ID U3KCJ2_FICAL Unreviewed; 795 AA.
AC U3KCJ2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 28-MAR-2018, entry version 29.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=PDE10A {ECO:0000313|Ensembl:ENSFALP00000012746};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae;
OC Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000012746, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000012746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N.,
RA Kawakami T., Kunstner A., Makinen H., Nadachowska-Brzyska K.,
RA Qvarnstrom A., Uebbing S., Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula
RT flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000012746}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2013) 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
CC family. {ECO:0000256|RuleBase:RU363067,
CC ECO:0000256|SAAS:SAAS00865541}.
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DR EMBL; AGTO01010515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSFALT00000012796; ENSFALP00000012746; ENSFALG00000012196.
DR GeneTree; ENSGT00760000119066; -.
DR OMA; LKACRNN; -.
DR OrthoDB; EOG091G037C; -.
DR Proteomes; UP000016665; Unplaced.
DR GO; GO:0030552; F:cAMP binding; IEA:Ensembl.
DR GO; GO:0004118; F:cGMP-stimulated cyclic-nucleotide phosphodiesterase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043949; P:regulation of cAMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00471; HDc; 1.
DR PROSITE; PS00126; PDEASE_I; 1.
PE 3: Inferred from homology;
KW Complete proteome {ECO:0000313|Proteomes:UP000016665};
KW Hydrolase {ECO:0000256|RuleBase:RU363067,
KW ECO:0000256|SAAS:SAAS00865573};
KW Metal-binding {ECO:0000256|RuleBase:RU363067,
KW ECO:0000256|SAAS:SAAS00865543};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT DOMAIN 100 253 GAF. {ECO:0000259|SMART:SM00065}.
FT DOMAIN 275 431 GAF. {ECO:0000259|SMART:SM00065}.
FT DOMAIN 521 687 HD. {ECO:0000259|SMART:SM00471}.
SQ SEQUENCE 795 AA; 90030 MW; 8FFF00FFA24D819C CRC64;
MEDGSNSASC FRRFTDCFLN TSLTDEKVKA YLSLHPQVLD EFVSESVSAE TVEKWLKRKN
NRQEDETAPK EVSRYQDTNM QGVVYELNSY IEQRLDTGGD NQLLLYELSS IIKIATKADG
FALYFLGECN NSLCVFTPPG AKEGHPRLIP AGPIAHGTTV SAYVARSRKT LLVEDILGDE
RFPKGTGLES GTRIQSVLCL PIVTAIGDLI GILELYRHWG KEAFHHSHQE VATANLAWAS
VAIHQVQVCR GLAKQTELND FLLDVSKTYF DNIVAIDSLL EHIMIYAKNL VNADRCALFQ
VDHKNKELYS DLFDIGEEND GKPVFKKTKE IRFSIEKGIA GQVARTGEVL NIPDAYADPR
FNREVDLYTG YTTRNILCMP IVSRGSVIGV VQMVNKISGS AFSKTDENNF KMFAVFCALA
LHCANMYHRI RHSECIYRVT MEKLSYHSVC TAEEWQNLMH CTLPPHIYKE IELYHFDISP
YEDVWPAIFV YMVHQSCGTA CFELEKLCRF TMSVKKNYRR VPYHNWKHAV TVAHCMYAIL
QNNQGLFTDL ERKGLLVACL CHDLDHRGYS NSYLQKFDHP LAALYSTSTM EQHHFSQTVS
ILQLEGHNVF SNLSSSEYEQ VLEIIRKAII ATDLALYFGN RKQLEELHQT GALNLKNQTH
RDRVIGLMMT ACDLCSVTKL WPVTRLTAND IYAEFWAEGD EMKKTGIQPI PMMDRDKKDE
VPQGQIGFYN AVAIPCYTTL AQIFPPTGPL LRACSSRDNL NQWEKVTRGE EASIWISSQS
LAPGTSDSLP VKIDD
//
