ID CAH13_HUMAN Reviewed; 262 AA.
AC Q8N1Q1;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 172.
DE RecName: Full=Carbonic anhydrase 13;
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase XIII;
DE AltName: Full=Carbonic anhydrase XIII;
DE Short=CA-XIII;
GN Name=CA13;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP CHARACTERIZATION, AND TISSUE SPECIFICITY.
RX PubMed=14600151; DOI=10.1074/jbc.m308984200;
RA Lehtonen J., Shen B., Vihinen M., Casini A., Scozzafava A., Supuran C.T.,
RA Parkkila A.-K., Saarnio J., Kivelae A.J., Waheed A., Sly W.S., Parkkila S.;
RT "Characterization of CA XIII, a novel member of the carbonic anhydrase
RT isozyme family.";
RL J. Biol. Chem. 279:2719-2727(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH ZINC AND THE
RP INHIBITOR ACETAZOLAMIDE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND COFACTOR.
RX PubMed=18618712; DOI=10.1002/prot.22144;
RA Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A.,
RA Pedone C., Scozzafava A., Supuran C.T., De Simone G.;
RT "Crystal structure of human carbonic anhydrase XIII and its complex with
RT the inhibitor acetazolamide.";
RL Proteins 74:164-175(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-261 IN COMPLEX WITH INHIBITOR.
RG Structural genomics consortium (SGC);
RT "X-ray structure of human carbonic anhydrase 13 in complex with
RT inhibitor.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:18618712};
CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC {ECO:0000269|PubMed:18618712}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.8 mM for CO(2) {ECO:0000269|PubMed:18618712};
CC -!- INTERACTION:
CC Q8N1Q1; Q8N4Y2-3: CRACR2B; NbExp=3; IntAct=EBI-11982647, EBI-11982645;
CC Q8N1Q1; Q6UUV7: CRTC3; NbExp=3; IntAct=EBI-11982647, EBI-3453588;
CC -!- TISSUE SPECIFICITY: Expressed in thymus, small intestine, spleen,
CC prostate, ovary, colon and testis. {ECO:0000269|PubMed:14600151}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AK095314; BAC04528.1; -; mRNA.
DR EMBL; BC052602; AAH52602.1; -; mRNA.
DR CCDS; CCDS6236.1; -.
DR RefSeq; NP_940986.1; NM_198584.2.
DR PDB; 3CZV; X-ray; 2.00 A; A/B=1-262.
DR PDB; 3D0N; X-ray; 1.55 A; A/B=1-262.
DR PDB; 3DA2; X-ray; 2.05 A; A/B=1-261.
DR PDB; 4HU1; X-ray; 1.95 A; A/B=1-262.
DR PDB; 4KNM; X-ray; 1.90 A; A/B=1-262.
DR PDB; 4KNN; X-ray; 1.40 A; A/B=1-262.
DR PDB; 4QIZ; X-ray; 1.55 A; A/B=1-262.
DR PDB; 4QJP; X-ray; 1.62 A; A/B=1-262.
DR PDB; 4QJX; X-ray; 1.95 A; A=1-262.
DR PDB; 4QSJ; X-ray; 1.70 A; A/B=1-262.
DR PDB; 5E2N; X-ray; 1.53 A; A/B=1-262.
DR PDB; 5LLA; X-ray; 1.50 A; A/B=1-262.
DR PDB; 5LLN; X-ray; 1.60 A; A/B=1-262.
DR PDB; 5OGJ; X-ray; 1.06 A; A/B=1-262.
DR PDB; 5OHH; X-ray; 1.42 A; A/B=1-262.
DR PDB; 6G5U; X-ray; 1.70 A; A/B=1-262.
DR PDBsum; 3CZV; -.
DR PDBsum; 3D0N; -.
DR PDBsum; 3DA2; -.
DR PDBsum; 4HU1; -.
DR PDBsum; 4KNM; -.
DR PDBsum; 4KNN; -.
DR PDBsum; 4QIZ; -.
DR PDBsum; 4QJP; -.
DR PDBsum; 4QJX; -.
DR PDBsum; 4QSJ; -.
DR PDBsum; 5E2N; -.
DR PDBsum; 5LLA; -.
DR PDBsum; 5LLN; -.
DR PDBsum; 5OGJ; -.
DR PDBsum; 5OHH; -.
DR PDBsum; 6G5U; -.
DR AlphaFoldDB; Q8N1Q1; -.
DR SMR; Q8N1Q1; -.
DR BioGRID; 132020; 6.
DR IntAct; Q8N1Q1; 2.
DR STRING; 9606.ENSP00000318912; -.
DR BindingDB; Q8N1Q1; -.
