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Reviewed, UniProtKB/Swiss-Prot Q9D6N1 (CAH13_MOUSE)

Last modified November 3, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Carbonic anhydrase 13
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase XIII
      Short name=CA-XIII
    Carbonate dehydratase XIII
Gene names
Name: Ca13
Synonyms: Car13
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length262 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc By similarity.

Tissue specificity

Expressed in spleen, lung, kidney, heart, brain, skeletal muscle and testis. Ref.4

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionLyase
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 262262Carbonic anhydrase 13
PRO_0000077441

Sites

Metal binding951Zinc; catalytic By similarity
Metal binding971Zinc; catalytic By similarity
Metal binding1201Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9D6N1-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: E3CA4674C1CF4A12

FASTA26229,522
        10         20         30         40         50         60 
MARLSWGYGE HNGPIHWNEL FPIADGDQQS PIEIKTKEVK YDSSLRPLSI KYDPASAKII 

        70         80         90        100        110        120 
SNSGHSFNVD FDDTEDKSVL RGGPLTGNYR LRQFHLHWGS ADDHGSEHVV DGVRYAAELH 

       130        140        150        160        170        180 
VVHWNSDKYP SFVEAAHESD GLAVLGVFLQ IGEHNPQLQK ITDILDSIKE KGKQTRFTNF 

       190        200        210        220        230        240 
DPLCLLPSSW DYWTYPGSLT VPPLLESVTW IVLKQPISIS SQQLARFRSL LCTAEGESAA 

       250        260 
FLLSNHRPPQ PLKGRRVRAS FY 

« Hide

References

« Hide '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: C3H.
[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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
[4]"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: 14600151] [Abstract]
Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00109304.
RefSeqNP_078771.1.
UniGeneMm.158776

3D structure databases

HSSPHSSP built from PDB template 1CIM based on UniProtKB P00918.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9D6N1.

Proteomic databases

PRIDEQ9D6N1.

Genome annotation databases

EnsemblENSMUST00000029071; ENSMUSP00000029071; ENSMUSG00000027555; Mus musculus. [Genome view]
GeneID71934.
KEGGmmu:71934.
UCSCuc008oqo.1. mouse.

Organism-specific databases

CTD71934.
MGIMGI:1931322. Car13.

Phylogenomic databases

HOGENOMQ9D6N1.
HOVERGENQ9D6N1.
OMAMSRLSWG.

Enzyme and pathway databases

BRENDA4.2.1.1. 244.

Gene expression databases

ArrayExpressQ9D6N1.
BgeeQ9D6N1.
CleanExMM_CAR13.
GenevestigatorQ9D6N1.
GermOnlineENSMUSG00000027555. Mus musculus.

Family and domain databases

InterProIPR001148. Carbonic_anhydrase_a-class_cat.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018443. Carbonic_anhydrase_CA13.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952:SF31. Carbonic_anhydrase_CA13. 1 hit.
PTHR18952. Euk_COanhd. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
ProDomPD000865. Euk_COanhd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBQ9D6N1.
NextBio334994.
SOURCESearch...

Entry information

Entry nameCAH13_MOUSE
AccessionPrimary (citable) accession number: Q9D6N1
Secondary accession number(s): Q3UBM2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: June 1, 2001
Last modified: November 3, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents