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Database: UniProt
Entry: U3KCJ2_FICAL
LinkDB: U3KCJ2_FICAL
Original site: U3KCJ2_FICAL 
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
//
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