(data stored in ACNUC17706 zone)

HOGENOM: CANFA13_48_PE6

ID   CANFA13_48_PE6                       STANDARD;      PRT;   691 AA.
AC   CANFA13_48_PE6; Q28279;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=cGMP-gated cation channel alpha-1;AltName: Full=Cyclic
DE   nucleotide-gated cation channel 1;AltName: Full=Cyclic nucleotide-gated
DE   channel alpha-1; Short=CNG channel alpha-1; Short=CNG-1;
DE   Short=CNG1;AltName: Full=Cyclic nucleotide-gated channel,
DE   photoreceptor;AltName: Full=Rod photoreceptor cGMP-gated channel subunit
DE   alpha; (CANFA13_48.PE6).
GN   Name=CNGA1; Synonyms=CNCG, CNCG1;
OS   CANIS LUPUS FAMILIARIS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CANFA13_48.PE6.
CC       Canis familiaris chromosome 13 BROADD2 partial sequence 46303309..47242
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:CNGA1_CANFA
CC   -!- FUNCTION: Visual signal transduction is mediated by a G-protein
CC       coupled cascade using cGMP as second messenger. This protein can
CC       be activated by cGMP which leads to an opening of the cation
CC       channel and thereby causing a depolarization of rod
CC       photoreceptors.
CC   -!- SUBUNIT: Homotetramer or higher oligomer.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel
CC       (TC 1.A.1.5) family. CNGA1 subfamily.
CC   -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC   -!- GENE_FAMILY: HOG000007898 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Canis_familiaris;ENSCAFG00000001917;ENSCAFT00000003035;ENSCAFP00000002817.
DR   EMBL; U83905; - ;
DR   EMBL; X99914; - ;
DR   UniProtKB/Swiss-Prot; Q28279; -.
DR   EMBL; X99914; CAA68186.1; -; Genomic_DNA.
DR   EMBL; U83905; AAB61707.1; -; mRNA.
DR   PIR; JC6509; JC6509.
DR   RefSeq; NP_001003222.1; NM_001003222.1.
DR   UniGene; Cfa.3753; -.
DR   ProteinModelPortal; Q28279; -.
DR   STRING; Q28279; -.
DR   Ensembl; ENSCAFT00000003035; ENSCAFP00000002817; ENSCAFG00000001917.
DR   GeneID; 403891; -.
DR   KEGG; cfa:403891; -.
DR   CTD; 1259; -.
DR   eggNOG; maNOG12039; -.
DR   GeneTree; ENSGT00550000074376; -.
DR   PhylomeDB; Q28279; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS00889; CNMP_BINDING_2; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   HOGENOMDNA; CANFA13_48.PE6; -.
KW   ENSCAFG00000001917fold_1320000031; ENSCAFP00000002817fold_1320000031;
KW   U83905; X99914;
KW   cGMP; cGMP-binding; Complete proteome; Glycoprotein; Ion transport;
KW   Ionic channel; Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW   Reference proteome; Sensory transduction; Transmembrane;
KW   Transmembrane helix; Transport; Vision.
SQ   SEQUENCE   691 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKKNIINTWY SFVNIPNVIV PDIEKEIRRM ENGARSSFSD DDGDDDSASM FEESENETPH
     ARDSCRNNSQ RRDPSQREQY LPGAIALFNV NNSSNKEQEP KEKKKKKKEK KSKSGDKNEN
     KKDSEKKKKK EKEKEKKNKE EKGKDKKEEE KKEVMVIDPA GNMYYNWLFC ITLPVMYNWT
     MVIARACFDE LQSDYLEYWI IFDYLSDIVY LLDMFVRTRT GYLEQGLLVR EEAKLIEKYK
     SNLQFKLDFL SVIPTDLLYF KLGWNYPEIR LNRLLRISRM FEFFQRTETR TNYPNIFRIS
     NLVMYIVIII HWNACVYFSI SKAIGFGNDT WVYPDVNDPE FGRLARKYVY SLYWSTLTLT
     TIGETPPPVR DSEYVFVVVD FLIGVLIFAT IVGNIGSMIS NMNAARAEFQ ARIDAIKQYM
     HFRNVSKDME KRVIKWFDYL WTNKKTVDEK EVLKYLPDKL RAEIAINVHL DTLKKVRIFA
     DCEAGLLVEL VLKLQPQVYS PGDYICKKGD IGREMYIIKE GKLAVVADDG ITQFVVLSDG
     SYFGEISILN IKGSKAGNRR TANIKSIGYS DLFCLSKDDL MEALTEYPDA KTMLEEKGKQ
     ILMKDGLLDI NIANAGSDPK DLEEKVTRME GSVDLLQTRF ARILAEYESM QQKLKQRLTK
     VERFLKPIID TEFSALEGTG DESRPLDSTQ D
//

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