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Database: UniProt
Entry: L5KVG1_PTEAL
LinkDB: L5KVG1_PTEAL
Original site: L5KVG1_PTEAL 
ID   L5KVG1_PTEAL            Unreviewed;      1121 AA.
AC   L5KVG1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Cyclic nucleotide-gated cation channel beta-1 {ECO:0000313|EMBL:ELK15429.1};
GN   ORFNames=PAL_GLEAN10011101 {ECO:0000313|EMBL:ELK15429.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK15429.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KB030537; ELK15429.1; -; Genomic_DNA.
DR   STRING; 9402.L5KVG1; -.
DR   eggNOG; KOG0499; Eukaryota.
DR   InParanoid; L5KVG1; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR45638:SF16; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL BETA-1; 1.
DR   PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS00889; CNMP_BINDING_2; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   4: Predicted;
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        268..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        306..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          526..630
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          73..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          714..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..115
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..144
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1121 AA;  124328 MW;  90FEDD84F80442BD CRC64;
     MAKPGRDMEL NHLVQDQLPG QVASRLGPSH MLDHLPNVPS YRPPTTRIPV LISRRTALSS
     SSFAKETRSS VRRLVPATKE HPEVQVEDAD ADSHPLIVED SPPSPELPPP SPATADTLAV
     PGSAPETHRK RLPSQDDEAE ELKALSPAET PVVAWSDTST PQGTDGQGRA SSTASQNSAI
     INDRLQELVK LFKERTEKVK EKLIDPDVTS DEESPQPSPA KKAPEPAPDA KPAEAGPVEE
     EHYCDMLCCK FKRRPWKKYQ FPKSIDPLTN LMYILWLFFV VMAWNWNCWL IPVRWAFPYQ
     TPDNIHLWLL MDYLCDLIYF LDITVFQIRL QFVKGGDIIT DKKEMRNNYL KSPRFKMDML
     CLLPLDLLYL KFGVNPLLRL PRCLKYMAFF EFNNRLESIL SKAYVYRVIR TTAYLLYSLH
     LNSCLYYWAS AYQGIGSTHW VYDGVGNREG APPIQRGSEW QRKGVAGASQ CSTDVAHVPE
     RGLAVPVTPG AVSSADESEL MVQLPDKMRL DLAIDVNYDI VSKVALFQGC DRQMIFDMLK
     RLRSVVYLPN DYVCKKGEIG REMYIIQAGQ VQVLGGPDGK SVLVTLKVGS VFGEISLLAV
     GGGNRRTANV VAHGFTNLFI LDKKDLNEIL VHYPESQKLL RKKARRMLRN NNKPKEKSVL
     ILPPRAGTPK LFNAALAAAG KMGAKGAKGG QLAHLRARLK ELAALEAAAK RQQLLEQAKS
     SEDAAGEAGS VARDQPAPPD QPAPPIQAKS SEDAAGEVGL AAQDQPAPLX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX
     XXXXXXXXXX XXXXXXXGWG EGAVSISEHL LCQSPTLISR D
//
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