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Protein

Carbonic anhydrase-related protein

Gene

CA8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Does not have a carbonic anhydrase catalytic activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei116 – 1161Ancestral zinc ligand
Metal bindingi118 – 1181ZincSequence Analysis
Metal bindingi141 – 1411ZincSequence Analysis

GO - Molecular functioni

  1. carbonate dehydratase activity Source: ProtInc
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. one-carbon metabolic process Source: InterPro
  2. phosphatidylinositol-mediated signaling Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

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
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:1382. CA8.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Cerebellar ataxia, mental retardation, and dysequilibrium syndrome 31 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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001S → P in CMARQ3; affects protein stability owing to accelerated proteasomal degradation. 1 Publication
VAR_063634

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi613227. phenotype.
Orphaneti1766. Dysequilibrium syndrome.
PharmGKBiPA25997.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290Carbonic anhydrase-related proteinPRO_0000077433Add
BLAST

Proteomic databases

MaxQBiP35219.
PaxDbiP35219.
PeptideAtlasiP35219.
PRIDEiP35219.

PTM databases

PhosphoSiteiP35219.

Expressioni

Gene expression databases

BgeeiP35219.
CleanExiHS_CA8.
ExpressionAtlasiP35219. baseline and differential.
GenevestigatoriP35219.

Organism-specific databases

HPAiCAB025545.
CAB047309.
HPA024748.

Interactioni

Protein-protein interaction databases

BioGridi107222. 27 interactions.
IntActiP35219. 1 interaction.
MINTiMINT-1406878.
STRINGi9606.ENSP00000314407.

Structurei

Secondary structure

1
290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 344Combined sources
Helixi37 – 393Combined sources
Helixi42 – 454Combined sources
Helixi56 – 583Combined sources
Helixi63 – 664Combined sources
Beta strandi71 – 733Combined sources
Beta strandi77 – 848Combined sources
Beta strandi89 – 924Combined sources
Beta strandi97 – 1015Combined sources
Beta strandi110 – 11910Combined sources
Beta strandi128 – 1314Combined sources
Beta strandi137 – 14610Combined sources
Turni147 – 1493Combined sources
Helixi153 – 1564Combined sources
Beta strandi163 – 17412Combined sources
Helixi177 – 1837Combined sources
Helixi184 – 1896Combined sources
Beta strandi194 – 1996Combined sources
Helixi203 – 2064Combined sources
Beta strandi215 – 2217Combined sources
Beta strandi229 – 23810Combined sources
Beta strandi240 – 2423Combined sources
Helixi244 – 2507Combined sources
Beta strandi254 – 2563Combined sources
Beta strandi286 – 2883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W2JX-ray1.60A1-290[»]
ProteinModelPortaliP35219.
SMRiP35219. Positions 23-290.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35219.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi15 – 3622Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP35219.
KOiK01672.
OMAiDGMLGDN.
OrthoDBiEOG7WMCK7.
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.
IPR018434. Carbonic_anhydrase_RP_CA8.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF99. PTHR18952:SF99. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061Q → R in BAG52209 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001S → P in CMARQ3; affects protein stability owing to accelerated proteasomal degradation. 1 Publication
VAR_063634

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_004047.3. NM_004056.4.
UniGeneiHs.654388.

Genome annotation databases

EnsembliENST00000317995; ENSP00000314407; ENSG00000178538.
GeneIDi767.
KEGGihsa:767.
UCSCiuc003xtz.1. human.

Polymorphism databases

DMDMi461681.

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_004047.3. NM_004056.4.
UniGeneiHs.654388.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W2JX-ray1.60A1-290[»]
ProteinModelPortaliP35219.
SMRiP35219. Positions 23-290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107222. 27 interactions.
IntActiP35219. 1 interaction.
MINTiMINT-1406878.
STRINGi9606.ENSP00000314407.

Chemistry

DrugBankiDB00909. Zonisamide.

PTM databases

PhosphoSiteiP35219.

Polymorphism databases

DMDMi461681.

Proteomic databases

MaxQBiP35219.
PaxDbiP35219.
PeptideAtlasiP35219.
PRIDEiP35219.

Protocols and materials databases

DNASUi767.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000317995; ENSP00000314407; ENSG00000178538.
GeneIDi767.
KEGGihsa:767.
UCSCiuc003xtz.1. human.

Organism-specific databases

CTDi767.
GeneCardsiGC08M061151.
HGNCiHGNC:1382. CA8.
HPAiCAB025545.
CAB047309.
HPA024748.
MIMi114815. gene.
613227. phenotype.
neXtProtiNX_P35219.
Orphaneti1766. Dysequilibrium syndrome.
PharmGKBiPA25997.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP35219.
KOiK01672.
OMAiDGMLGDN.
OrthoDBiEOG7WMCK7.
PhylomeDBiP35219.
TreeFamiTF316425.

Miscellaneous databases

ChiTaRSiCA8. human.
EvolutionaryTraceiP35219.
GeneWikiiCA8.
GenomeRNAii767.
NextBioi3102.
PROiP35219.
SOURCEiSearch...

Gene expression databases

BgeeiP35219.
CleanExiHS_CA8.
ExpressionAtlasiP35219. baseline and differential.
GenevestigatoriP35219.

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.
IPR018434. Carbonic_anhydrase_RP_CA8.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF99. PTHR18952:SF99. 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. "The deduced amino acid sequence of human carbonic anhydrase-related protein (CARP) is 98% identical to the mouse homologue."
    Skaggs L.A., Bergenhem N.C.H., Venta P.J., Tashian R.E.
    Gene 126:291-292(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular identification of carbonic anhydrases (CA) and CA-related (CAR) genes."
    Chen Y., Huang C.-H.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Crystal structure of human carbonic anhydrase-related protein VIII reveals the basis for catalytic silencing."
    Picaud S.S., Muniz J.R.C., Kramm A., Pilka E.S., Kochan G., Oppermann U., Yue W.W.
    Proteins 76:507-511(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  8. "CA8 mutations cause a novel syndrome characterized by ataxia and mild mental retardation with predisposition to quadrupedal gait."
    Turkmen S., Guo G., Garshasbi M., Hoffmann K., Alshalah A.J., Mischung C., Kuss A., Humphrey N., Mundlos S., Robinson P.N.
    PLoS Genet. 5:E1000487-E1000487(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMARQ3 PRO-100, CHARACTERIZATION OF VARIANT CMARQ3 PRO-100.

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: February 4, 2015
This is version 132 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

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.