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P35219 (CAH8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbonic anhydrase-related protein

Short name=CARP
Alternative name(s):
Carbonic anhydrase VIII
Short name=CA-VIII
Gene names
Name:CA8
Synonyms:CALS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Does not have a carbonic anhydrase catalytic activity.

Involvement in disease

Cerebellar ataxia, mental retardation, and dysequilibrium syndrome 3 (CMARQ3) [MIM:613227]: A congenital cerebellar ataxia associated with dysarthia, quadrupedal gait and mental retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 290290Carbonic anhydrase-related protein
PRO_0000077433

Regions

Compositional bias15 – 3622Glu-rich (acidic)

Sites

Metal binding1181Zinc Potential
Metal binding1411Zinc Potential
Site1161Ancestral zinc ligand

Natural variations

Natural variant1001S → P in CMARQ3; affects protein stability owing to accelerated proteasomal degradation. Ref.8
VAR_063634

Experimental info

Sequence conflict1061Q → R in BAG52209. Ref.3

Secondary structure

................................................. 290
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35219 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C142711660A972DB

FASTA29032,973
        10         20         30         40         50         60 
MADLSFIEDT VAFPEKEEDE EEEEEGVEWG YEEGVEWGLV FPDANGEYQS PINLNSREAR 

        70         80         90        100        110        120 
YDPSLLDVRL SPNYVVCRDC EVTNDGHTIQ VILKSKSVLS GGPLPQGHEF ELYEVRFHWG 

       130        140        150        160        170        180 
RENQRGSEHT VNFKAFPMEL HLIHWNSTLF GSIDEAVGKP HGIAIIALFV QIGKEHVGLK 

       190        200        210        220        230        240 
AVTEILQDIQ YKGKSKTIPC FNPNTLLPDP LLRDYWVYEG SLTIPPCSEG VTWILFRYPL 

       250        260        270        280        290 
TISQLQIEEF RRLRTHVKGA ELVEGCDGIL GDNFRPTQPL SDRVIRAAFQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6174.1.
PIRJN0576.
RefSeqNP_004047.3. NM_004056.4.
UniGeneHs.654388.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2W2JX-ray1.60A1-290[»]
ProteinModelPortalP35219.
SMRP35219. Positions 23-290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107222. 3 interactions.
IntActP35219. 1 interaction.
MINTMINT-1406878.
STRING9606.ENSP00000314407.

Chemistry

BindingDBP35219.

PTM databases

PhosphoSiteP35219.

Polymorphism databases

DMDM461681.

Proteomic databases

MaxQBP35219.
PaxDbP35219.
PeptideAtlasP35219.
PRIDEP35219.

Protocols and materials databases

DNASU767.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317995; ENSP00000314407; ENSG00000178538.
GeneID767.
KEGGhsa:767.
UCSCuc003xtz.1. human.

Organism-specific databases

CTD767.
GeneCardsGC08M061151.
HGNCHGNC:1382. CA8.
HPACAB025545.
CAB047309.
HPA024748.
MIM114815. gene.
613227. phenotype.
neXtProtNX_P35219.
Orphanet1766. Dysequilibrium syndrome.
PharmGKBPA25997.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3338.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidP35219.
KOK01672.
OMAGHEFELH.
OrthoDBEOG7WMCK7.
PhylomeDBP35219.
TreeFamTF316425.

Gene expression databases

ArrayExpressP35219.
BgeeP35219.
CleanExHS_CA8.
GenevestigatorP35219.

Family and domain databases

Gene3D3.10.200.10. 1 hit.
InterProIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018434. Carbonic_anhydrase_RP_CA8.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF99. PTHR18952:SF99. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. SSF51069. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCA8. human.
EvolutionaryTraceP35219.
GeneWikiCA8.
GenomeRNAi767.
NextBio3102.
PROP35219.
SOURCESearch...

Entry information

Entry nameCAH8_HUMAN
AccessionPrimary (citable) accession number: P35219
Secondary accession number(s): A8K0A5, B3KQZ7, Q32MY2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM