GenomeNet

Database: UniProt
Entry: G1PM78_MYOLU
LinkDB: G1PM78_MYOLU
Original site: G1PM78_MYOLU 
ID   G1PM78_MYOLU            Unreviewed;       759 AA.
AC   G1PM78;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   23-MAY-2018, entry version 44.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN   Name=PDE6A {ECO:0000313|Ensembl:ENSMLUP00000011994};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
OC   Vespertilionidae; Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000011994, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000011994, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J.,
RA   Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E.,
RA   Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J.,
RA   Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S.,
RA   Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I.,
RA   Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I.,
RA   Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J.,
RA   Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D.,
RA   Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L.,
RA   Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S.,
RA   Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G.,
RA   Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K.,
RA   Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T.,
RA   Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J.,
RA   Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S.,
RA   Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29
RT   mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000011994}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) 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:SAAS01040771}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AAPE02049866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 59463.ENSMLUP00000011994; -.
DR   Ensembl; ENSMLUT00000013185; ENSMLUP00000011994; ENSMLUG00000013174.
DR   eggNOG; KOG3689; Eukaryota.
DR   eggNOG; ENOG410XRI7; LUCA.
DR   GeneTree; ENSGT00760000119066; -.
DR   InParanoid; G1PM78; -.
DR   OMA; LICNIMN; -.
DR   OrthoDB; EOG091G01RK; -.
DR   TreeFam; TF316499; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046037; P:GMP metabolic process; IEA:Ensembl.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; 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; IPR032958; PDE6A.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   InterPro; IPR023174; PDEase_CS.
DR   PANTHER; PTHR11347:SF115; PTHR11347:SF115; 1.
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; 1.
DR   PROSITE; PS51845; PDEASE_I_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001074};
KW   Hydrolase {ECO:0000256|RuleBase:RU363067,
KW   ECO:0000256|SAAS:SAAS01040760};
KW   Metal-binding {ECO:0000256|RuleBase:RU363067,
KW   ECO:0000256|SAAS:SAAS01040765};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074}.
FT   DOMAIN      484    759       PDEase. {ECO:0000259|PROSITE:PS51845}.
SQ   SEQUENCE   759 AA;  88210 MW;  20D6B3F6D2FC2A54 CRC64;
     MDEVTEEEVE KFLDSNVGFA KQYYDLRYRA KVISDLLGAK EAAVDFSSYH PLSSVEESEI
     IFDLLRDFQE NLQAEKCIFN VMKKLCFLLQ ADRMSLFMYR ARNGIAELAT RLFNVHKDAV
     LEECLVVPDS EIVFPLDMGV VGHVAHSKKL TNVPNTEEDE HFCDFVDTLT EYQTKNILAS
     PIMNGKDVVA IIMAVNKVGG PHFTKSDEEI LLKYLNFANL IMKVFHLSYL HNCETRRGQI
     LLWSGSKVFE ELTDIERQFH KALYTVRAFL NCDRYSVGLL DMTKQKEFFD VWPVLMGEAP
     PYTGPRTPDG REINFYKVID YILHGKEDIK VIPPNPPSDH WALASGLPTY VAQNGLICNI
     MNAPAEDFFE FQKEPLDESG WVIKNVLSMP IVNKKEEIVG VATFYNRKDG KPFDEMDETL
     MESLAQFLGW SVLNPDTYES MNKLEYRKDI FQDMVKYHVK CDNEEIQKIL KTREVYGKEP
     WECEEEELAE ILQEELPDAE KYEINKFHFS DLPLTELELV KCGIQMYYEL KVVDKFHIPQ
     EALVRFMYSL SKGYRRITYH NWRHGFNVGQ TMFSLLVTGK LKRYFTDLEA LAMVTAAFCH
     DIDHRGTNNL YQMKSQNPLA KLHGSSILER HHLEFGKTLL RDEGLNIFQN LNRRQHEHAI
     HMMDIAIIAT DLALYFKKRT MFQKIVDQSK TFETQQEWTQ YMMLEQTRKE IVMAMMMTAC
     DLSAITKPWE VQSKVALLVA AEFWEQGDLE RTVLQQNPI
//
DBGET integrated database retrieval system