DR ChEMBL; CHEMBL3912; -.
DR DrugBank; DB00562; Benzthiazide.
DR DrugBank; DB00606; Cyclothiazide.
DR DrugBank; DB07115; N-(4-chlorobenzyl)-N-methylbenzene-1,4-disulfonamide.
DR DrugBank; DB00909; Zonisamide.
DR DrugCentral; Q8N1Q1; -.
DR iPTMnet; Q8N1Q1; -.
DR PhosphoSitePlus; Q8N1Q1; -.
DR BioMuta; CA13; -.
DR DMDM; 30580350; -.
DR OGP; Q8N1Q1; -.
DR EPD; Q8N1Q1; -.
DR jPOST; Q8N1Q1; -.
DR MassIVE; Q8N1Q1; -.
DR MaxQB; Q8N1Q1; -.
DR PaxDb; 9606-ENSP00000318912; -.
DR PeptideAtlas; Q8N1Q1; -.
DR ProteomicsDB; 71627; -.
DR Pumba; Q8N1Q1; -.
DR Antibodypedia; 12589; 223 antibodies from 29 providers.
DR DNASU; 377677; -.
DR Ensembl; ENST00000321764.4; ENSP00000318912.3; ENSG00000185015.8.
DR GeneID; 377677; -.
DR KEGG; hsa:377677; -.
DR MANE-Select; ENST00000321764.4; ENSP00000318912.3; NM_198584.3; NP_940986.1.
DR UCSC; uc003ydg.3; human.
DR AGR; HGNC:14914; -.
DR CTD; 377677; -.
DR DisGeNET; 377677; -.
DR GeneCards; CA13; -.
DR HGNC; HGNC:14914; CA13.
DR HPA; ENSG00000185015; Tissue enhanced (intestine).
DR MIM; 611436; gene.
DR neXtProt; NX_Q8N1Q1; -.
DR OpenTargets; ENSG00000185015; -.
DR PharmGKB; PA134891311; -.
DR VEuPathDB; HostDB:ENSG00000185015; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000160659; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; Q8N1Q1; -.
DR OMA; HDIEVKW; -.
DR OrthoDB; 49814at2759; -.
DR PhylomeDB; Q8N1Q1; -.
DR TreeFam; TF316425; -.
DR PathwayCommons; Q8N1Q1; -.
DR Reactome; R-HSA-1475029; Reversible hydration of carbon dioxide.
DR SABIO-RK; Q8N1Q1; -.
DR SignaLink; Q8N1Q1; -.
DR BioGRID-ORCS; 377677; 8 hits in 1161 CRISPR screens.
DR ChiTaRS; CA13; human.
DR EvolutionaryTrace; Q8N1Q1; -.
DR GenomeRNAi; 377677; -.
DR Pharos; Q8N1Q1; Tclin.
DR PRO; PR:Q8N1Q1; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q8N1Q1; Protein.
DR Bgee; ENSG00000185015; Expressed in jejunal mucosa and 176 other cell types or tissues.
DR Genevisible; Q8N1Q1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0004089; F:carbonate dehydratase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR CDD; cd03119; alpha_CA_I_II_III_XIII; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF81; CARBONIC ANHYDRASE 13; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..262
FT /note="Carbonic anhydrase 13"
FT /id="PRO_0000077440"
FT DOMAIN 4..261
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 65
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18618712"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18618712"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:18618712"
FT BINDING 200..201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT VARIANT 68
FT /note="N -> S (in dbSNP:rs4740046)"
FT /id="VAR_059207"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:5OGJ"
FT HELIX 14..19
FT /evidence="ECO:0007829|PDB:5OGJ"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5OGJ"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:5OGJ"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:5OGJ"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:5OGJ"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 141..151
FT /evidence="ECO:0007829|PDB:5OGJ"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:5OGJ"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:5OGJ"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:5OGJ"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5OGJ"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:5OGJ"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:5OGJ"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:5OGJ"
SQ SEQUENCE 262 AA; 29443 MW; AE677F028ED729FE CRC64;
MSRLSWGYRE HNGPIHWKEF FPIADGDQQS PIEIKTKEVK YDSSLRPLSI KYDPSSAKII
SNSGHSFNVD FDDTENKSVL RGGPLTGSYR LRQVHLHWGS ADDHGSEHIV DGVSYAAELH
VVHWNSDKYP SFVEAAHEPD GLAVLGVFLQ IGEPNSQLQK ITDTLDSIKE KGKQTRFTNF
DLLSLLPPSW DYWTYPGSLT VPPLLESVTW IVLKQPINIS SQQLAKFRSL LCTAEGEAAA
FLVSNHRPPQ PLKGRKVRAS FH
//
