Q8N1Q1 (CAH13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbonic anhydrase 13
EC=4.2.1.1

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

Gene names

Name:

CA13

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	262 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Reversible hydration of carbon dioxide.
Catalytic activity	H2CO3 = CO2 + H2O.
Cofactor	Zinc By similarity.
Enzyme regulation	Inhibited by acetazolamide. Ref.4
Tissue specificity	Expressed in thymus, small intestine, spleen, prostate, ovary, colon and testis. Ref.3
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.
Biophysicochemical properties	Kinetic parameters: KM=13.8 mM for CO2 Ref.4

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Metal-binding Zinc
Molecular function	Lyase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bicarbonate transport Traceable author statement. Source: Reactome one-carbon metabolic process Inferred from electronic annotation. Source: InterPro small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	carbonate dehydratase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 262

262

Carbonic anhydrase 13

PRO_0000077440

Regions

Region

200 – 201

2

Substrate binding By similarity

Sites

Active site

65

1

Proton acceptor By similarity

Active site

68

1

By similarity

Active site

129

1

By similarity

Metal binding

95

1

Zinc; catalytic

Metal binding

97

1

Zinc; catalytic

Metal binding

120

1

Zinc; catalytic

Natural variations

Natural variant

68

1

N → S.
Corresponds to variant rs4740046 [ dbSNP | Ensembl ].

VAR_059207

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

262

Helix Strand Turn

Details...

Turn

10 – 12

3

Helix

14 – 19

6

Helix

22 – 25

4

Beta strand

26 – 28

3

Turn

36 – 38

3

Beta strand

48 – 51

4

Beta strand

56 – 62

7

Beta strand

64 – 71

8

Beta strand

75 – 82

8

Beta strand

89 – 98

10

Beta strand

107 – 110

4

Beta strand

116 – 125

10

Turn

126 – 128

3

Helix

132 – 135

4

Beta strand

141 – 151

11

Helix

156 – 162

7

Helix

163 – 168

6

Beta strand

174 – 176

3

Helix

182 – 185

4

Beta strand

192 – 197

6

Beta strand

208 – 215

8

Beta strand

217 – 219

3

Helix

221 – 227

7

Beta strand

230 – 234

5

Beta strand

258 – 260

3

Sequences

	Sequence		Length	Mass (Da)
	Q8N1Q1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: AE677F028ED729FE	FASTA	262	29,443
	10 20 30 40 50 60 MSRLSWGYRE HNGPIHWKEF FPIADGDQQS PIEIKTKEVK YDSSLRPLSI KYDPSSAKII 70 80 90 100 110 120 SNSGHSFNVD FDDTENKSVL RGGPLTGSYR LRQVHLHWGS ADDHGSEHIV DGVSYAAELH 130 140 150 160 170 180 VVHWNSDKYP SFVEAAHEPD GLAVLGVFLQ IGEPNSQLQK ITDTLDSIKE KGKQTRFTNF 190 200 210 220 230 240 DLLSLLPPSW DYWTYPGSLT VPPLLESVTW IVLKQPINIS SQQLAKFRSL LCTAEGEAAA 250 260 FLVSNHRPPQ PLKGRKVRAS FH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Tissue: Tongue.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[3]	"Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family." Lehtonen J., Shen B., Vihinen M., Casini A., Scozzafava A., Supuran C.T., Parkkila A.-K., Saarnio J., Kivelae A.J., Waheed A., Sly W.S., Parkkila S. J. Biol. Chem. 279:2719-2727(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
[4]	"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: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR ACETAZOLAMIDE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[5]	"X-ray structure of human carbonic anhydrase 13 in complex with inhibitor." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-261 IN COMPLEX WITH INHIBITOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK095314 mRNA. Translation: BAC04528.1.
BC052602 mRNA. Translation: AAH52602.1.

IPI

IPI00394767.

RefSeq

NP_940986.1. NM_198584.2.

UniGene

Hs.127189.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CZV	X-ray	2.00	A/B	1-262	[»]
3D0N	X-ray	1.55	A/B	1-262	[»]
3DA2	X-ray	2.05	A/B	1-261	[»]

ProteinModelPortal

Q8N1Q1.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000318912.

PTM databases

PhosphoSite

Q8N1Q1.

Polymorphism databases

DMDM

30580350.

2D gel databases

OGP

Q8N1Q1.

Proteomic databases

PaxDb

Q8N1Q1.

PeptideAtlas

Q8N1Q1.

PRIDE

Q8N1Q1.

Protocols and materials databases

DNASU

377677.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000321764; ENSP00000318912; ENSG00000185015.

GeneID

377677.

KEGG

hsa:377677.

UCSC

uc003ydg.2. human.

Organism-specific databases

CTD

377677.

GeneCards

GC08P086232.

HGNC

HGNC:14914. CA13.

HPA

CAB025567.
HPA024689.

MIM

611436. gene.

neXtProt

NX_Q8N1Q1.

PharmGKB

PA134891311.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3338.

HOGENOM

HOG000112637.

HOVERGEN

HBG002837.

InParanoid

Q8N1Q1.

KO

K01672.

OMA

SSQQLAK.

OrthoDB

EOG4X97HR.

Enzyme and pathway databases

BRENDA

4.2.1.1. 3474.

Reactome

REACT_111217. Metabolism.

Gene expression databases

Bgee

Q8N1Q1.

CleanEx

HS_CA13.

Genevestigator

Q8N1Q1.

GermOnline

ENSG00000185015. Homo sapiens.

Family and domain databases

Gene3D

3.10.200.10. 1 hit.

InterPro

IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018443. Carbonic_anhydrase_CA13.
[Graphical view]

PANTHER

PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF31. PTHR18952:SF31. 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. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q8N1Q1.

ChEMBL

CHEMBL3912.

ChiTaRS

CA13. human.

EvolutionaryTrace

Q8N1Q1.

GenomeRNAi

377677.

NextBio

100682.

SOURCE

Search...

Entry information

Entry name

CAH13_HUMAN

Accession

Primary (citable) accession number: Q8N1Q1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 9, 2003
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 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.