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Protein

Carbonic anhydrase-related protein

Gene

CA8

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

Functioni

Does not have a carbonic anhydrase catalytic activity.

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

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

Keywordsi

LigandMetal-binding, Zinc

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000178538.9
HGNCiHGNC:1382 CA8
MIMi114815 gene
neXtProtiNX_P35219

Subcellular locationi

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 dbSNP:rs267606695EnsemblClinVar.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
ProteomicsDBi54985

PTM databases

iPTMnetiP35219
PhosphoSitePlusiP35219

Expressioni

Gene expression databases

BgeeiENSG00000178538
CleanExiHS_CA8
GenevisibleiP35219 HS

Organism-specific databases

HPAiCAB025545
CAB047309
HPA024748

Interactioni

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi107222, 36 interactors
IntActiP35219, 15 interactors
MINTiP35219
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

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

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
InterProiView protein in InterPro
IPR001148 CA_dom
IPR036398 CA_dom_sf
IPR023561 Carbonic_anhydrase_a-class
IPR018338 Carbonic_anhydrase_a-class_CS
PANTHERiPTHR18952 PTHR18952, 1 hit
PfamiView protein in Pfam
PF00194 Carb_anhydrase, 1 hit
SMARTiView protein in SMART
SM01057 Carb_anhydrase, 1 hit
SUPFAMiSSF51069 SSF51069, 1 hit
PROSITEiView protein in PROSITE
PS00162 ALPHA_CA_1, 1 hit
PS51144 ALPHA_CA_2, 1 hit

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 dbSNP:rs267606695EnsemblClinVar.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

Similar proteinsi

Entry informationi

Entry nameiCAH8_HUMAN
AccessioniPrimary (citable) accession number: P35219
Secondary accession number(s): A8K0A5, B3KQZ7, Q32MY2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 157 of the entry and version 3 of the sequence. See 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

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

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