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Reviewed, UniProtKB/Swiss-Prot Q8CI85 (CAH12_MOUSE)

Last modified October 13, 2009. Version 61. 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

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Names and origin

Protein namesRecommended name:
    Carbonic anhydrase 12
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase XII
      Short name=CA-XII
    Carbonate dehydratase XII
Gene names
Name: Ca12
Synonyms: Car12
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein By similarity.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

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Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal
Transmembrane
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 354330Carbonic anhydrase 12
PRO_0000004249

Regions

Topological domain25 – 301277Extracellular Potential
Transmembrane302 – 32221 Potential
Topological domain323 – 35432Cytoplasmic Potential

Sites

Metal binding1201Zinc; catalytic
Metal binding1221Zinc; catalytic
Metal binding1461Zinc; catalytic

Amino acid modifications

Glycosylation281N-linked (GlcNAc...) Potential
Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation881N-linked (GlcNAc...) Potential
Disulfide bond50 ↔ 231 By similarity

Experimental info

Sequence conflict2971D → N in BAC35074. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q8CI85-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 98ED581BF2A16111

FASTA35439,695
        10         20         30         40         50         60 
MPHRSLRATV VLLLVILKKQ PSSSAPLNGS KWTYVGPAGE KNWSKKYPSC GGLLQSPIDL 

        70         80         90        100        110        120 
HSDILQYDAS LAPLQFQGYN VSVEKLLNLT NDGHSVRLNL NSDMYIQGLQ PHHYRAEQLH 

       130        140        150        160        170        180 
LHWGNRNDPH GSEHTVSGKH FAAELHIVHY NSDLYPDFST ASDKSEGLAV LAVLIEIGSA 

       190        200        210        220        230        240 
NPSYDKIFSH LQHVKYKGQQ VLIPGFNIEE LLPESPGEYY RYEGSLTTPP CYPTVLWTVF 

       250        260        270        280        290        300 
RNPVQISQEQ LLALETALYF THMDDPTPRE MINNFRQVQK FDERLVYISF RQGLLTDTGL 

       310        320        330        340        350 
SLGIILSVAL AGVLGISIVL AVSIWLFKRK KSKKGDNKGV IYKPAIKKEA EVHA

« Hide

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References

[1]"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: Kidney.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AK052639 mRNA. Translation: BAC35074.1.
BC035941 mRNA. Translation: AAH35941.1.
IPIIPI00319707.
RefSeqNP_848483.3.
UniGeneMm.277921

3D structure databases

HSSPHSSP built from PDB template 1JD0 based on UniProtKB O43570.
SMRQ8CI85. Positions 31-290.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8CI85.

PTM databases

PhosphoSiteQ8CI85.

Genome annotation databases

EnsemblENSMUST00000071889; ENSMUSP00000071786; ENSMUSG00000032373; Mus musculus. [Genome view]
GeneID76459.
KEGGmmu:76459.
UCSCuc009qfc.1. mouse.

Organism-specific databases

CTD76459.
MGIMGI:1923709. Car12.

Phylogenomic databases

HOGENOMQ8CI85.
HOVERGENQ8CI85.

Enzyme and pathway databases

BRENDA4.2.1.1. 244.

Gene expression databases

ArrayExpressQ8CI85.
BgeeQ8CI85.
CleanExMM_CAR12.
GenevestigatorQ8CI85.
GermOnlineENSMUSG00000032373. Mus musculus.

Family and domain databases

InterProIPR001148. Carbonic_anhydrase_a-class_cat.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018430. Carbonic_anhydrase_CA12.
[Graphical view]
PANTHERPTHR18952:SF19. Carbonic_anhydrase_CA12. 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

NextBio345196.
SOURCESearch...

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Entry information

Entry nameCAH12_MOUSE
AccessionPrimary (citable) accession number: Q8CI85
Secondary accession number(s): Q8BKG6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: March 1, 2003
Last modified: October 13, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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