Q99N23 (CAH15_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbonic anhydrase 15
EC=4.2.1.1

Alternative name(s):
Carbonate dehydratase XV
Carbonic anhydrase XV
Short name=CA-XV

Gene names

Name:	Ca15
Synonyms:	Car15

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	324 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Reversible hydration of carbon dioxide By similarity.
Catalytic activity	H2CO3 = CO2 + H2O.
Cofactor	Zinc By similarity.
Enzyme regulation	Repressed by coumarins. Ref.3
Subcellular location	Secreted Potential.
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	anchored to plasma membrane Inferred from direct assay. Source: MGI extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Inferred from direct assay. Source: MGI
Molecular function	carbonate dehydratase activity Inferred from direct assay. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 324	306	Carbonic anhydrase 15		PRO_0000004253
Regions
	Region	231 – 232	2	Substrate binding By similarity
Sites
	Active site	90	1	Proton acceptor By similarity
	Active site	155	1	By similarity
	Metal binding	122	1	Zinc; catalytic By similarity
	Metal binding	124	1	Zinc; catalytic By similarity
	Metal binding	147	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	184	1	N-linked (GlcNAc...) Potential
	Glycosylation	194	1	N-linked (GlcNAc...) Potential
	Glycosylation	203	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q99N23 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: D285DD086476372F	FASTA	324	35,482
	10 20 30 40 50 60 MWALDFLLSF LLIQLAAQVD SSGTWCYDSQ DPKCGPAHWK ELAPACGGPT QSPINIDLRL 70 80 90 100 110 120 VQRDYTLKPF IFQGYDSAPQ DPWVLENDGH TVLLRVNSCQ QNCPAIRGAG LPSPEYRLLQ 130 140 150 160 170 180 LHFHWGSPGH QGSEHSLDEK HGSMEMHMVH MNTKYQSMED ARSQPDGFAI LAVLLVEEDR 190 200 210 220 230 240 DNTNFSAIVS GLKNLSSPGV AVNLTSTFAL ASLLPSALRL LRYYRYSGSL TTPGCEPAVL 250 260 270 280 290 300 WTVFENTVPI GHAQVVQFQA VLQTGPPGLH PRPLTSNFRP QQPLGGRRIS ASPEASVRSS 310 320 VSTLPCLHLA LVGLGVGLRL WQGP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization and evolution of two new members of the alpha-carbonic anhydrase gene family in mouse: Car13 and Car15." Hewett-Emmett D., Shimmin L.C. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Kidney.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[3]	"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: 19206230] [Abstract] Cited for: ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF231122 mRNA. Translation: AAK16671.1. BC019975 mRNA. Translation: AAH19975.1.
IPI	IPI00118013.
RefSeq	NP_085035.1. NM_030558.2.
UniGene	Mm.390864.
3D structure databases
ProteinModelPortal	Q99N23.
SMR	Q99N23. Positions 24-294.
ModBase	Search...
Protein-protein interaction databases
STRING	Q99N23.
Proteomic databases
PRIDE	Q99N23.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000118960; ENSMUSP00000113400; ENSMUSG00000090236.
GeneID	80733.
KEGG	mmu:80733.
Organism-specific databases
CTD	80733.
MGI	MGI:1931324. Car15.
Phylogenomic databases
GeneTree	ENSGT00570000078862.
HOVERGEN	HBG002837.
InParanoid	Q99N23.
PhylomeDB	Q99N23.
Gene expression databases
ArrayExpress	Q99N23.
Bgee	Q99N23.
CleanEx	MM_CAR15.
Genevestigator	Q99N23.
GermOnline	ENSMUSG00000003166. Mus musculus.
Family and domain databases
InterPro	IPR001148. a_carbonic_anhydrase. IPR023561. Carbonic_anhydrase_a-class. [Graphical view]
Gene3D	G3DSA:3.10.200.10. Euk_COanhd. 1 hit.
KO	K01672.
PANTHER	PTHR18952. Euk_COanhd. 1 hit.
Pfam	PF00194. Carb_anhydrase. 1 hit. [Graphical view]
SMART	SM01057. Carb_anhydrase. 1 hit. [Graphical view]
SUPFAM	SSF51069. Euk_COanhd. 1 hit.
PROSITE	PS00162. ALPHA_CA_1. False negative. PS51144. ALPHA_CA_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	350091.
SOURCE	Search...

Entry information

Entry name

CAH15_MOUSE

Accession

Primary (citable) accession number: Q99N23

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 9, 2003
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program