ID A0A2Y9J8S9_ENHLU Unreviewed; 555 AA.
AC A0A2Y9J8S9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Carbonic anhydrase 9 isoform X1 {ECO:0000313|RefSeq:XP_022357368.1};
GN Name=LOC111146216 {ECO:0000313|RefSeq:XP_022357368.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022357368.1};
RN [1] {ECO:0000313|RefSeq:XP_022357368.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022357368.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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};
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DR RefSeq; XP_022357368.1; XM_022501660.1.
DR AlphaFoldDB; A0A2Y9J8S9; -.
DR STRING; 391180.A0A2Y9J8S9; -.
DR KEGG; elk:111146216; -.
DR OrthoDB; 49814at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR InterPro; IPR038779; CCDC107.
DR PANTHER; PTHR37345; COILED-COIL DOMAIN-CONTAINING PROTEIN 107; 1.
DR PANTHER; PTHR37345:SF1; COILED-COIL DOMAIN-CONTAINING PROTEIN 107; 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 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..555
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036470008"
FT TRANSMEM 509..527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 233..484
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT REGION 27..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 103..130
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 44..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 60564 MW; 429DFCC1ACC45010 CRC64;
MAGSVPFAGL LGLLLVSALP GVLGDRPSPD LRAHPGGHAQ VGPEATEPRR RSPPKDQREW
ARAGALPLGA LYTAAVVAFV LYKCLQGKDE AAVLQEEEGK KESSQSEQQL AHLTQQLAQT
EQHLNNLMAQ LDPLFERPAR ASEYEASDHP PAVARQQAKQ GCGRSRTSVE DLPREDPPGD
EDPPGEQDPS GMKTEPGKED SLKLEDLPTV EAPRDPQGSQ NNDYRHNKGD DHSHWRYGGD
PPWPQVSPAC AGRFQSPVDI RPELAAFCRA LQPPELLGFE LPKLPELRLR NNGHTVQLTL
PPGLEMALGP GREYRALQLH LHWGAAGRPG SEHTVDGHRF PAEIHVVHLS TAFAKVDEAL
GRPGGLAVLA AFLQEGPEEN SAYEQLLSHL EEITEEDSET WVPGLDVSAL LPSDLSRYFR
YEGSLTTPPC AQGVIWTVFN QTVRLSAKQL HTLSGSLWGP DDSQLQLNFR ARQPLNGRII
EASFLTGTES SPRTVEPVHL NSCLAAGDIL ALVFGLLFAV TSIAFLVQMR RQQRFRSGTK
GNVSYHPAEV TETVA
//
