ID   CAH9_MOUSE              Reviewed;         437 AA.
AC   Q8VHB5; Q8K1G1; Q8VDE4;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Carbonic anhydrase 9;
DE            EC=4.2.1.1 {ECO:0000250|UniProtKB:Q16790};
DE   AltName: Full=Carbonate dehydratase IX;
DE   AltName: Full=Carbonic anhydrase IX;
DE            Short=CA-IX;
DE            Short=CAIX;
DE   AltName: Full=Membrane antigen MN homolog;
DE   Flags: Precursor;
GN   Name=Ca9; Synonyms=Car9;
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 [GENOMIC DNA] (ISOFORM 1).
RC   STRAIN=129/Ola;
RX   PubMed=14604546; DOI=10.1016/j.jim.2003.08.011;
RA   Zat'ovicova M., Tarabkova K., Svastova E., Gibadulinova A., Mucha V.,
RA   Jakubickova L., Biesova Z., Rafajova M., Ortova Gut M.O., Parkkila S.,
RA   Parkkila A.-K., Waheed A., Sly W.S., Horak I., Pastorek J., Pastorekova S.;
RT   "Monoclonal antibodies generated in carbonic anhydrase IX-deficient mice
RT   recognize different domains of tumour-associated hypoxia-induced carbonic
RT   anhydrase IX.";
RL   J. Immunol. Methods 282:117-134(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Ortova M.;
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=ICR; TISSUE=Small intestine;
RA   Wang Y.P., Yoshikawa K., Kozaki K., Miyaishi O., Nakagawa A., Muramatsu H.,
RA   Kawada Y., Uchida K., Nishikawa N., Saga S.;
RT   "Alternative spliced mRNA coding for MN/CA9.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion between carbon dioxide and
CC       water and the dissociated ions of carbonic acid (i.e. bicarbonate and
CC       hydrogen ions). {ECO:0000250|UniProtKB:Q16790}.
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:Q16790};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10749;
CC         Evidence={ECO:0000250|UniProtKB:Q16790};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10750;
CC         Evidence={ECO:0000250|UniProtKB:Q16790};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q16790};
CC   -!- ACTIVITY REGULATION: Inhibited by acetazolamide.
CC       {ECO:0000250|UniProtKB:Q16790}.
CC   -!- SUBUNIT: Forms oligomers linked by disulfide bonds.
CC       {ECO:0000250|UniProtKB:Q16790}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q16790}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:Q16790}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q16790}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:Q16790}. Cell projection, microvillus membrane
CC       {ECO:0000250|UniProtKB:Q16790}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:Q16790}. Note=Found on the surface microvilli
CC       and in the nucleus, particularly in nucleolus.
CC       {ECO:0000250|UniProtKB:Q16790}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VHB5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VHB5-2; Sequence=VSP_007409, VSP_007410;
CC   -!- PTM: Asn-325 bears high-mannose type glycan structures.
CC       {ECO:0000250|UniProtKB:Q16790}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; AY049077; AAL14193.1; -; Genomic_DNA.
DR   EMBL; AJ245857; CAC80975.1; -; mRNA.
DR   EMBL; AB086322; BAC00816.1; -; mRNA.
DR   CCDS; CCDS18099.1; -. [Q8VHB5-1]
DR   RefSeq; NP_647466.2; NM_139305.2. [Q8VHB5-1]
DR   AlphaFoldDB; Q8VHB5; -.
DR   SMR; Q8VHB5; -.
DR   STRING; 10090.ENSMUSP00000030183; -.
DR   GlyCosmos; Q8VHB5; 2 sites, No reported glycans.
DR   GlyGen; Q8VHB5; 2 sites.
DR   PhosphoSitePlus; Q8VHB5; -.
DR   MaxQB; Q8VHB5; -.
DR   PaxDb; 10090-ENSMUSP00000030183; -.
DR   ProteomicsDB; 265424; -. [Q8VHB5-1]
DR   ProteomicsDB; 265425; -. [Q8VHB5-2]
DR   Antibodypedia; 3915; 1491 antibodies from 46 providers.
