ID V8PH73_OPHHA Unreviewed; 137 AA.
AC V8PH73;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Receptor-type tyrosine-protein phosphatase gamma {ECO:0000313|EMBL:ETE73368.1};
DE Flags: Fragment;
GN Name=PTPRG {ECO:0000313|EMBL:ETE73368.1};
GN ORFNames=L345_00789 {ECO:0000313|EMBL:ETE73368.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE73368.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE73368.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE73368.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00010718}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE73368.1}.
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DR EMBL; AZIM01000101; ETE73368.1; -; Genomic_DNA.
DR AlphaFoldDB; V8PH73; -.
DR Proteomes; UP000018936; Unassembled WGS sequence.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
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; IPR023561; Carbonic_anhydrase_a-class.
DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF134; CARBONIC ANHYDRASE 15; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 3: Inferred from homology;
KW Receptor {ECO:0000313|EMBL:ETE73368.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018936}.
FT DOMAIN 28..137
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE73368.1"
FT NON_TER 137
FT /evidence="ECO:0000313|EMBL:ETE73368.1"
SQ SEQUENCE 137 AA; 15608 MW; 0D59CCDFE428A63D CRC64;
QTVYFLRRKG EEGEGEEKKE EEKKNENEEE EEEEEAGGGV WIRRTHQSPI DIIDHQAHVG
AEYQEIRLVG FDNESSNKTW MKNTGKTVAI LLKDDYFISG AGLPGRFKAE KVEFHWGQSN
GSAGSEHSIN GRRFPVE
//