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P07451 (CAH3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbonic anhydrase 3

EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase III
Carbonic anhydrase III
Short name=CA-III
Gene names
Name:CA3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc.

Enzyme regulation

Activated by proton donors such as imidazole and the dipeptide histidylhistidine. Inhibited by coumarins and sulfonamide derivatives such as acetazolamide. Ref.8 Ref.9 Ref.10

Subcellular location

Cytoplasm.

Tissue specificity

Muscle specific.

Developmental stage

At 6 weeks gestation, transcripts accumulate at low levels in the somites and at high levels throughout the notochord. As gestation continues, CA3 becomes abundant in all developing muscle masses and continues at high to moderate levels in the notochord. Ref.7

Post-translational modification

S-glutathionylated in hepatocytes under oxidative stress By similarity.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Biophysicochemical properties

Kinetic parameters:

KM=52.0 mM for CO2 Ref.10

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 260259Carbonic anhydrase 3
PRO_0000077426

Regions

Region64 – 674Involved in proton transfer
Region198 – 1992Substrate binding By similarity

Sites

Active site1271 By similarity
Metal binding941Zinc; catalytic
Metal binding961Zinc; catalytic
Metal binding1191Zinc; catalytic

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1821S-glutathionyl cysteine By similarity
Modified residue1871S-glutathionyl cysteine By similarity

Natural variations

Natural variant311V → I. Ref.3 Ref.4 Ref.5
Corresponds to variant rs20571 [ dbSNP | Ensembl ].
VAR_016180

Experimental info

Mutagenesis641K → H: Enhanced proton transfer in catalysis. Ref.12
Mutagenesis671R → H: Enhanced proton transfer in catalysis. Ref.12
Mutagenesis1971F → L: Enhanced activity by at least 10-fold. Ref.11

Secondary structure

....................................................... 260
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07451 [UniParc].

Last modified March 20, 2007. Version 3.
Checksum: A305334167233FCF

FASTA26029,557
        10         20         30         40         50         60 
MAKEWGYASH NGPDHWHELF PNAKGENQSP VELHTKDIRH DPSLQPWSVS YDGGSAKTIL 

        70         80         90        100        110        120 
NNGKTCRVVF DDTYDRSMLR GGPLPGPYRL RQFHLHWGSS DDHGSEHTVD GVKYAAELHL 

       130        140        150        160        170        180 
VHWNPKYNTF KEALKQRDGI AVIGIFLKIG HENGEFQIFL DALDKIKTKG KEAPFTKFDP 

       190        200        210        220        230        240 
SCLFPACRDY WTYQGSFTTP PCEECIVWLL LKEPMTVSSD QMAKLRSLLS SAENEPPVPL 

       250        260 
VSNWRPPQPI NNRVVRASFK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and derived amino acid sequence of a cDNA encoding human muscle carbonic anhydrase."
Lloyd J., McMillan S., Hopkinson D., Edwards Y.H.
Gene 41:233-239(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence, tissue-specific expression, and chromosome location of human carbonic anhydrase III: the human CAIII gene is located on the same chromosome as the closely linked CAI and CAII genes."
Wade R., Gunning P., Eddy R., Shows T., Kedes L.
Proc. Natl. Acad. Sci. U.S.A. 83:9571-9575(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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. expand/collapse author list , 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], VARIANT ILE-31.
Tissue: Pericardium and Skeletal muscle.
[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. expand/collapse author list , 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], VARIANT ILE-31.
[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], VARIANT ILE-31.
Tissue: Muscle.
[6]"Human muscle carbonic anhydrase: gene structure and DNA methylation patterns in fetal and adult tissues."
Lloyd J., Brownson C., Tweedie S., Charlton J., Edwards Y.H.
Genes Dev. 1:594-602(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Sequence comparisons and functional studies of the proximal promoter of the carbonic anhydrase 3 (CA3) gene."
Sowden J., Smith H., Morrison K., Edwards Y.
Gene 214:157-165(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11, DEVELOPMENTAL STAGE.
[8]"A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases."
Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T.
Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[9]"Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors."
Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T.
J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[10]"Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide."
Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., Pedone C., Scozzafava A., Supuran C.T., De Simone G.
Proteins 74:164-175(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[11]"Human carbonic anhydrase III: structural and kinetic study of catalysis and proton transfer."
Duda D.M., Tu C., Fisher S.Z., An H., Yoshioka C., Govindasamy L., Laipis P.J., Agbandje-McKenna M., Silverman D.N., McKenna R.
Biochemistry 44:10046-10053(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-260 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF PHE-197, ACTIVATION BY IMIDAZOLE AND HISTIDYLHISTIDINE.
[12]"Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III."
Elder I., Fisher Z., Laipis P.J., Tu C., McKenna R., Silverman D.N.
Proteins 68:337-343(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-260 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF LYS-64 AND ARG-67.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29458 Genomic DNA. Translation: AAA52293.1.
M29452 Genomic DNA. No translation available.
AK096880 mRNA. Translation: BAG53390.1.
AK313254 mRNA. Translation: BAG36064.1.
CH471068 Genomic DNA. Translation: EAW87133.1.
BC004897 mRNA. Translation: AAH04897.1.
AJ006473 Genomic DNA. Translation: CAA07056.1.
CCDSCCDS6238.1.
PIRCRHU3. A26658.
RefSeqNP_005172.1. NM_005181.3.
UniGeneHs.82129.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z93X-ray2.10A1-260[»]
1Z97X-ray2.10A1-260[»]
2HFWX-ray2.50A1-259[»]
3UYNX-ray2.60A1-260[»]
3UYQX-ray1.70A1-260[»]
ProteinModelPortalP07451.
SMRP07451. Positions 2-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107216. 1 interaction.
STRING9606.ENSP00000285381.

Chemistry

BindingDBP07451.
ChEMBLCHEMBL2885.

PTM databases

PhosphoSiteP07451.

Polymorphism databases

DMDM134047703.

2D gel databases

UCD-2DPAGEP07451.

Proteomic databases

PaxDbP07451.
PRIDEP07451.

Protocols and materials databases

DNASU761.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285381; ENSP00000285381; ENSG00000164879.
GeneID761.
KEGGhsa:761.
UCSCuc003ydj.3. human.

Organism-specific databases

CTD761.
GeneCardsGC08P086285.
H-InvDBHIX0078885.
HGNCHGNC:1374. CA3.
HPACAB004967.
HPA021775.
HPA026700.
MIM114750. gene.
neXtProtNX_P07451.
PharmGKBPA25990.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3338.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidP07451.
KOK01672.
OMAEAPFTHF.
PhylomeDBP07451.
TreeFamTF316425.

Enzyme and pathway databases

BRENDA4.2.1.1. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP07451.
BgeeP07451.
CleanExHS_CA3.
GenevestigatorP07451.

Family and domain databases

Gene3D3.10.200.10. 1 hit.
InterProIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018441. Carbonic_anhydrase_CA3.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF96. PTHR18952:SF96. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. SSF51069. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07451.
GeneWikiCarbonic_anhydrase_III,_muscle_specific.
GenomeRNAi761.
NextBio3078.
PROP07451.
SOURCESearch...

Entry information

Entry nameCAH3_HUMAN
AccessionPrimary (citable) accession number: P07451
Secondary accession number(s): B2R867, B3KUC8, O60842
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: March 20, 2007
Last modified: July 9, 2014
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM