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Protein

Carbonic anhydrase-related protein

Gene

CA8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Does not have a carbonic anhydrase catalytic activity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei87Proton acceptorPROSITE-ProRule annotation1
Sitei116Ancestral zinc ligand1
Metal bindingi118ZincSequence analysis1
Metal bindingi141ZincSequence analysis1

GO - Molecular functioni

  • carbonate dehydratase activity Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS11294-MONOMER.
BRENDAi4.2.1.1. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase-related protein
Short name:
CARP
Alternative name(s):
Carbonic anhydrase VIII
Short name:
CA-VIII
Gene namesi
Name:CA8
Synonyms:CALS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:1382. CA8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Cerebellar ataxia, mental retardation, and dysequilibrium syndrome 3 (CMARQ3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA congenital cerebellar ataxia associated with dysarthia, quadrupedal gait and mental retardation.
See also OMIM:613227
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063634100S → P in CMARQ3; affects protein stability owing to accelerated proteasomal degradation. 1 PublicationCorresponds to variant rs267606695dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi767.
MalaCardsiCA8.
MIMi613227. phenotype.
OpenTargetsiENSG00000178538.
Orphaneti1766. Dysequilibrium syndrome.
PharmGKBiPA25997.

Chemistry databases

DrugBankiDB00909. Zonisamide.

Polymorphism and mutation databases

BioMutaiCA8.
DMDMi461681.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000774331 – 290Carbonic anhydrase-related proteinAdd BLAST290

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP35219.
MaxQBiP35219.
PaxDbiP35219.
PeptideAtlasiP35219.
PRIDEiP35219.

PTM databases

iPTMnetiP35219.
PhosphoSitePlusiP35219.

Expressioni

Gene expression databases

BgeeiENSG00000178538.
CleanExiHS_CA8.
GenevisibleiP35219. HS.

Organism-specific databases

HPAiCAB025545.
CAB047309.
HPA024748.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CRXO431863EBI-718700,EBI-748171
GGA2Q9UJY43EBI-718700,EBI-447646
HSD17B14Q9BPX15EBI-718700,EBI-742664
LNX1Q8TBB13EBI-718700,EBI-739832
MAGED1Q9Y5V35EBI-718700,EBI-716006
SPDL1Q96EA43EBI-718700,EBI-715381
TBX3O151193EBI-718700,EBI-3452216

Protein-protein interaction databases

BioGridi107222. 30 interactors.
IntActiP35219. 14 interactors.
MINTiMINT-1406878.
STRINGi9606.ENSP00000314407.

Structurei

Secondary structure

1290
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 34Combined sources4
Helixi37 – 39Combined sources3
Helixi42 – 45Combined sources4
Helixi56 – 58Combined sources3
Helixi63 – 66Combined sources4
Beta strandi71 – 73Combined sources3
Beta strandi77 – 84Combined sources8
Beta strandi89 – 92Combined sources4
Beta strandi97 – 101Combined sources5
Beta strandi110 – 119Combined sources10
Beta strandi128 – 131Combined sources4
Beta strandi137 – 146Combined sources10
Turni147 – 149Combined sources3
Helixi153 – 156Combined sources4
Beta strandi163 – 174Combined sources12
Helixi177 – 183Combined sources7
Helixi184 – 189Combined sources6
Beta strandi194 – 199Combined sources6
Helixi203 – 206Combined sources4
Beta strandi215 – 221Combined sources7
Beta strandi229 – 238Combined sources10
Beta strandi240 – 242Combined sources3
Helixi244 – 250Combined sources7
Beta strandi254 – 256Combined sources3
Beta strandi286 – 288Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2W2JX-ray1.60A1-290[»]
ProteinModelPortaliP35219.
SMRiP35219.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35219.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 289Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST263

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi15 – 36Glu-rich (acidic)Add BLAST22

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated
Contains 1 alpha-carbonic anhydrase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP35219.
KOiK01672.
OMAiDGMLGDN.
OrthoDBiEOG091G0XFM.
PhylomeDBiP35219.
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.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 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.

