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Protein

Carbonic anhydrase 4

Gene

CA4

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Reversible hydration of carbon dioxide. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 (By similarity).By similarity

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+By similarity

Enzyme regulationi

Inhibited by acetazolamide.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881Proton acceptorBy similarity
Metal bindingi115 – 1151Zinc; catalyticBy similarity
Metal bindingi117 – 1171Zinc; catalyticBy similarity
Metal bindingi140 – 1401Zinc; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-BTA-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-BTA-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-BTA-1475029. Reversible hydration of carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 4 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase IV
Carbonic anhydrase IV
Short name:
CA-IV
Gene namesi
Name:CA4
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 19

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2096971.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818By similarityAdd
BLAST
Chaini19 – 284266Carbonic anhydrase 4PRO_0000004224Add
BLAST
Propeptidei285 – 31228Removed in mature formBy similarityPRO_0000004225Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 36By similarity
Glycosylationi33 – 331N-linked (GlcNAc...)Sequence analysis
Disulfide bondi46 ↔ 229By similarity
Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence analysis
Glycosylationi195 – 1951N-linked (GlcNAc...)Sequence analysis
Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence analysis
Lipidationi284 – 2841GPI-anchor amidated serineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ95323.
PRIDEiQ95323.

Interactioni

Subunit structurei

Interacts with SLC4A4.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000023909.

Chemistry

BindingDBiQ95323.

Structurei

3D structure databases

ProteinModelPortaliQ95323.
SMRiQ95323. Positions 23-284.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni225 – 2262Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ95323.
KOiK18246.
OMAiMDRGSEH.
OrthoDBiEOG7MD4QN.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018343. Carbonic_anhydrase_CA4.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF95. PTHR18952:SF95. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q95323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLLALLVL AAAPPQARAA SHWCYQIQVK PSNYTCLEPD EWEGSCQNNR
60 70 80 90 100
QSPVNIVTAK TQLDPNLGRF SFSGYNMKHQ WVVQNNGHTV MVLLENKPSI
110 120 130 140 150
AGGGLSTRYQ ATQLHLHWSR AMDRGSEHSF DGERFAMEMH IVHEKEKGLS
160 170 180 190 200
GNASQNQFAE DEIAVLAFMV EDGSKNVNFQ PLVEALSDIP RPNMNTTMKE
210 220 230 240 250
GVSLFDLLPE EESLRHYFRY LGSLTTPTCD EKVVWTVFQK PIQLHRDQIL
260 270 280 290 300
AFSQKLFYDD QQKVNMTDNV RPVQSLGQRQ VFRSGAPGLL LAQPLPTLLA
310
PVLACLTVGF LR
Length:312
Mass (Da):35,151
Last modified:February 1, 1997 - v1
Checksum:iBAEA320C09426351
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58870 mRNA. Translation: AAB09466.1.
BC142534 mRNA. Translation: AAI42535.1.
RefSeqiNP_776322.1. NM_173897.1.
UniGeneiBt.555.

Genome annotation databases

EnsembliENSBTAT00000023909; ENSBTAP00000023909; ENSBTAG00000017969.
GeneIDi280741.
KEGGibta:280741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U58870 mRNA. Translation: AAB09466.1.
BC142534 mRNA. Translation: AAI42535.1.
RefSeqiNP_776322.1. NM_173897.1.
UniGeneiBt.555.

3D structure databases

ProteinModelPortaliQ95323.
SMRiQ95323. Positions 23-284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000023909.

Chemistry

BindingDBiQ95323.
ChEMBLiCHEMBL2096971.

Proteomic databases

PaxDbiQ95323.
PRIDEiQ95323.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000023909; ENSBTAP00000023909; ENSBTAG00000017969.
GeneIDi280741.
KEGGibta:280741.

Organism-specific databases

CTDi762.

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ95323.
KOiK18246.
OMAiMDRGSEH.
OrthoDBiEOG7MD4QN.
TreeFamiTF316425.

Enzyme and pathway databases

ReactomeiR-BTA-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-BTA-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-BTA-1475029. Reversible hydration of carbon dioxide.

Miscellaneous databases

NextBioi20804912.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018343. Carbonic_anhydrase_CA4.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF95. PTHR18952:SF95. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bos taurus carbonic anhydrase IV (bovine carbonic anhydrase IV) mRNA, complete cds."
    Tamai S.
    Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Holstein.
    Tissue: Kidney.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.

Entry informationi

Entry nameiCAH4_BOVIN
AccessioniPrimary (citable) accession number: Q95323
Secondary accession number(s): A5PKL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 1, 1997
Last modified: May 11, 2016
This is version 127 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.