.

SMR

P05165. Positions 63-728.

ModBase

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Protein-protein interaction databases

DIP

DIP-57493N.

IntAct

P05165. 4 interactions.

STRING

9606.ENSP00000365462.

PTM databases

PhosphoSite

P05165.

Polymorphism databases

DMDM

308153661.

Proteomic databases

PaxDb

P05165.

PRIDE

P05165.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000376279; ENSP00000365456; ENSG00000175198.
ENST00000376285; ENSP00000365462; ENSG00000175198.
ENST00000376286; ENSP00000365463; ENSG00000175198.

GeneID

5095.

KEGG

hsa:5095.

UCSC

uc001voo.3. human.
uc010aga.3. human.

Organism-specific databases

CTD

5095.

GeneCards

GC13P100741.

HGNC

HGNC:8653. PCCA.

HPA

HPA041716.
HPA047792.

MIM

232000. gene.
606054. phenotype.

neXtProt

NX_P05165.

Orphanet

35. Propionic acidemia.

PharmGKB

PA32992.

GenAtlas

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Phylogenomic databases

eggNOG

COG4770.

HOGENOM

HOG000008989.

HOVERGEN

HBG000555.

KO

K01965.

OMA

HERECSI.

OrthoDB

EOG4Q58NT.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

SABIO-RK

P05165.

UniPathway

UPA00945; UER00908.

Gene expression databases

ArrayExpress

P05165.

Bgee

P05165.

CleanEx

HS_PCCA.

Genevestigator

P05165.

GermOnline

ENSG00000175198. Homo sapiens.

Family and domain databases

Gene3D

3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.

InterPro

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]

Pfam

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]

SMART

SM00878. Biotin_carb_C. 1 hit.
[Graphical view]

SUPFAM

SSF51230. Hybrid_motif. 1 hit.
SSF52440. PreATP-grasp-like. 1 hit.
SSF51246. Rudmnt_hyb_motif. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

ChiTaRS

PCCA. human.

DrugBank

DB00121. Biotin.

EvolutionaryTrace

P05165.

GenomeRNAi

5095.

NextBio

19656.

SOURCE

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Entry information

Entry name

PCCA_HUMAN

Accession

Primary (citable) accession number: P05165
Secondary accession number(s): B4DKY8 , B4DPF9, C9JPQ8, Q15979, Q8WXQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	October 5, 2010
Last modified:	May 1, 2013
This is version 157 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.