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Protein

Carbonic anhydrase 13

Gene

CA13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+By similarity

Enzyme regulationi

Inhibited by acetazolamide.1 Publication

Kineticsi

  1. KM=13.8 mM for CO21 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651Proton acceptorBy similarity
Active sitei68 – 681By similarity
Metal bindingi95 – 951Zinc; catalytic
Metal bindingi97 – 971Zinc; catalytic
Metal bindingi120 – 1201Zinc; catalytic
Active sitei129 – 1291By similarity

GO - Molecular functioni

  1. carbonate dehydratase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. bicarbonate transport Source: Reactome
  2. one-carbon metabolic process Source: InterPro
  3. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_121123. Reversible hydration of carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 13 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase XIII
Carbonic anhydrase XIII
Short name:
CA-XIII
Gene namesi
Name:CA13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:14914. CA13.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. myelin sheath Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134891311.

Chemistry

DrugBankiDB00909. Zonisamide.

Polymorphism and mutation databases

BioMutaiCA13.
DMDMi30580350.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262Carbonic anhydrase 13PRO_0000077440Add
BLAST

Proteomic databases

MaxQBiQ8N1Q1.
PaxDbiQ8N1Q1.
PeptideAtlasiQ8N1Q1.
PRIDEiQ8N1Q1.

2D gel databases

OGPiQ8N1Q1.

PTM databases

PhosphoSiteiQ8N1Q1.

Expressioni

Tissue specificityi

Expressed in thymus, small intestine, spleen, prostate, ovary, colon and testis.1 Publication

Gene expression databases

BgeeiQ8N1Q1.
CleanExiHS_CA13.
GenevestigatoriQ8N1Q1.

Organism-specific databases

HPAiCAB025567.
HPA024689.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000318912.

Structurei

Secondary structure

1
262
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni10 – 123Combined sources
Helixi14 – 207Combined sources
Helixi22 – 254Combined sources
Beta strandi26 – 283Combined sources
Turni36 – 383Combined sources
Beta strandi48 – 514Combined sources
Beta strandi56 – 627Combined sources
Beta strandi64 – 718Combined sources
Beta strandi74 – 829Combined sources
Beta strandi89 – 9810Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi116 – 12510Combined sources
Turni126 – 1283Combined sources
Helixi132 – 1354Combined sources
Beta strandi141 – 15111Combined sources
Helixi156 – 1627Combined sources
Helixi163 – 1686Combined sources
Beta strandi174 – 1763Combined sources
Helixi182 – 1854Combined sources
Beta strandi192 – 1976Combined sources
Beta strandi208 – 2158Combined sources
Beta strandi217 – 2193Combined sources
Helixi221 – 2277Combined sources
Beta strandi230 – 2345Combined sources
Beta strandi258 – 2603Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CZVX-ray2.00A/B1-262[»]
3D0NX-ray1.55A/B1-262[»]
3DA2X-ray2.05A/B1-261[»]
4HU1X-ray1.95A/B1-262[»]
4KNMX-ray1.90A/B1-262[»]
4KNNX-ray1.40A/B1-262[»]
4QSJX-ray1.70A/B1-262[»]
ProteinModelPortaliQ8N1Q1.
SMRiQ8N1Q1. Positions 5-262.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N1Q1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni200 – 2012Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ8N1Q1.
KOiK01672.
OMAiQIGEPNS.
OrthoDBiEOG7WMCK7.
PhylomeDBiQ8N1Q1.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8N1Q1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRLSWGYRE HNGPIHWKEF FPIADGDQQS PIEIKTKEVK YDSSLRPLSI
60 70 80 90 100
KYDPSSAKII SNSGHSFNVD FDDTENKSVL RGGPLTGSYR LRQVHLHWGS
110 120 130 140 150
ADDHGSEHIV DGVSYAAELH VVHWNSDKYP SFVEAAHEPD GLAVLGVFLQ
160 170 180 190 200
IGEPNSQLQK ITDTLDSIKE KGKQTRFTNF DLLSLLPPSW DYWTYPGSLT
210 220 230 240 250
VPPLLESVTW IVLKQPINIS SQQLAKFRSL LCTAEGEAAA FLVSNHRPPQ
260
PLKGRKVRAS FH
Length:262
Mass (Da):29,443
Last modified:October 1, 2002 - v1
Checksum:iAE677F028ED729FE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681N → S.
Corresponds to variant rs4740046 [ dbSNP | Ensembl ].
VAR_059207

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK095314 mRNA. Translation: BAC04528.1.
BC052602 mRNA. Translation: AAH52602.1.
CCDSiCCDS6236.1.
RefSeqiNP_940986.1. NM_198584.2.
UniGeneiHs.127189.

Genome annotation databases

EnsembliENST00000321764; ENSP00000318912; ENSG00000185015.
GeneIDi377677.
KEGGihsa:377677.
UCSCiuc003ydg.2. human.

Polymorphism and mutation databases

BioMutaiCA13.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK095314 mRNA. Translation: BAC04528.1.
BC052602 mRNA. Translation: AAH52602.1.
CCDSiCCDS6236.1.
RefSeqiNP_940986.1. NM_198584.2.
UniGeneiHs.127189.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CZVX-ray2.00A/B1-262[»]
3D0NX-ray1.55A/B1-262[»]
3DA2X-ray2.05A/B1-261[»]
4HU1X-ray1.95A/B1-262[»]
4KNMX-ray1.90A/B1-262[»]
4KNNX-ray1.40A/B1-262[»]
4QSJX-ray1.70A/B1-262[»]
ProteinModelPortaliQ8N1Q1.
SMRiQ8N1Q1. Positions 5-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000318912.

Chemistry

BindingDBiQ8N1Q1.
ChEMBLiCHEMBL2095180.
DrugBankiDB00909. Zonisamide.

PTM databases

PhosphoSiteiQ8N1Q1.

Polymorphism and mutation databases

BioMutaiCA13.
DMDMi30580350.

2D gel databases

OGPiQ8N1Q1.

Proteomic databases

MaxQBiQ8N1Q1.
PaxDbiQ8N1Q1.
PeptideAtlasiQ8N1Q1.
PRIDEiQ8N1Q1.

Protocols and materials databases

DNASUi377677.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321764; ENSP00000318912; ENSG00000185015.
GeneIDi377677.
KEGGihsa:377677.
UCSCiuc003ydg.2. human.

Organism-specific databases

CTDi377677.
GeneCardsiGC08P086232.
HGNCiHGNC:14914. CA13.
HPAiCAB025567.
HPA024689.
MIMi611436. gene.
neXtProtiNX_Q8N1Q1.
PharmGKBiPA134891311.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ8N1Q1.
KOiK01672.
OMAiQIGEPNS.
OrthoDBiEOG7WMCK7.
PhylomeDBiQ8N1Q1.
TreeFamiTF316425.

Enzyme and pathway databases

ReactomeiREACT_121123. Reversible hydration of carbon dioxide.

Miscellaneous databases

ChiTaRSiCA13. human.
EvolutionaryTraceiQ8N1Q1.
GenomeRNAii377677.
NextBioi100682.
PROiQ8N1Q1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N1Q1.
CleanExiHS_CA13.
GenevestigatoriQ8N1Q1.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCAH13_HUMAN
AccessioniPrimary (citable) accession number: Q8N1Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: October 1, 2002
Last modified: April 29, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.