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Protein

Carbonic anhydrase-related protein

Gene

Ca8

Organism
Mus musculus (Mouse)
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
Sitei117 – 1171Ancestral zinc ligand
Metal bindingi119 – 1191ZincSequence analysis
Metal bindingi142 – 1421ZincSequence analysis

GO - Molecular functioni

GO - Biological processi

  • one-carbon metabolic process Source: InterPro
  • phosphatidylinositol-mediated signaling Source: MGI
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, Cals1, Car8, Carp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:88253. Car8.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi115 – 1173EVR → QVH: Restores zinc-binding and activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 291291Carbonic anhydrase-related proteinPRO_0000077434Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP28651.
MaxQBiP28651.
PaxDbiP28651.
PRIDEiP28651.

PTM databases

iPTMnetiP28651.
PhosphoSiteiP28651.

Expressioni

Tissue specificityi

Expressed only in Purkinje cells.

Gene expression databases

BgeeiP28651.
CleanExiMM_CAR8.
GenevisibleiP28651. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000063511.

Structurei

3D structure databases

ProteinModelPortaliP28651.
SMRiP28651. Positions 24-291.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi15 – 3723Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP28651.
KOiK01672.
OMAiDGMLGDN.
OrthoDBiEOG7WMCK7.
PhylomeDBiP28651.
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.

P28651-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLSFIEDA VAFPEKEEDE EEEEEEGVEW GYEEGVEWGL VFPDANGEYQ
60 70 80 90 100
SPINLNSREA RYDPSLLDVR LSPNYVVCRD CEVTNDGHTI QVILKSKSVL
110 120 130 140 150
SGGPLPQGQE FELYEVRFHW GRENQRGSEH TVNFKAFPME LHLIHWNSTL
160 170 180 190 200
FGSIDEAVGK PHGIAIIALF VQIGKEHVGL KAVTEILQDI QYKGKSKTIP
210 220 230 240 250
CFNPNTLLPD PLLRDYWVYE GSLTIPPCSE GVTWILFRYP LTISQMQIEE
260 270 280 290
FRRLRTHVKG AELVEGCDGI LGDNFRPTQP LSDRVIRAAF Q
Length:291
Mass (Da):33,081
Last modified:January 23, 2007 - v5
Checksum:iFAA2B1678A9AEF54
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti261 – 2611A → V in CAA43668 (PubMed:2121526).Curated
Sequence conflicti285 – 2851V → I in BAC25100 (PubMed:16141072).Curated
Sequence conflicti291 – 2911Q → SSQRDREQTHLHQ in CAA43668 (PubMed:2121526).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61397 mRNA. Translation: CAA43668.1.
AK004896 mRNA. Translation: BAC25100.1.
BC010773 mRNA. Translation: AAH10773.1.
CCDSiCCDS17954.1.
PIRiS12867.
RefSeqiNP_031618.2. NM_007592.3.
UniGeneiMm.119320.

Genome annotation databases

EnsembliENSMUST00000066674; ENSMUSP00000063511; ENSMUSG00000041261.
GeneIDi12319.
KEGGimmu:12319.
UCSCiuc008rxv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61397 mRNA. Translation: CAA43668.1.
AK004896 mRNA. Translation: BAC25100.1.
BC010773 mRNA. Translation: AAH10773.1.
CCDSiCCDS17954.1.
PIRiS12867.
RefSeqiNP_031618.2. NM_007592.3.
UniGeneiMm.119320.

3D structure databases

ProteinModelPortaliP28651.
SMRiP28651. Positions 24-291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000063511.

PTM databases

iPTMnetiP28651.
PhosphoSiteiP28651.

Proteomic databases

EPDiP28651.
MaxQBiP28651.
PaxDbiP28651.
PRIDEiP28651.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066674; ENSMUSP00000063511; ENSMUSG00000041261.
GeneIDi12319.
KEGGimmu:12319.
UCSCiuc008rxv.1. mouse.

Organism-specific databases

CTDi12319.
MGIiMGI:88253. Car8.

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP28651.
KOiK01672.
OMAiDGMLGDN.
OrthoDBiEOG7WMCK7.
PhylomeDBiP28651.
TreeFamiTF316425.

Miscellaneous databases

NextBioi280888.
PROiP28651.
SOURCEiSearch...

Gene expression databases

BgeeiP28651.
CleanExiMM_CAR8.
GenevisibleiP28651. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a novel carbonic anhydrase-related polypeptide and its exclusive presence in Purkinje cells."
    Kato K.
    FEBS Lett. 271:137-140(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "Two point mutations convert a catalytically inactive carbonic anhydrase-related protein (CARP) to an active enzyme."
    Sjoeblom B., Elleby B., Wallgren K., Jonsson B.-H., Lindskog S.
    FEBS Lett. 398:322-325(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, MUTAGENESIS.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  4. "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].
    Tissue: Colon.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Liver and Lung.

Entry informationi

Entry nameiCAH8_MOUSE
AccessioniPrimary (citable) accession number: P28651
Secondary accession number(s): Q8CF58, Q91XF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 129 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Although it belongs to the alpha-carbonic anhydrase family, Arg-117 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.