CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023557
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Guanylate cyclase soluble subunit alpha-2 
Protein Synonyms/Alias
 GCS-alpha-2 
Gene Name
 Gucy1a2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
665PTTYQLLKREDSFTFacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 Has guanylyl cyclase on binding to the beta-1 subunit. 
Sequence Annotation
 DOMAIN 519 646 Guanylate cyclase.  
Keyword
 cGMP biosynthesis; Complete proteome; Cytoplasm; GTP-binding; Lyase; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 730 AA 
Protein Sequence
MSRRKISSES FSSLGSDYLE TSPEEEGECP LSKLCWNGSR SPPGPPGSRA AAMAATPVPA 60
ASVAAAAAAV AAGSKRAQRR RRVNLDSLGE SISLLTAPSP QTIHMTLKRT LQYYEHQVIG 120
YRDAEKNFHN ISNRCSSADH SNKEEIEDVS GILRCTANVL GLKFQEIQER FGEEFFKICF 180
DENERVLRAV GSTLQDFFNG FDALLEHIRT SFGKQATLES PSFLCKELPE GTLKLHYFHP 240
HHTVGFAMLG MIKAAGKRIY HLNVEVEQIE NEKFCSDGST PSNYSCLTFL IKECETTQIT 300
KNIPQGTSQI PTDLRISINT FCRTFPFHLM FDPNMVVLQL GEGLRKQLRC DNHKVLKFED 360
CFEIVSPKVN ATFDRVLLRL STPFVIRTKP EASGTDNEDK VMEIKGQMIH VPESNAILFL 420
GSPCVDKLDE LIGRGLHLSD IPIHDATRDV ILVGEQAKAQ DGLKKRMDKL KATLEKTHQA 480
LEEEKKKTVD LLYSIFPGDV AQQLWQRQQV QARKFDDVTM LFSDIVGFTA ICAQCTPMQV 540
ISMLNELYTR FDHQCGFLDI YKVETIGDAY CVASGLHRKS LCHAKPIALM ALKMMELSEE 600
VLTPDGRPIQ MRIGIHSGSV LAGVVGVRMP RYCLFGNNVT LASKFESGSH PRRINISPTT 660
YQLLKREDSF TFIPRSREEL PDNFPKEIPG VCYFLELRTG PKPPKPSLSS SRIKKVSYNI 720
GTMFLRETSL 730 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0004383; F:guanylate cyclase activity; IDA:RGD.
 GO:0020037; F:heme binding; IEA:InterPro.
 GO:0046982; F:protein heterodimerization activity; NAS:RGD.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro.
 GO:0030828; P:positive regulation of cGMP biosynthetic process; IEA:Compara. 
Interpro
 IPR001054; A/G_cyclase.
 IPR018297; A/G_cyclase_CS.
 IPR011645; Haem_no_assoc-bd.
 IPR011644; Heme_NO-bd.
 IPR024096; NO_sig/Golgi_transp_ligand-bd. 
Pfam
 PF00211; Guanylate_cyc
 PF07700; HNOB
 PF07701; HNOBA 
SMART
 SM00044; CYCc 
PROSITE
 PS00452; GUANYLATE_CYCLASE_1
 PS50125; GUANYLATE_CYCLASE_2 
PRINTS