ID F6YS25_HORSE Unreviewed; 349 AA.
AC F6YS25;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 3.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Carbonic anhydrase {ECO:0000256|RuleBase:RU367011};
DE EC=4.2.1.1 {ECO:0000256|RuleBase:RU367011};
GN Name=CA2 {ECO:0000313|Ensembl:ENSECAP00000014302.3,
GN ECO:0000313|VGNC:VGNC:15963};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000014302.3, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000014302.3, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000014302.3,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000014302.3}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000014302.3};
RG Ensembl;
RL Submitted (NOV-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 -!- CATALYTIC ACTIVITY:
CC Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69;
CC Evidence={ECO:0000256|ARBA:ARBA00036058};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU367011};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00010718, ECO:0000256|RuleBase:RU367011}.
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DR AlphaFoldDB; F6YS25; -.
DR Ensembl; ENSECAT00000017593.4; ENSECAP00000014302.3; ENSECAG00000016228.4.
DR VGNC; VGNC:15963; CA2.
DR GeneTree; ENSGT00940000160385; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR OMA; WADSFPI; -.
DR OrthoDB; 49814at2759; -.
DR TreeFam; TF316425; -.
DR Proteomes; UP000002281; Chromosome 9.
DR Bgee; ENSECAG00000016228; Expressed in muscle tissue and 24 other cell types or tissues.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004064; F:arylesterase activity; IEA:Ensembl.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0018820; F:cyanamide hydratase activity; IEA:RHEA.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; IEA:Ensembl.
DR GO; GO:0044070; P:regulation of monoatomic anion transport; 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:SF120; CARBONIC ANHYDRASE 2; 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 1: Evidence at protein level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Lyase {ECO:0000256|RuleBase:RU367011};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367011};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F6YS25};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367011}.
FT DOMAIN 91..348
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..51
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 38176 MW; 96DD7A98E54B71A8 CRC64;
PRPRGAHGGR GAPEPAQRPP RGRPPRPRAS PGTSPRRSGP PGPPPSGRPR APSWREPIKA
GDGATRGHTV QAPDSRRYTG ANSCRARTSA QPCPITGDTA STTHWHKDFP IAKGQRQSPV
DIDTKAAVHD AALKPLAVHY EQATSRRIVN NGHSFNVEFD DSQDKAVLQG GPLTGTYRLI
QFHFHWGSSD GQGSEHTVDK KKYAAELHLV HWNTKYGDFG KAVQQPDGLA VVGVFLKVGG
AKPGLQKVLD VLDSIKTKGK SADFTNFDPR GLLPESLDYW TYPGSLTTPP LLECVTWIVL
REPISVSSEQ LLKFRSLNFN AEGKPEDPMV DNWRPAQPLN NRQIRASFK
//
