ID A0A1S3SFQ7_SALSA Unreviewed; 1193 AA.
AC A0A1S3SFQ7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=LOC106609188 {ECO:0000313|RefSeq:XP_014063174.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014063174.1};
RN [1] {ECO:0000313|RefSeq:XP_014063174.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014063174.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|RuleBase:RU363067};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions, while site 2 has a preference for
CC magnesium and/or manganese ions. {ECO:0000256|RuleBase:RU363067};
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|RuleBase:RU363067}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014063174.1; XM_014207699.1.
DR AlphaFoldDB; A0A1S3SFQ7; -.
DR GeneID; 106609188; -.
DR KEGG; sasa:106609188; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000087266; Chromosome ssa07.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF104; PHOSPHODIESTERASE; 1.
DR Pfam; PF00233; PDEase_I; 2.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363067};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 661..1121
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 279..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1063..1078
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 131397 MW; A0407650FC170361 CRC64;
MTMEVEADSG RRISRSAHEK CPRAVERNGY VKTCVTPLYQ DAGCQSWLRL ADIWSSLRLS
SAVCVGSVSV ILALLVRLVD WDVEQQSCSS NSKNNGESGS LVYFVATCVV ELLLNVWYLV
SPVFTLVCAF FWVGLYLIRC GVLIRTAVFL LAVCHFGEAA AQSLLYGAED QLLSFTATVV
VLSCLAVGAL MVVRLGQGVS VIVFISIIRT VSLISLNKIR ASWRPYLAYL VGVLGVLLAR
YADRLLTGSV PLGAGCSYVT AGKEENIIPV FKRRRRSSSV VSSDMAHSHS NSKSHRRTSL
PCLPREQSSG TCVVVDIAVM GEAHGLISDL LADPSLPPNT CSSLRAVSNL LSTQISLQPL
HRPRINPLQA LSDTHTCSDS EDWPEREKLA IPKRLRRSLP PGLLRRISST WTTTTSATGL
PTIEPGPVRR DRSASIKPLQ DSPQCSMVNS ESWNSSVMLT ISKSRSMSAS YSASATSNHL
YNRRMTRPGY PPSNISPLAS PCHSPPVQGT PVSSPTTKSC SVDLPDPVDS QGERLVDPQA
PHRALTHSIS APSSTTPHWG PPSLCSSCGR PYSRLSHGEG SMDKGDRIPH PDDPAVASSD
CESTYETNHS DSSDFAQNEE DGEGAMKPSD TQDGCRSYQP EGIVLQPLMP PPEDTQPILA
PEPLVMSELD PLMTQLNSWN FPIFNLVEKT HGRSGCILSQ VSYRLFEDTG LFETFKIPVK
EFMNYFHALE NGYRDIPYHN RIHATDVLHA VWYLTTQAVP GLPNLLTDHS SDSDSDSGLL
TPSHIGHTGF LVSKMSAVME EGYGCLSGLI PSLELMALYV AAAMHDYDHP GRTNAFLVAT
SAPQVGRERG KEGGRRERED GEDGWMDLTK GTGKAVLYND RSVLENHHAA SAWNLFMSRP
EYNFLGNLEH VEFKRFRFLV IEAILATDLK KHFDFLAEFN AKVGDDGCSG IDWSNENDRL
LVCQMCIKLA DINGPLKHKD LHLQWTEGIV NEFYEQGDEE SSLGLPISPF MDRSAPQLAK
LQESFITHIV GPLCSSYDSA ALMPGNWVDP ADARRKEGEE VGERETEEEE EDTAEEDAST
SSESSQKHVV KLKKSRRRVF CPITQHLLDN HEMWTRVIVS ETRDTPDREA PNCLSIPAEL
ITAIHEEEDE PASKEEPIDG QGEETEGEET GLAEEEEVVE QSETAEKREE ELE
//
