CAH9_MOUSE
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 03-AUG-2022, entry version 141.
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 GlyGen; Q8VHB5; 2 sites.
DR PhosphoSitePlus; Q8VHB5; -.
DR MaxQB; Q8VHB5; -.
DR PaxDb; Q8VHB5; -.
DR PRIDE; Q8VHB5; -.
DR ProteomicsDB; 265424; -. [Q8VHB5-1]
DR Antibodypedia; 3915; 1240 antibodies from 45 providers.
DR DNASU; 230099; -.
DR Ensembl; ENSMUST00000030183; ENSMUSP00000030183; ENSMUSG00000028463. [Q8VHB5-1]
DR GeneID; 230099; -.
DR KEGG; mmu:230099; -.
DR UCSC; uc008sqa.1; mouse. [Q8VHB5-1]
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; VQMRRQQ; -.
DR PhylomeDB; Q8VHB5; -.
DR TreeFam; TF316425; -.
DR Reactome; R-MMU-1475029; Reversible hydration of carbon dioxide.
DR BioGRID-ORCS; 230099; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q8VHB5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VHB5; protein.
DR Bgee; ENSMUSG00000028463; Expressed in epithelium of stomach and 92 other tissues.
DR ExpressionAtlas; Q8VHB5; baseline and differential.
DR Genevisible; Q8VHB5; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0016836; F:hydro-lyase activity; IBA:GO_Central.
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; -; 1.
DR InterPro; IPR018429; CA9.
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 PANTHER; PTHR18952:SF18; PTHR18952:SF18; 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 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
