ID M3XUB4_MUSPF Unreviewed; 322 AA.
AC M3XUB4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
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:ENSMPUP00000002664.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000002664.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000256|RuleBase:RU367011}.
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|RuleBase:RU367011};
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
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DR EMBL; AEYP01047477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01047478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01047479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01047480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01047481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01047482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01047483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3XUB4; -.
DR STRING; 9669.ENSMPUP00000002664; -.
DR Ensembl; ENSMPUT00000002719.1; ENSMPUP00000002664.1; ENSMPUG00000002692.1.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000156978; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; M3XUB4; -.
DR OMA; CAITKVK; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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:SF25; CARBONIC ANHYDRASE 5B, MITOCHONDRIAL; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT TRANSMEM 220..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..301
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
SQ SEQUENCE 322 AA; 37128 MW; 6569698AF2EFE318 CRC64;
MVVMSSLRVI LQASPCKSLW RRFQTPRFVP ARPCSLYTCT YKSRNRALHP LWETVDLVPG
GERQSPINIR WRDSVYDPGL KPLTISYDPT TCLHVWNNGY SFLVEFEDST DKSVIEGGPL
EHNYRLKQFH FHWGAIDAWG SEHTVDSKCY PAELHLVHWN AVRFENFEDA AQEEHGLAVI
GVFLKLGKHH KELQKLVDTL PSIKHKEYIL KKGFLKPNGI IVYLPFCSSF FFFAGGIPLP
VKKVTPCTAF PTMPSEVPRI KDELEQFRTL LFTSEGEKEK RMVDNFRPLQ PLMNRTVRSS
FRHDYVLNIQ AKPQPSTSQV IP
//
