CAH5A_RAT
ID CAH5A_RAT Reviewed; 304 AA.
AC P43165;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Carbonic anhydrase 5A, mitochondrial {ECO:0000305|PubMed:7937950};
DE EC=4.2.1.1 {ECO:0000269|PubMed:7937950};
DE AltName: Full=Carbonate dehydratase VA;
DE AltName: Full=Carbonic anhydrase VA;
DE Short=CA-VA;
DE Flags: Precursor;
GN Name=Ca5a {ECO:0000312|RGD:2243}; Synonyms=Ca5;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-46, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7937950; DOI=10.1073/pnas.91.22.10330;
RA Nagao Y., Srinivasan M., Platero J.S., Svendrowski M., Waheed A., Sly W.S.;
RT "Mitochondrial carbonic anhydrase (isozyme V) in mouse and rat: cDNA
RT cloning, expression, subcellular localization, processing, and tissue
RT distribution.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:10330-10334(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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).
CC -!- FUNCTION: Mitochondrial carbonic anhydrase that catalyzes the
CC reversible conversion of carbon dioxide to bicarbonate/HCO3
CC (PubMed:7937950). Mitochondria are impermeable to HCO3, and thus this
CC intramitochondrial carbonic anhydrase is pivotal in providing HCO3 for
CC multiple mitochondrial enzymes that catalyze the formation of essential
CC metabolites of intermediary metabolism in the urea and Krebs cycles (By
CC similarity). {ECO:0000250|UniProtKB:P35218,
CC ECO:0000269|PubMed:7937950}.
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; Evidence={ECO:0000269|PubMed:7937950};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10749;
CC Evidence={ECO:0000305|PubMed:7937950};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10750;
CC Evidence={ECO:0000305|PubMed:7937950};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P23589};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7937950}.
CC -!- TISSUE SPECIFICITY: High in liver, also detected in heart, lung,
CC kidney, spleen and intestine. {ECO:0000269|PubMed:7937950}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; U12268; AAA50832.1; -; mRNA.
DR EMBL; BC088147; AAH88147.1; -; mRNA.
DR PIR; I59261; I59261.
DR RefSeq; NP_062166.1; NM_019293.3.
DR AlphaFoldDB; P43165; -.
DR SMR; P43165; -.
DR STRING; 10116.ENSRNOP00000025848; -.
DR PaxDb; P43165; -.
DR Ensembl; ENSRNOT00000025848; ENSRNOP00000025848; ENSRNOG00000019098.
DR GeneID; 54233; -.
DR KEGG; rno:54233; -.
DR UCSC; RGD:2243; rat.
DR CTD; 763; -.
DR RGD; 2243; Ca5a.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000162066; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; P43165; -.
DR OMA; NAWKTSA; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; P43165; -.
DR TreeFam; TF316425; -.
DR Reactome; R-RNO-1475029; Reversible hydration of carbon dioxide.
DR PRO; PR:P43165; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000019098; Expressed in liver and 2 other tissues.
DR Genevisible; P43165; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:RGD.
DR GO; GO:0016836; F:hydro-lyase 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 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 PANTHER; PTHR18952; PTHR18952; 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 Direct protein sequencing; Lyase; Metal-binding; Mitochondrion;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:7937950"
FT CHAIN 35..304
FT /note="Carbonic anhydrase 5A, mitochondrial"
FT /id="PRO_0000004236"
FT DOMAIN 35..295
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P23589"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P23589"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P23589"
SQ SEQUENCE 304 AA; 34499 MW; C997805D690F95D0 CRC64;
MLRAKMLGRG PYKPLAILRH MGPLCATRPQ HWRFQHSYAE KHSNCARHPL WTGPVSSPGG
TQQSPINIQW TDSVYDPKLA PLRVSYDAAS CRYLWNTGYF FQVEFDDSCE ESGISGGPLG
NHYRLKQFHF HWGATDEWGS EHMVDGHAYP AELHLVHWNS MKYENYKKAT TGENGLAVIG
VFLKLGAHHE ALQRLVDILP EVRHKDTQVT MGPFDPSCLL PACRDYWTYP GSLTTPPLAE
SVTWIVHKMP IEVSPSQLST FRTLLFSGRG EDEEVMVNNF RPLQPLRGRN VRSSFQVPRV
GTKS
