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Protein

Carbonic anhydrase 1

Gene

Ca1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Enzyme regulationi

Inhibited by acetazolamide.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651Proton acceptorBy similarity
Metal bindingi95 – 951Zinc; catalytic
Metal bindingi97 – 971Zinc; catalytic
Metal bindingi120 – 1201Zinc; catalytic
Active sitei129 – 1291By similarity
Binding sitei200 – 2001SubstrateBy similarity

GO - Molecular functioni

  1. carbonate dehydratase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. one-carbon metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199094. Erythrocytes take up carbon dioxide and release oxygen.
REACT_199096. Reversible hydration of carbon dioxide.
REACT_199098. Erythrocytes take up oxygen and release carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 1 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase I
Carbonic anhydrase I
Short name:
CA-I
Gene namesi
Name:Ca1
Synonyms:Car1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:88268. Car1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 261260Carbonic anhydrase 1PRO_0000077413Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP13634.
PRIDEiP13634.

PTM databases

PhosphoSiteiP13634.

Expressioni

Gene expression databases

CleanExiMM_CAR1.
ExpressionAtlasiP13634. baseline and differential.
GenevestigatoriP13634.

Interactioni

Protein-protein interaction databases

BioGridi198481. 2 interactions.
IntActiP13634. 1 interaction.
MINTiMINT-4089732.

Structurei

3D structure databases

ProteinModelPortaliP13634.
SMRiP13634. Positions 5-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni200 – 2012Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP13634.
KOiK01672.
OMAiVTWIICK.
OrthoDBiEOG7WMCK7.
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.
IPR018442. Carbonic_anhydrase_CA1.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF82. PTHR18952:SF82. 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.

P13634-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASADWGYGS ENGPDQWSKL YPIANGNNQS PIDIKTSEAN HDSSLKPLSI
60 70 80 90 100
SYNPATAKEI VNVGHSFHVI FDDSSNQSVL KGGPLADSYR LTQFHFHWGN
110 120 130 140 150
SNDHGSEHTV DGTRYSGELH LVHWNSAKYS SASEAISKAD GLAILGVLMK
160 170 180 190 200
VGPANPSLQK VLDALNSVKT KGKRAPFTNF DPSSLLPSSL DYWTYFGSLT
210 220 230 240 250
HPPLHESVTW VICKDSISLS PEQLAQLRGL LSSAEGEPAV PVLSNHRPPQ
260
PLKGRTVRAS F
Length:261
Mass (Da):28,331
Last modified:October 3, 2012 - v4
Checksum:iD179AA7BA38EDF0E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti238 – 2381P → S in AAA37354. (PubMed:3104601)Curated
Sequence conflicti238 – 2381P → S in AAA50291. (PubMed:3104601)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32452 mRNA. Translation: AAA37354.1.
L36655
, M28197, L36650, L36651, L36652, L36653, L36654 Genomic DNA. Translation: AAA50291.1.
AK003066 mRNA. Translation: BAB22544.1.
AK146372 mRNA. Translation: BAE27121.1.
AK162331 mRNA. Translation: BAE36857.1.
AK167969 mRNA. Translation: BAE39964.1.
AK172076 mRNA. Translation: BAE42813.1.
AC167976 Genomic DNA. No translation available.
CH466577 Genomic DNA. Translation: EDL05133.1.
BC110681 mRNA. Translation: AAI10682.1.
BC132432 mRNA. Translation: AAI32433.1.
BC132434 mRNA. Translation: AAI32435.1.
BC011223 mRNA. Translation: AAH11223.1.
CCDSiCCDS17248.1.
PIRiA26344.
RefSeqiNP_001077426.1. NM_001083957.1.
NP_033929.2. NM_009799.4.
XP_006530112.1. XM_006530049.1.
UniGeneiMm.273195.

Genome annotation databases

EnsembliENSMUST00000094365; ENSMUSP00000091925; ENSMUSG00000027556.
ENSMUST00000181860; ENSMUSP00000137926; ENSMUSG00000027556.
GeneIDi12346.
KEGGimmu:12346.
UCSCiuc008oqp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M32452 mRNA. Translation: AAA37354.1.
L36655
, M28197, L36650, L36651, L36652, L36653, L36654 Genomic DNA. Translation: AAA50291.1.
AK003066 mRNA. Translation: BAB22544.1.
AK146372 mRNA. Translation: BAE27121.1.
AK162331 mRNA. Translation: BAE36857.1.
AK167969 mRNA. Translation: BAE39964.1.
AK172076 mRNA. Translation: BAE42813.1.
AC167976 Genomic DNA. No translation available.
CH466577 Genomic DNA. Translation: EDL05133.1.
BC110681 mRNA. Translation: AAI10682.1.
BC132432 mRNA. Translation: AAI32433.1.
BC132434 mRNA. Translation: AAI32435.1.
BC011223 mRNA. Translation: AAH11223.1.
CCDSiCCDS17248.1.
PIRiA26344.
RefSeqiNP_001077426.1. NM_001083957.1.
NP_033929.2. NM_009799.4.
XP_006530112.1. XM_006530049.1.
UniGeneiMm.273195.

3D structure databases

ProteinModelPortaliP13634.
SMRiP13634. Positions 5-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198481. 2 interactions.
IntActiP13634. 1 interaction.
MINTiMINT-4089732.

PTM databases

PhosphoSiteiP13634.

Proteomic databases

PaxDbiP13634.
PRIDEiP13634.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000094365; ENSMUSP00000091925; ENSMUSG00000027556.
ENSMUST00000181860; ENSMUSP00000137926; ENSMUSG00000027556.
GeneIDi12346.
KEGGimmu:12346.
UCSCiuc008oqp.1. mouse.

Organism-specific databases

CTDi12346.
MGIiMGI:88268. Car1.

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP13634.
KOiK01672.
OMAiVTWIICK.
OrthoDBiEOG7WMCK7.
TreeFamiTF316425.

Enzyme and pathway databases

ReactomeiREACT_199094. Erythrocytes take up carbon dioxide and release oxygen.
REACT_199096. Reversible hydration of carbon dioxide.
REACT_199098. Erythrocytes take up oxygen and release carbon dioxide.

Miscellaneous databases

NextBioi280986.
PROiP13634.
SOURCEiSearch...

Gene expression databases

CleanExiMM_CAR1.
ExpressionAtlasiP13634. baseline and differential.
GenevestigatoriP13634.

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.
IPR018442. Carbonic_anhydrase_CA1.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF82. PTHR18952:SF82. 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

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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.
    , 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: BALB/c, C57BL/6J and NOD.
    Tissue: Cecum and Spleen.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: FVB/N.
    Tissue: Brain and Colon.

Entry informationi

Entry nameiCAH1_MOUSE
AccessioniPrimary (citable) accession number: P13634
Secondary accession number(s): Q3TS19, Q9DC84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 3, 2012
Last modified: February 4, 2015
This is version 132 of the entry and version 4 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.