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Reviewed, UniProtKB/Swiss-Prot Q9QZA0 (CAH5B_MOUSE)

Last modified November 3, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Carbonic anhydrase 5B, mitochondrial
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase VB
      Short name=CA-VB
    Carbonate dehydratase VB
Gene names
Name: Ca5b
Synonyms: Car5b
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc By similarity.

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

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Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionLyase
Gene Ontology (GO)
   Biological processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion Ref.1

Inferred from direct assay. Source: MGI

   Molecular functioncarbonate dehydratase activity Ref.1

Inferred from direct assay. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion By similarity
Chain34 – 317284Carbonic anhydrase 5B, mitochondrial
PRO_0000004238

Sites

Metal binding1301Zinc; catalytic By similarity
Metal binding1321Zinc; catalytic By similarity
Metal binding1551Zinc; catalytic By similarity

Experimental info

Sequence conflict2691S → F in BAC39501. Ref.2
Sequence conflict3081P → A in AAF08291. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q9QZA0-1 [UniParc].

Last modified May 9, 2003. Version 2.
Checksum: 719016A75305BFD3

FASTA31736,623
        10         20         30         40         50         60 
MAVMNHLRVI LQVSSSTLPW RRCWVPRLVP RRSCSLYTCT YRTRNRALPP LWENLDLVPA 

        70         80         90        100        110        120 
GDRQSPINIR WRDSVYDPGL KPLTISYDPA TCLHIWNNGY SFLVEFEDST DKSVVEGGPL 

       130        140        150        160        170        180 
EHNYRLKQFH FHWGAIDAWG SEHTVDSKCY PAELHLVHWN AVKFESFEDA ALEENGLAVI 

       190        200        210        220        230        240 
GVFLKLGKHH KELQKLVDTL PSIKHKDTLV EFGSFDPSCL MPTCPDYWTY SGSLTTPPLS 

       250        260        270        280        290        300 
ESVTWIIKKQ PVEVDRDQLE QFRTLLFTSE GEKEKRMVDN FRPLQPLMNR TVRSSFRHDY 

       310 
VLNIQVKPKP TASEVTP

« Hide

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References

« Hide 'large scale' references
[1]"Mitochondrial carbonic anhydrase CA VB: differences in tissue distribution and pattern of evolution from those of CA VA suggest distinct physiological roles."
Shah G.N., Hewett-Emmett D., Grubb J.H., Migas M.C., Fleming R.E., Waheed A., Sly W.S.
Proc. Natl. Acad. Sci. U.S.A. 97:1677-1682(2000) [PubMed: 10677517] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Mammary gland.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF192978 mRNA. Translation: AAF08291.1.
AK085670 mRNA. Translation: BAC39501.1.
BC034413 mRNA. Translation: AAH34413.1.
IPIIPI00317025.
RefSeqNP_851832.2.
UniGeneMm.180953
Mm.426337

3D structure databases

HSSPHSSP built from PDB template 1KEQ based on UniProtKB P23589.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9QZA0.

Proteomic databases

PRIDEQ9QZA0.

Genome annotation databases

EnsemblENSMUST00000033739; ENSMUSP00000033739; ENSMUSG00000031373; Mus musculus. [Genome view]
GeneID56078.
KEGGmmu:56078.
UCSCuc009uvc.1. mouse.

Organism-specific databases

CTD56078.
MGIMGI:1926249. Car5b.

Phylogenomic databases

HOGENOMQ9QZA0.
HOVERGENQ9QZA0.
OMASVIEGGP.

Enzyme and pathway databases

BRENDA4.2.1.1. 244.

Gene expression databases

ArrayExpressQ9QZA0.
BgeeQ9QZA0.
CleanExMM_CAR5B.
GenevestigatorQ9QZA0.
GermOnlineENSMUSG00000031373. Mus musculus.

Family and domain databases

InterProIPR001148. Carbonic_anhydrase_a-class_cat.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018437. Carbonic_anhydrase_CA5_mt.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952:SF25. Carbonic_anhydrase_CA5_mt. 1 hit.
PTHR18952. Euk_COanhd. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
ProDomPD000865. Euk_COanhd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio311872.
SOURCESearch...

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Entry information

Entry nameCAH5B_MOUSE
AccessionPrimary (citable) accession number: Q9QZA0
Secondary accession number(s): Q8C3J9, Q8K014
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 9, 2003
Last modified: November 3, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents