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P35219

- CAH8_HUMAN

UniProt

P35219 - CAH8_HUMAN

Protein

Carbonic anhydrase-related protein

Gene

CA8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    Pathology & Biotechi

    Involvement in diseasei

    Cerebellar ataxia, mental retardation, and dysequilibrium syndrome 3 (CMARQ3) [MIM:613227]: A congenital cerebellar ataxia associated with dysarthia, quadrupedal gait and mental retardation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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

    ArrayExpressiP35219.
    BgeeiP35219.
    CleanExiHS_CA8.
    GenevestigatoriP35219.

    Organism-specific databases

    HPAiCAB025545.
    CAB047309.
    HPA024748.

    Interactioni

    Protein-protein interaction databases

    BioGridi107222. 3 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 – 344
    Helixi37 – 393
    Helixi42 – 454
    Helixi56 – 583
    Helixi63 – 664
    Beta strandi71 – 733
    Beta strandi77 – 848
    Beta strandi89 – 924
    Beta strandi97 – 1015
    Beta strandi110 – 11910
    Beta strandi128 – 1314
    Beta strandi137 – 14610
    Turni147 – 1493
    Helixi153 – 1564
    Beta strandi163 – 17412
    Helixi177 – 1837
    Helixi184 – 1896
    Beta strandi194 – 1996
    Helixi203 – 2064
    Beta strandi215 – 2217
    Beta strandi229 – 23810
    Beta strandi240 – 2423
    Helixi244 – 2507
    Beta strandi254 – 2563
    Beta strandi286 – 2883

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiP35219.
    KOiK01672.
    OMAiGHEFELH.
    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

    MADLSFIEDT VAFPEKEEDE EEEEEGVEWG YEEGVEWGLV FPDANGEYQS    50
    PINLNSREAR YDPSLLDVRL SPNYVVCRDC EVTNDGHTIQ VILKSKSVLS 100
    GGPLPQGHEF ELYEVRFHWG RENQRGSEHT VNFKAFPMEL HLIHWNSTLF 150
    GSIDEAVGKP HGIAIIALFV QIGKEHVGLK AVTEILQDIQ YKGKSKTIPC 200
    FNPNTLLPDP LLRDYWVYEG SLTIPPCSEG VTWILFRYPL TISQLQIEEF 250
    RRLRTHVKGA ELVEGCDGIL GDNFRPTQPL SDRVIRAAFQ 290
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6174.1.
    PIRi JN0576.
    RefSeqi NP_004047.3. NM_004056.4.
    UniGenei Hs.654388.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2W2J X-ray 1.60 A 1-290 [» ]
    ProteinModelPortali P35219.
    SMRi P35219. Positions 23-290.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107222. 3 interactions.
    IntActi P35219. 1 interaction.
    MINTi MINT-1406878.
    STRINGi 9606.ENSP00000314407.

    Chemistry

    BindingDBi P35219.

    PTM databases

    PhosphoSitei P35219.

    Polymorphism databases

    DMDMi 461681.

    Proteomic databases

    MaxQBi P35219.
    PaxDbi P35219.
    PeptideAtlasi P35219.
    PRIDEi P35219.

    Protocols and materials databases

    DNASUi 767.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317995 ; ENSP00000314407 ; ENSG00000178538 .
    GeneIDi 767.
    KEGGi hsa:767.
    UCSCi uc003xtz.1. human.

    Organism-specific databases

    CTDi 767.
    GeneCardsi GC08M061151.
    HGNCi HGNC:1382. CA8.
    HPAi CAB025545.
    CAB047309.
    HPA024748.
    MIMi 114815. gene.
    613227. phenotype.
    neXtProti NX_P35219.
    Orphaneti 1766. Dysequilibrium syndrome.
    PharmGKBi PA25997.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3338.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi P35219.
    KOi K01672.
    OMAi GHEFELH.
    OrthoDBi EOG7WMCK7.
    PhylomeDBi P35219.
    TreeFami TF316425.

    Miscellaneous databases

    ChiTaRSi CA8. human.
    EvolutionaryTracei P35219.
    GeneWikii CA8.
    GenomeRNAii 767.
    NextBioi 3102.
    PROi P35219.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35219.
    Bgeei P35219.
    CleanExi HS_CA8.
    Genevestigatori P35219.

    Family and domain databases

    Gene3Di 3.10.200.10. 1 hit.
    InterProi IPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    IPR018434. Carbonic_anhydrase_RP_CA8.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF99. PTHR18952:SF99. 1 hit.
    Pfami PF00194. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SMARTi SM01057. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51069. SSF51069. 1 hit.
    PROSITEi PS00162. ALPHA_CA_1. 1 hit.
    PS51144. ALPHA_CA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 128 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