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Reviewed, UniProtKB/Swiss-Prot P13634 (CAH1_MOUSE)

Last modified October 13, 2009. Version 85. 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 1
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase I
      Short name=CA-I
    Carbonate dehydratase I
Gene names
Name: Ca1
Synonyms: Car1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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

Initiator methionine11Removed By similarity
Chain2 – 261260Carbonic anhydrase 1
PRO_0000077413

Sites

Metal binding951Zinc; catalytic
Metal binding971Zinc; catalytic
Metal binding1201Zinc; catalytic

Experimental info

Sequence conflict2381S → P Ref.3
Sequence conflict2381S → P Ref.4

Sequences

Sequence LengthMass (Da)Tools
P13634-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 814AAA7BA38EDF0C

FASTA26128,321
        10         20         30         40         50         60 
MASADWGYGS ENGPDQWSKL YPIANGNNQS PIDIKTSEAN HDSSLKPLSI SYNPATAKEI 

        70         80         90        100        110        120 
VNVGHSFHVI FDDSSNQSVL KGGPLADSYR LTQFHFHWGN SNDHGSEHTV DGTRYSGELH 

       130        140        150        160        170        180 
LVHWNSAKYS SASEAISKAD GLAILGVLMK VGPANPSLQK VLDALNSVKT KGKRAPFTNF 

       190        200        210        220        230        240 
DPSSLLPSSL DYWTYFGSLT HPPLHESVTW VICKDSISLS PEQLAQLRGL LSSAEGESAV 

       250        260 
PVLSNHRPPQ PLKGRTVRAS F 

« Hide

References

« Hide 'large scale' references
[1]"Molecular evolution of the carbonic anhydrase genes: calculation of divergence time for mouse carbonic anhydrase I and II."
Fraser P.J., Curtis P.J.
J. Mol. Evol. 23:294-299(1986) [PubMed: 3104601] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The mouse carbonic anhydrase I gene contains two tissue-specific promoters."
Fraser P.J., Cummings P., Curtis P.J.
Mol. Cell. Biol. 9:3308-3313(1989) [PubMed: 2571923] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Brain.
[3]"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: Spleen.
[4]"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: Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

M32452 mRNA. Translation: AAA37354.1.
L36655 expand/collapse EMBL AC list , M28197, L36650, L36651, L36652, L36653, L36654 Genomic DNA. Translation: AAA50291.1.
AK003066 mRNA. Translation: BAB22544.1.
BC011223 mRNA. Translation: AAH11223.1.
IPIIPI00230320.
PIRA26344.
RefSeqNP_001077426.1.
NP_033929.2.
UniGeneMm.273195

3D structure databases

HSSPHSSP built from PDB template 1BZM based on UniProtKB P00915.
SMRP13634. Positions 5-261.
ModBaseSearch...

Protein-protein interaction databases

STRINGP13634.

PTM databases

PhosphoSiteP13634.

Proteomic databases

PRIDEP13634.

Genome annotation databases

EnsemblENSMUST00000094365; ENSMUSP00000091925; ENSMUSG00000027556; Mus musculus. [Genome view]
GeneID12346.
KEGGmmu:12346.

Organism-specific databases

CTD12346.
MGIMGI:88268. Car1.

Phylogenomic databases

HOGENOMP13634.
HOVERGENP13634.

Enzyme and pathway databases

BRENDA4.2.1.1. 244.

Gene expression databases

ArrayExpressP13634.
BgeeP13634.
CleanExMM_CAR1.
GenevestigatorP13634.
GermOnlineENSMUSG00000027556. Mus musculus.

Family and domain databases

InterProIPR001148. Carbonic_anhydrase_a-class_cat.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018442. Carbonic_anhydrase_CA1.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952:SF30. Carbonic_anhydrase_CA1. 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

NextBio280986.
SOURCESearch...

Entry information

Entry nameCAH1_MOUSE
AccessionPrimary (citable) accession number: P13634
Secondary accession number(s): Q9DC84
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: October 13, 2009
This is version 85 of the entry and version 3 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