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Q9QZA0 (CAH5B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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 5B, mitochondrial
EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase VB
Carbonic anhydrase VB
Short name=CA-VB
Gene names
Name:Ca5b
Synonyms:Car5b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

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

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.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processone-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrion

Inferred from direct assay Ref.1PubMed 18614015. Source: MGI

   Molecular_functioncarbonate dehydratase activity

Inferred from direct assay Ref.1. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Region235 – 2362Substrate binding By similarity

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

Sequences

Sequence LengthMass (Da)Tools
Q9QZA0 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF192978 mRNA. Translation: AAF08291.1.
AK085670 mRNA. Translation: BAC39501.1.
BC034413 mRNA. Translation: AAH34413.1.
IPIIPI00317025.
RefSeqNP_851832.2. NM_181315.4.
UniGeneMm.180953.

3D structure databases

ProteinModelPortalQ9QZA0.
SMRQ9QZA0. Positions 33-297.
ModBaseSearch...

PTM databases

PhosphoSiteQ9QZA0.

Proteomic databases

PaxDbQ9QZA0.
PRIDEQ9QZA0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033739; ENSMUSP00000033739; ENSMUSG00000031373.
GeneID56078.
KEGGmmu:56078.

Organism-specific databases

CTD56078.
MGIMGI:1926249. Car5b.

Phylogenomic databases

eggNOGCOG3338.
GeneTreeENSGT00560000076828.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidQ9QZA0.
KOK01672.
OrthoDBEOG4FR0RX.

Gene expression databases

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

Family and domain databases

Gene3D3.10.200.10. 1 hit.
InterProIPR018437. CA-V_mt.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF25. PTHR18952:SF25. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. Euk_COanhd. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL4634.
NextBio311872.
SOURCESearch...

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: May 1, 2013
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents