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Reviewed, UniProtKB/Swiss-Prot Q8N1Q1 (CAH13_HUMAN)

Last modified June 16, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 13
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase XIII
      Short name=CA-XIII
    Carbonate dehydratase XIII
Gene names
Name: CA13
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length262 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Reversible hydration of carbon dioxide.

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc By similarity.

Tissue specificity

Expressed in thymus, small intestine, spleen, prostate, ovary, colon and testis. Ref.3

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

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Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processone-carbon compound metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functioncarbonate dehydratase activity

Inferred from electronic annotation. Source: EC

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

Chain1 – 262262Carbonic anhydrase 13
PRO_0000077440

Sites

Metal binding951Zinc; catalytic By similarity
Metal binding971Zinc; catalytic By similarity
Metal binding1201Zinc; catalytic By similarity

Secondary structure

1 ................................................. 262
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q8N1Q1-1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: AE677F028ED729FE

FASTA26229,443
        10         20         30         40         50         60 
MSRLSWGYRE HNGPIHWKEF FPIADGDQQS PIEIKTKEVK YDSSLRPLSI KYDPSSAKII 

        70         80         90        100        110        120 
SNSGHSFNVD FDDTENKSVL RGGPLTGSYR LRQVHLHWGS ADDHGSEHIV DGVSYAAELH 

       130        140        150        160        170        180 
VVHWNSDKYP SFVEAAHEPD GLAVLGVFLQ IGEPNSQLQK ITDTLDSIKE KGKQTRFTNF 

       190        200        210        220        230        240 
DLLSLLPPSW DYWTYPGSLT VPPLLESVTW IVLKQPINIS SQQLAKFRSL LCTAEGEAAA 

       250        260 
FLVSNHRPPQ PLKGRKVRAS FH

« Hide

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References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Tongue.
[2]"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: Pancreas.
[3]"Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family."
Lehtonen J., Shen B., Vihinen M., Casini A., Scozzafava A., Supuran C.T., Parkkila A.-K., Saarnio J., Kivelae A.J., Waheed A., Sly W.S., Parkkila S.
J. Biol. Chem. 279:2719-2727(2004) [PubMed: 14600151] [Abstract]
Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AK095314 mRNA. Translation: BAC04528.1.
BC052602 mRNA. Translation: AAH52602.1.
IPIIPI00394767.
RefSeqNP_940986.1.
UniGeneHs.127189

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3CZVX-ray2.00A/B1-262[»]
3D0NX-ray1.55A/B1-262[»]
3DA2X-ray2.05A/B1-261[»]
ModBaseSearch...

2-D gel databases

OGPQ8N1Q1.

Proteomic databases

PeptideAtlasQ8N1Q1.
PRIDEQ8N1Q1.

Genome annotation databases

EnsemblENSG00000185015. Homo sapiens. [Contig view]
GeneID377677.
KEGGhsa:377677.

Organism-specific databases

GeneCardsGC08P086345.
H-InvDBHIX0007627.
HGNCHGNC:14914. CA13.
MIM611436. gene.
PharmGKBPA134925234.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ8N1Q1.
HOVERGENQ8N1Q1.
OMAQ8N1Q1. MSRLSWG.

Enzyme and pathway databases

BRENDA4.2.1.1. 247.

Gene expression databases

ArrayExpressQ8N1Q1.
BgeeQ8N1Q1.
CleanExHS_CA13.
GermOnlineENSG00000185015. Homo sapiens.

Family and domain databases

InterProIPR001148. Carbonic_anhydrase_a-class_cat.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018443. Carbonic_anhydrase_CA13.
[Graphical view]
Gene3DG3DSA:3.10.200.10. Euk_COanhd. 1 hit.
PANTHERPTHR18952:SF31. Carbonic_anhydrase_CA13. 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

NextBio100682.
SOURCESearch...

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Entry information

Entry nameCAH13_HUMAN
AccessionPrimary (citable) accession number: Q8N1Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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