CAH14_MOUSE
ID CAH14_MOUSE Reviewed; 337 AA.
AC Q9WVT6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Carbonic anhydrase 14;
DE EC=4.2.1.1 {ECO:0000305|PubMed:14660577};
DE AltName: Full=Carbonate dehydratase XIV;
DE AltName: Full=Carbonic anhydrase XIV {ECO:0000303|PubMed:14660577};
DE Short=CA-XIV {ECO:0000303|PubMed:14660577};
DE Flags: Precursor;
GN Name=Ca14 {ECO:0000312|MGI:MGI:1344341}; Synonyms=Car14, Catm;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=10336468; DOI=10.1074/jbc.274.22.15701;
RA Mori K., Ogawa Y., Ebihara K., Tamura N., Tashiro K., Kuwahara T.,
RA Mukoyama M., Sugawara A., Ozaki S., Tanaka I., Nakao K.;
RT "Isolation and characterization of CA XIV, a novel membrane-bound carbonic
RT anhydrase from mouse kidney.";
RL J. Biol. Chem. 274:15701-15705(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
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 [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 18-278 ALONE AND IN COMPLEX WITH
RP ACETAZOLAMIDE, DISULFIDE BOND, ZINC-BINDING SITES, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, GLYCOSYLATION AT ASN-213, AND COFACTOR.
RX PubMed=14660577; DOI=10.1074/jbc.m310809200;
RA Whittington D.A., Grubb J.H., Waheed A., Shah G.N., Sly W.S.,
RA Christianson D.W.;
RT "Expression, assay, and structure of the extracellular domain of murine
RT carbonic anhydrase XIV: implications for selective inhibition of membrane-
RT associated isozymes.";
RL J. Biol. Chem. 279:7223-7228(2004).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000305|PubMed:14660577}.
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:0000305|PubMed:14660577};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:14660577};
CC -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC {ECO:0000269|PubMed:14660577}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Most abundant in the kidney and heart, followed by
CC the skeletal muscle, brain, lung and liver.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AB005450; BAA78709.1; -; mRNA.
DR EMBL; BC046995; AAH46995.1; -; mRNA.
DR CCDS; CCDS17625.1; -.
DR RefSeq; NP_035927.1; NM_011797.2.
DR PDB; 1RJ5; X-ray; 2.81 A; A/B=18-278.
DR PDB; 1RJ6; X-ray; 2.90 A; A/B=18-278.
DR PDBsum; 1RJ5; -.
DR PDBsum; 1RJ6; -.
DR AlphaFoldDB; Q9WVT6; -.
DR SMR; Q9WVT6; -.
DR STRING; 10090.ENSMUSP00000036983; -.
DR GlyConnect; 2180; 1 N-Linked glycan (1 site).
DR GlyGen; Q9WVT6; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q9WVT6; -.
DR PhosphoSitePlus; Q9WVT6; -.
DR jPOST; Q9WVT6; -.
DR MaxQB; Q9WVT6; -.
DR PaxDb; Q9WVT6; -.
DR PeptideAtlas; Q9WVT6; -.
DR PRIDE; Q9WVT6; -.
DR ProteomicsDB; 265275; -.
DR Antibodypedia; 2374; 211 antibodies from 29 providers.
DR DNASU; 23831; -.
DR Ensembl; ENSMUST00000036181; ENSMUSP00000036983; ENSMUSG00000038526.
DR GeneID; 23831; -.
DR KEGG; mmu:23831; -.
DR UCSC; uc008qls.1; mouse.
DR CTD; 23831; -.
DR MGI; MGI:1344341; Car14.
DR VEuPathDB; HostDB:ENSMUSG00000038526; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000156893; -.
DR HOGENOM; CLU_039326_1_2_1; -.
DR InParanoid; Q9WVT6; -.
DR OMA; HGQEHWP; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; Q9WVT6; -.
DR TreeFam; TF316425; -.
DR BRENDA; 4.2.1.1; 3474.
DR Reactome; R-MMU-1475029; Reversible hydration of carbon dioxide.
DR BioGRID-ORCS; 23831; 1 hit in 72 CRISPR screens.
DR EvolutionaryTrace; Q9WVT6; -.
DR PRO; PR:Q9WVT6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9WVT6; protein.
DR Bgee; ENSMUSG00000038526; Expressed in pigmented layer of retina and 174 other tissues.
DR ExpressionAtlas; Q9WVT6; baseline and differential.
DR Genevisible; Q9WVT6; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:MGI.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015670; P:carbon dioxide transport; IC:MGI.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0006885; P:regulation of pH; IC:MGI.
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; IPR018431; Carbonic_anhydrase_CA14.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR PANTHER; PTHR18952:SF84; PTHR18952:SF84; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Lyase; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Zinc.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..337
FT /note="Carbonic anhydrase 14"
FT /id="PRO_0000004252"
FT TOPO_DOM 16..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..278
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 84
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14660577"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14660577"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:14660577"
FT BINDING 217..218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX7"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14660577"
FT DISULFID 40..221
FT /evidence="ECO:0000269|PubMed:14660577"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1RJ5"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1RJ5"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1RJ5"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1RJ5"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:1RJ5"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1RJ5"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1RJ5"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1RJ5"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1RJ5"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1RJ5"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:1RJ5"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:1RJ5"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:1RJ5"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1RJ5"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:1RJ5"
FT STRAND 157..166
FT /evidence="ECO:0007829|PDB:1RJ5"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:1RJ5"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:1RJ5"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:1RJ5"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1RJ5"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:1RJ5"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:1RJ5"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1RJ5"
FT HELIX 238..245
FT /evidence="ECO:0007829|PDB:1RJ5"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:1RJ5"
SQ SEQUENCE 337 AA; 37505 MW; 32F02F4DB78AC0C9 CRC64;
MLFFALLLKV TWILAADGGH HWTYEGPHGQ DHWPTSYPEC GGDAQSPINI QTDSVIFDPD
LPAVQPHGYD QLGTEPLDLH NNGHTVQLSL PPTLHLGGLP RKYTAAQLHL HWGQRGSLEG
SEHQINSEAT AAELHVVHYD SQSYSSLSEA AQKPQGLAVL GILIEVGETE NPAYDHILSR
LHEIRYKDQK TSVPPFSVRE LFPQQLEQFF RYNGSLTTPP CYQSVLWTVF NRRAQISMGQ
LEKLQETLSS TEEDPSEPLV QNYRVPQPLN QRTIFASFIQ AGPLYTTGEM LGLGVGILAG
CLCLLLAVYF IAQKIRKKRL GNRKSVVFTS ARATTEA
