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Protein

Carbonic anhydrase 5B, mitochondrial

Gene

Ca5b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi130 – 1301Zinc; catalyticBy similarity
Metal bindingi132 – 1321Zinc; catalyticBy similarity
Metal bindingi155 – 1551Zinc; catalyticBy similarity

GO - Molecular functioni

  1. carbonate dehydratase activity Source: MGI
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. one-carbon metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199096. Reversible hydration of carbon dioxide.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 5B, mitochondrial (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase VB
Carbonic anhydrase VB
Short name:
CA-VB
Gene namesi
Name:Ca5b
Synonyms:Car5b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1926249. Car5b.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionBy similarityAdd
BLAST
Chaini34 – 317284Carbonic anhydrase 5B, mitochondrialPRO_0000004238Add
BLAST

Proteomic databases

MaxQBiQ9QZA0.
PaxDbiQ9QZA0.
PRIDEiQ9QZA0.

PTM databases

PhosphoSiteiQ9QZA0.

Expressioni

Gene expression databases

BgeeiQ9QZA0.
CleanExiMM_CAR5B.
GenevestigatoriQ9QZA0.

Structurei

3D structure databases

ProteinModelPortaliQ9QZA0.
SMRiQ9QZA0. Positions 33-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni235 – 2362Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ9QZA0.
KOiK01672.
OMAiIKHKDTL.
OrthoDBiEOG7WMCK7.
PhylomeDBiQ9QZA0.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018437. CA-VB_mt.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF25. PTHR18952:SF25. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9QZA0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVMNHLRVI LQVSSSTLPW RRCWVPRLVP RRSCSLYTCT YRTRNRALPP
60 70 80 90 100
LWENLDLVPA GDRQSPINIR WRDSVYDPGL KPLTISYDPA TCLHIWNNGY
110 120 130 140 150
SFLVEFEDST DKSVVEGGPL EHNYRLKQFH FHWGAIDAWG SEHTVDSKCY
160 170 180 190 200
PAELHLVHWN AVKFESFEDA ALEENGLAVI GVFLKLGKHH KELQKLVDTL
210 220 230 240 250
PSIKHKDTLV EFGSFDPSCL MPTCPDYWTY SGSLTTPPLS ESVTWIIKKQ
260 270 280 290 300
PVEVDRDQLE QFRTLLFTSE GEKEKRMVDN FRPLQPLMNR TVRSSFRHDY
310
VLNIQVKPKP TASEVTP
Length:317
Mass (Da):36,623
Last modified:May 9, 2003 - v2
Checksum:i719016A75305BFD3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691S → F in BAC39501 (PubMed:16141072).Curated
Sequence conflicti308 – 3081P → A in AAF08291 (PubMed:10677517).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF192978 mRNA. Translation: AAF08291.1.
AK085670 mRNA. Translation: BAC39501.1.
BC034413 mRNA. Translation: AAH34413.1.
CCDSiCCDS30515.1.
RefSeqiNP_851832.2. NM_181315.4.
UniGeneiMm.180953.

Genome annotation databases

EnsembliENSMUST00000033739; ENSMUSP00000033739; ENSMUSG00000031373.
GeneIDi56078.
KEGGimmu:56078.
UCSCiuc009uvb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF192978 mRNA. Translation: AAF08291.1.
AK085670 mRNA. Translation: BAC39501.1.
BC034413 mRNA. Translation: AAH34413.1.
CCDSiCCDS30515.1.
RefSeqiNP_851832.2. NM_181315.4.
UniGeneiMm.180953.

3D structure databases

ProteinModelPortaliQ9QZA0.
SMRiQ9QZA0. Positions 33-297.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9QZA0.

Proteomic databases

MaxQBiQ9QZA0.
PaxDbiQ9QZA0.
PRIDEiQ9QZA0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033739; ENSMUSP00000033739; ENSMUSG00000031373.
GeneIDi56078.
KEGGimmu:56078.
UCSCiuc009uvb.2. mouse.

Organism-specific databases

CTDi56078.
MGIiMGI:1926249. Car5b.

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ9QZA0.
KOiK01672.
OMAiIKHKDTL.
OrthoDBiEOG7WMCK7.
PhylomeDBiQ9QZA0.
TreeFamiTF316425.

Enzyme and pathway databases

ReactomeiREACT_199096. Reversible hydration of carbon dioxide.

Miscellaneous databases

NextBioi311872.
PROiQ9QZA0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZA0.
CleanExiMM_CAR5B.
GenevestigatoriQ9QZA0.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018437. CA-VB_mt.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF25. PTHR18952:SF25. 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. "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.
    , 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.

Entry informationi

Entry nameiCAH5B_MOUSE
AccessioniPrimary (citable) accession number: Q9QZA0
Secondary accession number(s): Q8C3J9, Q8K014
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 9, 2003
Last modified: January 7, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

External Data

Dasty 3

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 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.