CAH1_RAT
ID CAH1_RAT Reviewed; 261 AA.
AC B0BNN3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Carbonic anhydrase 1 {ECO:0000250|UniProtKB:P00915};
DE EC=4.2.1.1 {ECO:0000250|UniProtKB:P00915};
DE AltName: Full=Carbonate dehydratase I {ECO:0000250|UniProtKB:P00915};
DE AltName: Full=Carbonic anhydrase I {ECO:0000250|UniProtKB:P00915};
DE Short=CA-I {ECO:0000250|UniProtKB:P00915};
GN Name=Ca1 {ECO:0000250|UniProtKB:P00915};
GN Synonyms=Car1 {ECO:0000312|EMBL:AAI58889.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:EDM00961.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAI58889.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Liver {ECO:0000312|EMBL:AAI58889.1};
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19343716; DOI=10.1002/pmic.200800664;
RA Maurya D.K., Sundaram C.S., Bhargava P.;
RT "Proteome profile of the mature rat olfactory bulb.";
RL Proteomics 9:2593-2599(2009).
CC -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide.
CC {ECO:0000250|UniProtKB:P00915}.
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 Evidence={ECO:0000250|UniProtKB:P00915};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00915};
CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC {ECO:0000250|UniProtKB:P00915}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19343716}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000255}.
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DR EMBL; CH473961; EDM00961.1; -; Genomic_DNA.
DR EMBL; BC158888; AAI58889.1; -; mRNA.
DR RefSeq; NP_001101130.1; NM_001107660.1.
DR RefSeq; XP_006232173.1; XM_006232111.1.
DR RefSeq; XP_008759064.1; XM_008760842.1.
DR AlphaFoldDB; B0BNN3; -.
DR SMR; B0BNN3; -.
DR BioGRID; 259578; 2.
DR IntAct; B0BNN3; 1.
DR STRING; 10116.ENSRNOP00000014267; -.
DR iPTMnet; B0BNN3; -.
DR PhosphoSitePlus; B0BNN3; -.
DR PaxDb; B0BNN3; -.
DR PeptideAtlas; B0BNN3; -.
DR PRIDE; B0BNN3; -.
DR Ensembl; ENSRNOT00000014267; ENSRNOP00000014267; ENSRNOG00000010698.
DR GeneID; 310218; -.
DR KEGG; rno:310218; -.
DR UCSC; RGD:1309780; rat.
DR CTD; 12346; -.
DR RGD; 1309780; Ca1.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000161270; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; B0BNN3; -.
DR OMA; DYGSEHT; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; B0BNN3; -.
DR TreeFam; TF316425; -.
DR Reactome; R-RNO-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-RNO-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-RNO-1475029; Reversible hydration of carbon dioxide.
DR PRO; PR:B0BNN3; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Proteomes; UP000234681; Chromosome 2.
DR Bgee; ENSRNOG00000010698; Expressed in spleen and 13 other tissues.
DR Genevisible; B0BNN3; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004064; F:arylesterase activity; ISO:RGD.
DR GO; GO:0004089; F:carbonate dehydratase activity; ISO:RGD.
DR GO; GO:0016836; F:hydro-lyase activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR Gene3D; 3.10.200.10; -; 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 InterPro; IPR018442; Carbonic_anhydrase_CA1.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR PANTHER; PTHR18952:SF82; PTHR18952:SF82; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Lyase; Metal-binding; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00915"
FT CHAIN 2..261
FT /note="Carbonic anhydrase 1"
FT /evidence="ECO:0000250|UniProtKB:P00915"
FT /id="PRO_0000349120"
FT DOMAIN 4..261
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REGION 239..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0000250|UniProtKB:P00915"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00915"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00915"
FT BINDING 200..201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00915"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P00915"
SQ SEQUENCE 261 AA; 28300 MW; DEF19D7C46E92171 CRC64;
MASADWGYDS KNGPDQWSKL YPIANGNNQS PIDIKTSEAK HDSSLKPVSV SYNPATAKEI
VNVGHSFHVV FDDSSNQSVL KGGPLADSYR LTQFHFHWGN SNDHGSEHTV DGAKYSGELH
LVHWNSAKYS SAAEAISKAD GLAIIGVLMK VGPANPNLQK VLDALSSVKT KGKRAPFTNF
DPSSLLPSSL DYWTYFGSLT HPPLHESVTW VICKESISLS PEQLAQLRGL LSSAEGEPAV
PVLSNHRPPQ PLKGRTVRAS F
