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Database: UniProt
Entry: M3Y4R6_MUSPF
LinkDB: M3Y4R6_MUSPF
Original site: M3Y4R6_MUSPF 
ID   M3Y4R6_MUSPF            Unreviewed;       319 AA.
AC   M3Y4R6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE            EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN   Name=CA6 {ECO:0000313|Ensembl:ENSMPUP00000006317.1,
GN   ECO:0000313|RefSeq:XP_004768673.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000006317.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000006317.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_004768673.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_004768673.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide. Its role in saliva is
CC       unknown. {ECO:0000256|ARBA:ARBA00025355}.
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:0000256|ARBA:ARBA00000943,
CC         ECO:0000256|RuleBase:RU367011};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU367011};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
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DR   EMBL; AEYP01070413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01070414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01070415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004768673.1; XM_004768616.3.
DR   STRING; 9669.ENSMPUP00000006317; -.
DR   Ensembl; ENSMPUT00000006426.1; ENSMPUP00000006317.1; ENSMPUG00000006371.1.
DR   GeneID; 101680019; -.
DR   KEGG; mpuf:101680019; -.
DR   CTD; 765; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   GeneTree; ENSGT00940000160409; -.
DR   HOGENOM; CLU_039326_1_0_1; -.
DR   OMA; PPTMRMT; -.
DR   OrthoDB; 49814at2759; -.
DR   Proteomes; UP000000715; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0001580; P:detection of chemical stimulus involved in sensory perception of bitter taste; IEA:Ensembl.
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:SF110; CARBONIC ANHYDRASE 6; 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.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|RuleBase:RU367011};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW   Signal {ECO:0000256|RuleBase:RU367011};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT   CHAIN           18..319
FT                   /note="Carbonic anhydrase"
FT                   /evidence="ECO:0000256|RuleBase:RU367011"
FT                   /id="PRO_5041007754"
FT   DOMAIN          21..278
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
SQ   SEQUENCE   319 AA;  36723 MW;  BEA9D956F0A68061 CRC64;
     MMALVALVAL LFLGAQAQHG SEWSYSEGAL DELHWPREYP TCGGRRQSPI NLERRKVQYN
     PSLKALNLTG YGVQEGEFHM INNGHTVQIS LPPTMRMTAP DGTQYTAEQM HFHWGGASSE
     IRGSEHTIDG IRFVAEIHIV HYNSKYESYD RAQSEPDGLA VLAALIEVKD HGENTYYSNF
     IAHLNNIQYP GQSTVLSDLD ILHMLPGDIQ HYYSYNGSLT TPPCTENVHW FVLAHHVPLS
     RAQIWKLENS ILDHHNKTLH NDYRSIQPLN NRVVETNLMN FPHLPYNLGP EFQLYIKKLN
     KWFEFSRRLT EKRNKKDKF
//
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