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   24-JAN-2024, entry version 169.
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   GlyCosmos; Q9WVT6; 1 site, 1 glycan.
DR   GlyGen; Q9WVT6; 1 site, 1 N-linked glycan (1 site).
DR   iPTMnet; Q9WVT6; -.
DR   PhosphoSitePlus; Q9WVT6; -.
DR   SwissPalm; Q9WVT6; -.
DR   jPOST; Q9WVT6; -.
DR   MaxQB; Q9WVT6; -.
DR   PaxDb; 10090-ENSMUSP00000036983; -.
DR   PeptideAtlas; Q9WVT6; -.
DR   ProteomicsDB; 265275; -.
DR   Antibodypedia; 2374; 228 antibodies from 29 providers.
DR   DNASU; 23831; -.
DR   Ensembl; ENSMUST00000036181.15; ENSMUSP00000036983.9; ENSMUSG00000038526.15.
DR   GeneID; 23831; -.
DR   KEGG; mmu:23831; -.
DR   UCSC; uc008qls.1; mouse.
DR   AGR; MGI:1344341; -.
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; HKNTRYA; -.
DR   OrthoDB; 49814at2759; -.
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 77 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 177 other cell types or tissues.
DR   ExpressionAtlas; Q9WVT6; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IDA:MGI.
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   CDD; cd03126; alpha_CA_XII_XIV; 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   PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR18952:SF84; CARBONIC ANHYDRASE 14; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
DR   Genevisible; Q9WVT6; MM.
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
//