DR   DNASU; 230099; -.
DR   Ensembl; ENSMUST00000030183.10; ENSMUSP00000030183.4; ENSMUSG00000028463.15. [Q8VHB5-1]
DR   GeneID; 230099; -.
DR   KEGG; mmu:230099; -.
DR   UCSC; uc008sqa.1; mouse. [Q8VHB5-1]
DR   AGR; MGI:2447188; -.
DR   CTD; 230099; -.
DR   MGI; MGI:2447188; Car9.
DR   VEuPathDB; HostDB:ENSMUSG00000028463; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   GeneTree; ENSGT00940000161646; -.
DR   HOGENOM; CLU_039326_1_1_1; -.
DR   InParanoid; Q8VHB5; -.
DR   OMA; MNFRATQ; -.
DR   OrthoDB; 49814at2759; -.
DR   PhylomeDB; Q8VHB5; -.
DR   TreeFam; TF316425; -.
DR   Reactome; R-MMU-1475029; Reversible hydration of carbon dioxide.
DR   BioGRID-ORCS; 230099; 3 hits in 79 CRISPR screens.
DR   PRO; PR:Q8VHB5; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q8VHB5; Protein.
DR   Bgee; ENSMUSG00000028463; Expressed in epithelium of stomach and 94 other cell types or tissues.
DR   ExpressionAtlas; Q8VHB5; baseline and differential.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004089; F:carbonate dehydratase activity; ISS:UniProtKB.
DR   GO; GO:0140677; F:molecular function activator activity; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI.
DR   GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR   GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR   GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0046903; P:secretion; IMP:MGI.
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:SF18; CARBONIC ANHYDRASE 9; 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.
DR   Genevisible; Q8VHB5; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Cell projection; Disulfide bond;
KW   Glycoprotein; Lyase; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..437
FT                   /note="Carbonic anhydrase 9"
FT                   /id="PRO_0000004244"
FT   TOPO_DOM        32..390
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        391..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        412..437
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          118..369
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   REGION          32..95
FT                   /note="Proteoglycan-like (PG)"
FT                   /evidence="ECO:0000250"
FT   REGION          34..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..390
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16790"
FT   COMPBIAS        57..83
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        179
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   BINDING         205
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16790"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16790"
FT   BINDING         230
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16790"
FT   BINDING         311..312
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00918"
FT   MOD_RES         427
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16790"
FT   CARBOHYD        98
FT                   /note="O-linked (GlcNAc...) threonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16790"
FT   CARBOHYD        325
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16790"
FT   DISULFID        135..315
FT                   /evidence="ECO:0000250|UniProtKB:Q16790"
FT   DISULFID        153
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:Q16790"
FT   VAR_SEQ         282
FT                   /note="G -> V (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_007409"
FT   VAR_SEQ         283..437
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_007410"
SQ   SEQUENCE   437 AA;  47265 MW;  88F23380DCD35344 CRC64;
     MASLGPSPWA PLSTPAPTAQ LLLFLLLQVS AQPQGLSGMQ GEPSLGDSSS GEDELGVDVL
     PSEEDAPEEA DPPDGEDPPE VNSEDRMEES LGLEDLSTPE APEHSQGSHG DEKGGGHSHW
     SYGGTLLWPQ VSPACAGRFQ SPVDIRLERT AFCRTLQPLE LLGYELQPLP ELSLSNNGHT
     VQLTLPPGLK MALGPGQEYR ALQLHLHWGT SDHPGSEHTV NGHRFPAEIH VVHLSTAFSE
     LHEALGRPGG LAVLAAFLQE SPEENSAYEQ LLSHLEEISE EGSKIEIPGL DVSALLPSDL
     SRYYRYEGSL TTPPCSQGVI WTVFNETVKL SAKQLHTLSV SLWGPRDSRL QLNFRATQPL
     NGRTIEASFP AAEDSSPEPV HVNSCFTAGD ILALVFGLLF AVTSIAFLLQ LRRQHRHRSG
     TKDRVSYSPA EMTETGA
//