UniProt: A0A3P9NPT1

Database: UniProt
Entry: A0A3P9NPT1_POERE

LinkDB:  A0A3P9NPT1_POERE 
Original site:  A0A3P9NPT1_POERE

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (9)   
   InterPro (5)   
   Pfam (1)   
   PROSITE (2)   
   SMART (1)   
All databases (17)   

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ID   A0A3P9NPT1_POERE        Unreviewed;       274 AA.
AC   A0A3P9NPT1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE            EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000011571.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000011571.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000011571.1};
RG   Ensembl;
RL   Submitted (SEP-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:ARBA00033630};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10749;
CC         Evidence={ECO:0000256|ARBA:ARBA00033630};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10750;
CC         Evidence={ECO:0000256|ARBA:ARBA00033630};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU367011};
CC   -!- SUBUNIT: Interacts with SLC4A4. {ECO:0000256|ARBA:ARBA00011736}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004589}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
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DR   AlphaFoldDB; A0A3P9NPT1; -.
DR   Ensembl; ENSPRET00000011700.1; ENSPREP00000011571.1; ENSPREG00000007362.1.
DR   GeneTree; ENSGT00940000155690; -.
DR   OMA; TGSGDWC; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000007362; Expressed in head.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of 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   CDD; cd03117; alpha_CA_IV_XV_like; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR   InterPro; IPR041874; CA4/CA15.
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:SF95; CARBONIC ANHYDRASE 4; 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   Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW   GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Lyase {ECO:0000256|RuleBase:RU367011};
KW   Membrane {ECO:0000256|ARBA:ARBA00022622};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU367011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT   DOMAIN          1..257
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
SQ   SEQUENCE   274 AA;  30267 MW;  35E994A1084306E6 CRC64;
     YYSQSTCDHP CNVPEKWAGG NVDCGGKSQS PINIVTRKTV KDERLTPIEF KNYQQTFKNS
     LTNNGHSVKV NIPITSTISG GDLSTTYKAV QFHLHWGKDG GPGSEHTIDG EQYPMELHIV
     HMKSSYADLT TALRDPNGVA VLGFFYEVSK SPNRMYDTII NGVQSVASKS SFSLPSISLA
     QLIPPEQKLT SYYRYRGSLT TPPCSESVVW TVFETPIPLS MDQMKAFSTV QFYDGTSMVN
     NFRPVQPLNG RLVYRSAGAT LWVSSLPMVY GSAP
//

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