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UniProtKB/Swiss-Prot entry Q8N1Q1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CAH13_HUMAN
Primary accession number Q8N1Q1
Secondary accession numbers None
Integrated into Swiss-Prot on May 9, 2003
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 51)
Name and origin of the protein
Protein name Carbonic anhydrase 13
Synonyms EC 4.2.1.1
Carbonic anhydrase XIII
CA-XIII
Carbonate dehydratase XIII
Gene name
Name: CA13
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
CHARACTERIZATION, AND TISSUE SPECIFICITY.
DOI=10.1074/jbc.M308984200; PubMed=14600151 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Characterization of CA XIII, a novel member of the carbonic anhydrase isozyme family.";
J. Biol. Chem. 279:2719-2727(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK095314; BAC04528.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC052602; AAH52602.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_940986.1; -.
UniGene Hs.127189
3D structure databases
PDB
3CZV; X-ray; 2.00 A; A/B=1-262.[ExPASy / RCSB / EBI]
3D0N; X-ray; 1.55 A; A/B=1-262.[ExPASy / RCSB / EBI]
3DA2; X-ray; 2.05 A; A/B=1-261.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 3CZV; -.
3D0N; -.
3DA2; -.
ModBase Q8N1Q1.
PTM databases
PhosphoSite Q8N1Q1; -.
2D gel databases
OGP Q8N1Q1; -.
Organism-specific databases
H-InvDB HIX0007627; -.
HGNC HGNC:14914; CA13.
GenAtlas CA13.
MIM 611436; gene. [NCBI / EBI]
PharmGKB PA134925234; -.
GeneCards Q8N1Q1.
Gene expression databases
ArrayExpress Q8N1Q1; -.
CleanEx HS_CA13; -.
GermOnline ENSG00000185015; Homo sapiens.
Ontologies
GO
GO:0004089; Molecular function: carbonate dehydratase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006730; Biological process: one-carbon compound metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001148; Euk_COanhd.
Graphical view of domain structure.
Gene3D G3DSA:3.10.200.10; Euk_COanhd; 1.
PANTHER PTHR18952; Euk_COanhd; 1.
Pfam PF00194; Carb_anhydrase; 1.
Pfam graphical view of domain structure.
ProDom PD000865; Euk_COanhd; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00162; ALPHA_CA_1; 1.
PS51144; ALPHA_CA_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8N1Q1.
Proteomic databases
PeptideAtlas Q8N1Q1; -.
Genome annotation databases
Ensembl ENSG00000185015; Homo sapiens. [Contig view]
GeneID 377677; -.
KEGG hsa:377677; -.
Phylogenomic databases
HOGENOM Q8N1Q1; -.
HOVERGEN Q8N1Q1; -.
Other
NextBio 100682; -.
SOURCE CA13; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Lyase; Metal-binding; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   262  262     Carbonic anhydrase 13. PRO_0000077440
METAL   95    95        Zinc; catalytic (By similarity). 
METAL   97    97        Zinc; catalytic (By similarity). 
METAL   120   120        Zinc; catalytic (By similarity). 
TURN   10    12  3      
HELIX   14    17  4      
TURN   18    20  3      
HELIX   22    25  4      
STRAND   26    28  3      
HELIX   36    38  3      
STRAND   48    51  4      
HELIX   54    56  3      
STRAND   57    62  6      
STRAND   64    71  8      
STRAND   74    82  9      
STRAND   89    98  10      
STRAND   107   110  4      
STRAND   116   125  10      
TURN   126   128  3      
HELIX   132   135  4      
STRAND   141   151  11      
TURN   156   158  3      
HELIX   159   162  4      
TURN   163   168  6      
STRAND   174   176  3      
HELIX   182   185  4      
STRAND   192   197  6      
STRAND   208   215  8      
STRAND   217   219  3      
HELIX   221   228  8      
STRAND   230   234  5      
Sequence information
Length: 262 AA [This is the length of the unprocessed precursor] Molecular weight: 29443 Da [This is the MW of the unprocessed precursor] CRC64: AE677F028ED729FE [This is a checksum on the sequence]
        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 

Q8N1Q1 in FASTA format

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