Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8CI85

- CAH12_MOUSE

UniProt

Q8CI85 - CAH12_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Carbonic anhydrase 12

Gene

Ca12

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

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zinc.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. one-carbon metabolic process Source: InterPro
  3. 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

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...

Topological domain

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

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei302 – 32221HelicalSequence AnalysisAdd
BLAST

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.
GeneTreeiENSGT00760000118915.
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:
EMBL
GenBank
DDBJ
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

EnsembliENSMUST00000071889; ENSMUSP00000071786; ENSMUSG00000032373.
GeneIDi76459.
KEGGimmu:76459.
UCSCiuc009qfc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK052639 mRNA. Translation: BAC35074.1 .
BC035941 mRNA. Translation: AAH35941.1 .
CCDSi CCDS23306.1.
RefSeqi NP_848483.3. NM_178396.4.
UniGenei Mm.277921.

3D structure databases

ProteinModelPortali Q8CI85.
SMRi Q8CI85. Positions 31-290.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8CI85. 2 interactions.
MINTi MINT-4089721.

PTM databases

PhosphoSitei Q8CI85.

Proteomic databases

MaxQBi Q8CI85.
PaxDbi Q8CI85.
PRIDEi Q8CI85.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000071889 ; ENSMUSP00000071786 ; ENSMUSG00000032373 .
GeneIDi 76459.
KEGGi mmu:76459.
UCSCi uc009qfc.2. mouse.

Organism-specific databases

CTDi 76459.
MGIi MGI:1923709. Car12.

Phylogenomic databases

eggNOGi COG3338.
GeneTreei ENSGT00760000118915.
HOGENOMi HOG000112637.
HOVERGENi HBG002837.
InParanoidi Q8CI85.
KOi K01672.
OrthoDBi EOG7WMCK7.
PhylomeDBi Q8CI85.
TreeFami TF316425.

Enzyme and pathway databases

Reactomei REACT_199096. Reversible hydration of carbon dioxide.

Miscellaneous databases

NextBioi 345196.
PROi Q8CI85.
SOURCEi Search...

Gene expression databases

Bgeei Q8CI85.
CleanExi MM_CAR12.
ExpressionAtlasi Q8CI85. baseline and differential.
Genevestigatori Q8CI85.

Family and domain databases

Gene3Di 3.10.200.10. 1 hit.
InterProi IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018430. Carbonic_anhydrase_CA12.
[Graphical view ]
PANTHERi PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF19. PTHR18952:SF19. 1 hit.
Pfami PF00194. Carb_anhydrase. 1 hit.
[Graphical view ]
SMARTi SM01057. Carb_anhydrase. 1 hit.
[Graphical view ]
SUPFAMi SSF51069. SSF51069. 1 hit.
PROSITEi PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 102 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