[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0378-1119(86)90103-4; PubMed=3086182 [NCBI, ExPASy, EBI, Israel, Japan] Lloyd J., McMillan S., Hopkinson D., Edwards Y.H.; "Nucleotide sequence and derived amino acid sequence of a cDNA encoding human muscle carbonic anhydrase."; Gene 41:233-239(1986).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3099285 [NCBI, ExPASy, EBI, Israel, Japan] Wade R., Gunning P., Eddy R., Shows T., Kedes L.; "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."; Proc. Natl. Acad. Sci. U.S.A. 83:9571-9575(1986).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-31. TISSUE=Muscle; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2824285 [NCBI, ExPASy, EBI, Israel, Japan] Lloyd J., Brownson C., Tweedie S., Charlton J., Edwards Y.H.; "Human muscle carbonic anhydrase: gene structure and DNA methylation patterns in fetal and adult tissues."; Genes Dev. 1:594-602(1987).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11, AND DEVELOPMENTAL STAGE. DOI=10.1016/S0378-1119(98)00201-7; PubMed=9651514 [NCBI, ExPASy, EBI, Israel, Japan] Sowden J., Smith H., Morrison K., Edwards Y.; "Sequence comparisons and functional studies of the proximal promoter of the carbonic anhydrase 3 (CA3) gene."; Gene 214:157-165(1998).

Comments

FUNCTION: Reversible hydration of carbon dioxide.
CATALYTIC ACTIVITY: H₂CO₃ = CO₂ + H₂O.
COFACTOR: Zinc (By similarity).
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.
SIMILARITY: Belongs to the alpha-carbonic anhydrase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M29458; AAA52293.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M29452; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
BC004897; AAH04897.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ006473; CAA07056.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A26658; CRHU3.

NP_005172.1; -.

3D structure databases

PDB

1Z93; X-ray; 2.10 A; A=1-260.	[ExPASy / RCSB / EBI]
1Z97; X-ray; 2.10 A; A=1-260.	[ExPASy / RCSB / EBI]
2HFW; X-ray; 2.50 A; A=1-260.	[ExPASy / RCSB / EBI]
2HFX; X-ray; 1.70 A; A=1-260.	[ExPASy / RCSB / EBI]
2HFY; X-ray; 2.60 A; A=1-260.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1Z93; -.
1Z97; -.
2HFW; -.
2HFX; -.
2HFY; -.

ModBase

P07451.

2D gel databases

HSC-2DPAGE

P07451; -.

Organism-specific databases

HIX0078885; -.

HGNC:1374; CA3.

CA3.

CAB004967; -.

114750; gene. [NCBI / EBI]

PharmGKB

PA24378; -.

GeneCards

P07451.

Gene expression databases

ArrayExpress

P07451; -.

CleanEx

HS_CA3; -.

GermOnline

ENSG00000164879; Homo sapiens.

Ontologies

GO:0004089;	Molecular function: carbonate dehydratase activity (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR001148; Euk_COanhd.
Graphical view of domain structure.

Gene3D

G3DSA:3.10.200.10; Euk_COanhd; 1.

PANTHER

PTHR18952; Euk_COanhd; 1.

Pfam

PF00194; Carb_anhydrase; 1.
Pfam graphical view of domain structure.

ProDom

PD000865; Euk_COanhd; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00162; ALPHA_CA_1; 1.
PS51144; ALPHA_CA_2; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSG00000164879; Homo sapiens. [Contig view]

GeneID

761; -.

KEGG

hsa:761; -.

Phylogenomic databases

HOGENOM

P07451; -.

HOVERGEN

P07451; -.

Other

NextBio

3078; -.

SOURCE

CA3; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Lyase; Metal-binding; Polymorphism; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 260`	`259`	`Carbonic anhydrase 3.`	`PRO_0000077426`
`METAL`	`94 94`		`Zinc; catalytic.`
`METAL`	`96 96`		`Zinc; catalytic.`
`METAL`	`119 119`		`Zinc; catalytic.`
`VARIANT`	`31 31`	`1`	`V -> I (in dbSNP:rs20571 [NCBI]).`	`VAR_016180 [3D]`
`STRAND`	`7 12`	`6`
`HELIX`	`13 16`	`4`
`TURN`	`17 19`	`3`
`HELIX`	`21 24`	`4`
`HELIX`	`35 37`	`3`
`STRAND`	`47 50`	`4`
`HELIX`	`53 55`	`3`
`STRAND`	`56 61`	`6`
`STRAND`	`66 70`	`5`
`STRAND`	`73 81`	`9`
`STRAND`	`88 97`	`10`
`STRAND`	`106 109`	`4`
`STRAND`	`115 123`	`9`
`HELIX`	`125 127`	`3`
`HELIX`	`130 133`	`4`
`STRAND`	`139 151`	`13`
`HELIX`	`154 162`	`9`
`HELIX`	`163 166`	`4`
`STRAND`	`171 174`	`4`
`HELIX`	`180 183`	`4`
`STRAND`	`190 195`	`6`
`STRAND`	`206 213`	`8`
`STRAND`	`215 217`	`3`
`HELIX`	`219 225`	`7`
`STRAND`	`229 231`	`3`
`STRAND`	`233 235`	`3`
`STRAND`	`256 259`	`4`

Sequence information

Length: 260 AA [This is the length of the unprocessed precursor]

Molecular weight: 29557 Da [This is the MW of the unprocessed precursor]

CRC64: A305334167233FCF [This is a checksum on the sequence]

        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

P07451 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools