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Protein

Carbonic anhydrase 13

Gene

Ca13

Organism
Mus musculus (Mouse)
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 coumarins, sulfonamide derivatives such as acetazolamide (AZA) and Foscarnet (phosphonoformate trisodium salt).3 Publications

Sites

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

GO - Molecular functioni

  • carbonate dehydratase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1. 3474.
ReactomeiR-MMU-1475029. 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
Synonyms:Car13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1931322. Car13.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • myelin sheath Source: MGI
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2186.
GuidetoPHARMACOLOGYi2748.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 262262Carbonic anhydrase 13PRO_0000077441Add
BLAST

Proteomic databases

MaxQBiQ9D6N1.
PaxDbiQ9D6N1.
PRIDEiQ9D6N1.

PTM databases

PhosphoSiteiQ9D6N1.

Expressioni

Tissue specificityi

Expressed in spleen, lung, kidney, heart, brain, skeletal muscle and testis.1 Publication

Gene expression databases

BgeeiQ9D6N1.
CleanExiMM_CAR13.
GenevisibleiQ9D6N1. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029071.

Chemistry

BindingDBiQ9D6N1.

Structurei

3D structure databases

ProteinModelPortaliQ9D6N1.
SMRiQ9D6N1. Positions 4-261.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ9D6N1.
KOiK01672.
OMAiLQIGEPN.
OrthoDBiEOG7WMCK7.
PhylomeDBiQ9D6N1.
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.

Q9D6N1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARLSWGYGE HNGPIHWNEL FPIADGDQQS PIEIKTKEVK YDSSLRPLSI
60 70 80 90 100
KYDPASAKII SNSGHSFNVD FDDTEDKSVL RGGPLTGNYR LRQFHLHWGS
110 120 130 140 150
ADDHGSEHVV DGVRYAAELH VVHWNSDKYP SFVEAAHESD GLAVLGVFLQ
160 170 180 190 200
IGEHNPQLQK ITDILDSIKE KGKQTRFTNF DPLCLLPSSW DYWTYPGSLT
210 220 230 240 250
VPPLLESVTW IVLKQPISIS SQQLARFRSL LCTAEGESAA FLLSNHRPPQ
260
PLKGRRVRAS FY
Length:262
Mass (Da):29,522
Last modified:June 1, 2001 - v1
Checksum:iE3CA4674C1CF4A12
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF231123 mRNA. Translation: AAK16672.1.
AK010166 mRNA. Translation: BAB26742.1.
AK150871 mRNA. Translation: BAE29922.1.
AK150897 mRNA. Translation: BAE29942.1.
AK151519 mRNA. Translation: BAE30468.1.
AK151978 mRNA. Translation: BAE30845.1.
AK153080 mRNA. Translation: BAE31705.1.
AK153258 mRNA. Translation: BAE31849.1.
AK153353 mRNA. Translation: BAE31927.1.
AK162621 mRNA. Translation: BAE36996.1.
BC064050 mRNA. Translation: AAH64050.1.
CCDSiCCDS17247.1.
RefSeqiNP_078771.1. NM_024495.5.
UniGeneiMm.158776.

Genome annotation databases

EnsembliENSMUST00000029071; ENSMUSP00000029071; ENSMUSG00000027555.
GeneIDi71934.
KEGGimmu:71934.
UCSCiuc008oqo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF231123 mRNA. Translation: AAK16672.1.
AK010166 mRNA. Translation: BAB26742.1.
AK150871 mRNA. Translation: BAE29922.1.
AK150897 mRNA. Translation: BAE29942.1.
AK151519 mRNA. Translation: BAE30468.1.
AK151978 mRNA. Translation: BAE30845.1.
AK153080 mRNA. Translation: BAE31705.1.
AK153258 mRNA. Translation: BAE31849.1.
AK153353 mRNA. Translation: BAE31927.1.
AK162621 mRNA. Translation: BAE36996.1.
BC064050 mRNA. Translation: AAH64050.1.
CCDSiCCDS17247.1.
RefSeqiNP_078771.1. NM_024495.5.
UniGeneiMm.158776.

3D structure databases

ProteinModelPortaliQ9D6N1.
SMRiQ9D6N1. Positions 4-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029071.

Chemistry

BindingDBiQ9D6N1.
ChEMBLiCHEMBL2186.
GuidetoPHARMACOLOGYi2748.

PTM databases

PhosphoSiteiQ9D6N1.

Proteomic databases

MaxQBiQ9D6N1.
PaxDbiQ9D6N1.
PRIDEiQ9D6N1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029071; ENSMUSP00000029071; ENSMUSG00000027555.
GeneIDi71934.
KEGGimmu:71934.
UCSCiuc008oqo.2. mouse.

Organism-specific databases

CTDi71934.
MGIiMGI:1931322. Car13.

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ9D6N1.
KOiK01672.
OMAiLQIGEPN.
OrthoDBiEOG7WMCK7.
PhylomeDBiQ9D6N1.
TreeFamiTF316425.

Enzyme and pathway databases

BRENDAi4.2.1.1. 3474.
ReactomeiR-MMU-1475029. Reversible hydration of carbon dioxide.

Miscellaneous databases

NextBioi334994.
PROiQ9D6N1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D6N1.
CleanExiMM_CAR13.
GenevisibleiQ9D6N1. MM.

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. "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: C3H/HeJ.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone, Bone marrow and Tongue.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  4. Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
  5. "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I."
    Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T.
    Bioorg. Med. Chem. Lett. 17:2210-2215(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  6. "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.
  7. "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.

Entry informationi

Entry nameiCAH13_MOUSE
AccessioniPrimary (citable) accession number: Q9D6N1
Secondary accession number(s): Q3UBM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: June 1, 2001
Last modified: January 20, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.