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P13634 (CAH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbonic anhydrase 1
EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase I
Carbonic anhydrase I
Short name=CA-I
Gene names
Name:Ca1
Synonyms:Car1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.

Enzyme regulation

Inhibited by acetazolamide By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
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: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 261260Carbonic anhydrase 1
PRO_0000077413

Regions

Region200 – 2012Substrate binding By similarity

Sites

Active site651Proton acceptor By similarity
Active site1291 By similarity
Metal binding951Zinc; catalytic
Metal binding971Zinc; catalytic
Metal binding1201Zinc; catalytic
Binding site2001Substrate By similarity

Experimental info

Sequence conflict2381S → P in BAB22544. Ref.3
Sequence conflict2381S → P in AAH11223. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P13634 [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

EMBL
GenBank
DDBJ		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. NM_001083957.1.
NP_033929.2. NM_009799.4.
UniGeneMm.273195.

3D structure databases

ProteinModelPortalP13634.
SMRP13634. Positions 5-261.
ModBaseSearch...

Protein-protein interaction databases

STRINGP13634.

PTM databases

PhosphoSiteP13634.

Proteomic databases

PRIDEP13634.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID12346.
KEGGmmu:12346.

Organism-specific databases

CTD12346.
MGIMGI:88268. Car1.

Phylogenomic databases

eggNOGroNOG06228.
HOGENOMHBG717384.
HOVERGENHBG002837.
InParanoidP13634.
OrthoDBEOG4X97HR.

Gene expression databases

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

Family and domain databases

InterProIPR001148. a_carbonic_anhydrase.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018442. Carbonic_anhydrase_CA1.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
KOK01672.
PANTHERPTHR18952:SF30. Carbonic_anhydrase_CA1. 1 hit.
PTHR18952. Euk_COanhd. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. Euk_COanhd. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

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: January 25, 2012
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents