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Protein

Carbonic anhydrase 12

Gene

Ca12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+By similarity

Enzyme regulationi

Inhibited by acetazolamide.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei94 – 941Proton acceptorBy similarity
Metal bindingi120 – 1201Zinc; catalytic
Metal bindingi122 – 1221Zinc; catalytic
Metal bindingi146 – 1461Zinc; catalytic
Active sitei155 – 1551By similarity

GO - Molecular functioni

  1. carbonate dehydratase activity Source: MGI
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. carbon dioxide transport Source: MGI
  2. chloride ion homeostasis Source: MGI
  3. one-carbon metabolic process Source: InterPro
  4. regulation of pH Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199096. Reversible hydration of carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 12 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase XII
Carbonic anhydrase XII
Short name:
CA-XII
Gene namesi
Name:Ca12
Synonyms:Car12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1923709. Car12.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 301277ExtracellularSequence AnalysisAdd
BLAST
Transmembranei302 – 32221HelicalSequence AnalysisAdd
BLAST
Topological domaini323 – 35432CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 354330Carbonic anhydrase 12PRO_0000004249Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi28 – 281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi50 ↔ 231By similarity
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8CI85.
PaxDbiQ8CI85.
PRIDEiQ8CI85.

PTM databases

PhosphoSiteiQ8CI85.

Expressioni

Gene expression databases

BgeeiQ8CI85.
CleanExiMM_CAR12.
ExpressionAtlasiQ8CI85. baseline and differential.
GenevestigatoriQ8CI85.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ8CI85. 2 interactions.
MINTiMINT-4089721.

Structurei

3D structure databases

ProteinModelPortaliQ8CI85.
SMRiQ8CI85. Positions 31-290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni227 – 2282Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3338.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ8CI85.
KOiK01672.
OrthoDBiEOG7WMCK7.
PhylomeDBiQ8CI85.
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.
IPR018430. Carbonic_anhydrase_CA12.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF19. PTHR18952:SF19. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8CI85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPHRSLRATV VLLLVILKKQ PSSSAPLNGS KWTYVGPAGE KNWSKKYPSC
60 70 80 90 100
GGLLQSPIDL HSDILQYDAS LAPLQFQGYN VSVEKLLNLT NDGHSVRLNL
110 120 130 140 150
NSDMYIQGLQ PHHYRAEQLH LHWGNRNDPH GSEHTVSGKH FAAELHIVHY
160 170 180 190 200
NSDLYPDFST ASDKSEGLAV LAVLIEIGSA NPSYDKIFSH LQHVKYKGQQ
210 220 230 240 250
VLIPGFNIEE LLPESPGEYY RYEGSLTTPP CYPTVLWTVF RNPVQISQEQ
260 270 280 290 300
LLALETALYF THMDDPTPRE MINNFRQVQK FDERLVYISF RQGLLTDTGL
310 320 330 340 350
SLGIILSVAL AGVLGISIVL AVSIWLFKRK KSKKGDNKGV IYKPAIKKEA

EVHA
Length:354
Mass (Da):39,695
Last modified:March 1, 2003 - v1
Checksum:i98ED581BF2A16111
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti297 – 2971D → N in BAC35074 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052639 mRNA. Translation: BAC35074.1.
BC035941 mRNA. Translation: AAH35941.1.
CCDSiCCDS23306.1.
RefSeqiNP_848483.3. NM_178396.4.
UniGeneiMm.277921.

Genome annotation databases

GeneIDi76459.
KEGGimmu:76459.
UCSCiuc009qfc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK052639 mRNA. Translation: BAC35074.1.
BC035941 mRNA. Translation: AAH35941.1.
CCDSiCCDS23306.1.
RefSeqiNP_848483.3. NM_178396.4.
UniGeneiMm.277921.

3D structure databases

ProteinModelPortaliQ8CI85.
SMRiQ8CI85. Positions 31-290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8CI85. 2 interactions.
MINTiMINT-4089721.

PTM databases

PhosphoSiteiQ8CI85.

Proteomic databases

MaxQBiQ8CI85.
PaxDbiQ8CI85.
PRIDEiQ8CI85.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi76459.
KEGGimmu:76459.
UCSCiuc009qfc.2. mouse.

Organism-specific databases

CTDi76459.
MGIiMGI:1923709. Car12.

Phylogenomic databases

eggNOGiCOG3338.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ8CI85.
KOiK01672.
OrthoDBiEOG7WMCK7.
PhylomeDBiQ8CI85.
TreeFamiTF316425.

Enzyme and pathway databases

ReactomeiREACT_199096. Reversible hydration of carbon dioxide.

Miscellaneous databases

NextBioi345196.
PROiQ8CI85.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CI85.
CleanExiMM_CAR12.
ExpressionAtlasiQ8CI85. baseline and differential.
GenevestigatoriQ8CI85.

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.
IPR018430. Carbonic_anhydrase_CA12.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF19. PTHR18952:SF19. 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

  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.
    , 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: 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.

Entry informationi

Entry nameiCAH12_MOUSE
AccessioniPrimary (citable) accession number: Q8CI85
Secondary accession number(s): Q8BKG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: March 1, 2003
Last modified: March 4, 2015
This is version 105 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

External Data

Dasty 3

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 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.