P35219-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLSFIEDT VAFPEKEEDE EEEEEGVEWG YEEGVEWGLV FPDANGEYQS
60 70 80 90 100
PINLNSREAR YDPSLLDVRL SPNYVVCRDC EVTNDGHTIQ VILKSKSVLS
110 120 130 140 150
GGPLPQGHEF ELYEVRFHWG RENQRGSEHT VNFKAFPMEL HLIHWNSTLF
160 170 180 190 200
GSIDEAVGKP HGIAIIALFV QIGKEHVGLK AVTEILQDIQ YKGKSKTIPC
210 220 230 240 250
FNPNTLLPDP LLRDYWVYEG SLTIPPCSEG VTWILFRYPL TISQLQIEEF
260 270 280 290
RRLRTHVKGA ELVEGCDGIL GDNFRPTQPL SDRVIRAAFQ
Length:290
Mass (Da):32,973
Last modified:January 23, 2007 - v3
Checksum:iC142711660A972DB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti106Q → R in BAG52209 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063634100S → P in CMARQ3; affects protein stability owing to accelerated proteasomal degradation. 1 PublicationCorresponds to variant rs267606695dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04656 mRNA. Translation: AAA35653.2.
AY075022 mRNA. Translation: AAL78170.1.
AK289470 mRNA. Translation: BAF82159.1.
AK314538 mRNA. Translation: BAG37128.1.
AK090655 mRNA. Translation: BAG52209.1.
CH471068 Genomic DNA. Translation: EAW86826.1.
BC069744 mRNA. Translation: AAH69744.1.
BC069794 mRNA. Translation: AAH69794.1.
BC108929 mRNA. Translation: AAI08930.1.
CCDSiCCDS6174.1.
PIRiJN0576.
RefSeqiNP_001308766.1. NM_001321837.1.
NP_001308767.1. NM_001321838.1.
NP_001308768.1. NM_001321839.1.
NP_004047.3. NM_004056.5.
UniGeneiHs.654388.
Hs.687269.

Genome annotation databases

EnsembliENST00000317995; ENSP00000314407; ENSG00000178538.
GeneIDi767.
KEGGihsa:767.
UCSCiuc003xtz.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04656 mRNA. Translation: AAA35653.2.
AY075022 mRNA. Translation: AAL78170.1.
AK289470 mRNA. Translation: BAF82159.1.
AK314538 mRNA. Translation: BAG37128.1.
AK090655 mRNA. Translation: BAG52209.1.
CH471068 Genomic DNA. Translation: EAW86826.1.
BC069744 mRNA. Translation: AAH69744.1.
BC069794 mRNA. Translation: AAH69794.1.
BC108929 mRNA. Translation: AAI08930.1.
CCDSiCCDS6174.1.
PIRiJN0576.
RefSeqiNP_001308766.1. NM_001321837.1.
NP_001308767.1. NM_001321838.1.
NP_001308768.1. NM_001321839.1.
NP_004047.3. NM_004056.5.
UniGeneiHs.654388.
Hs.687269.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2W2JX-ray1.60A1-290[»]
ProteinModelPortaliP35219.
SMRiP35219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107222. 30 interactors.
IntActiP35219. 14 interactors.
MINTiMINT-1406878.
STRINGi9606.ENSP00000314407.

Chemistry databases

DrugBankiDB00909. Zonisamide.

PTM databases

iPTMnetiP35219.
PhosphoSitePlusiP35219.

Polymorphism and mutation databases

BioMutaiCA8.
DMDMi461681.

Proteomic databases

EPDiP35219.
MaxQBiP35219.
PaxDbiP35219.
PeptideAtlasiP35219.
PRIDEiP35219.

Protocols and materials databases

DNASUi767.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000317995; ENSP00000314407; ENSG00000178538.
GeneIDi767.
KEGGihsa:767.
UCSCiuc003xtz.2. human.

Organism-specific databases

CTDi767.
DisGeNETi767.
GeneCardsiCA8.
HGNCiHGNC:1382. CA8.
HPAiCAB025545.
CAB047309.
HPA024748.
MalaCardsiCA8.
MIMi114815. gene.
613227. phenotype.
neXtProtiNX_P35219.
OpenTargetsiENSG00000178538.
Orphaneti1766. Dysequilibrium syndrome.
PharmGKBiPA25997.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP35219.
KOiK01672.
OMAiDGMLGDN.
OrthoDBiEOG091G0XFM.
PhylomeDBiP35219.
TreeFamiTF316425.

Enzyme and pathway databases

BioCyciZFISH:HS11294-MONOMER.
BRENDAi4.2.1.1. 2681.

Miscellaneous databases

ChiTaRSiCA8. human.
EvolutionaryTraceiP35219.
GeneWikiiCA8.
GenomeRNAii767.
PROiP35219.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000178538.
CleanExiHS_CA8.
GenevisibleiP35219. HS.

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.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 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...

Entry informationi

Entry nameiCAH8_HUMAN
AccessioniPrimary (citable) accession number: P35219
Secondary accession number(s): A8K0A5, B3KQZ7, Q32MY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Although it belongs to the alpha-carbonic anhydrase family, Arg-116 is present instead of the conserved His which is a zinc-binding residue. It is therefore expected that this protein lacks carbonic anhydrase activity.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.