CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010844
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenylate cyclase type 6 
Protein Synonyms/Alias
 ATP pyrophosphate-lyase 6; Adenylate cyclase type VI; Adenylyl cyclase 6; Ca(2+)-inhibitable adenylyl cyclase 
Gene Name
 Adcy6 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
127LVQVFQSKQFRSAKLubiquitination[1]
411ELFARFDKLAAENHCubiquitination[1]
565EEKAMLAKLQRTRANubiquitination[1]
606MGIDDSSKDNRGAQDubiquitination[1]
931KLQATGEKEEMEELQubiquitination[1]
1098AGVIGARKPQYDIWGubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
 Membrane-bound, calcium-inhibitable adenylyl cyclase. 
Sequence Annotation
 METAL 382 382 Magnesium 1 (By similarity).
 METAL 382 382 Magnesium 2 (By similarity).
 METAL 383 383 Magnesium 2; via carbonyl oxygen (By
 METAL 426 426 Magnesium 1 (By similarity).
 METAL 426 426 Magnesium 2 (By similarity).
 MOD_RES 553 553 Phosphoserine (By similarity).
 MOD_RES 573 573 Phosphoserine (By similarity).
 MOD_RES 659 659 Phosphoserine (By similarity).
 MOD_RES 916 916 Phosphothreonine (By similarity).
 CARBOHYD 277 277 N-linked (GlcNAc...) (Potential).
 CARBOHYD 790 790 N-linked (GlcNAc...) (Potential).
 CARBOHYD 875 875 N-linked (GlcNAc...) (Potential).  
Keyword
 ATP-binding; cAMP biosynthesis; Cell projection; Cilium; Complete proteome; Glycoprotein; Lyase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1165 AA 
Protein Sequence
MSWFSGLLVP KVDERKTAWG ERNGQKRPRH ANRASGFCAP RYMSCLKNAE PPSPTPAAHT 60
RCPWQDEAFI RRAGPGRGVE LGLRSVALGF DDTEVTTPMG TAEVAPDTSP RSGPSCWHRL 120
VQVFQSKQFR SAKLERLYQR YFFQMNQSSL TLLMAVLVLL MAVLLTFHAA PAQPQPAYVA 180
LLTCASVLFV VLMVVCNRHS FRQDSMWVVS YVVLGILAAV QVGGALAANP HSPSAGLWCP 240
VFFVYITYTL LPIRMRAAVL SGLGLSTLHL ILAWQLNSSD PFLWKQLGAN VVLFLCTNAI 300
GVCTHYPAEV SQRQAFQETR GYIQARLHLQ HENRQQERLL LSVLPQHVAM EMKEDINTKK 360
EDMMFHKIYI QKHDNVSILF ADIEGFTSLA SQCTAQELVM TLNELFARFD KLAAENHCLR 420
IKILGDCYYC VSGLPEARAD HAHCCVEMGV DMIEAISLVR EVTGVNVNMR VGIHSGRVHC 480
GVLGLRKWQF DVWSNDVTLA NHMEAGGGRR IHITRATLQY LNGDYEVEPG RGGERNAYLK 540
EQCIETFLIL GASQKRKEEK AMLAKLQRTR ANSMEGLMPR WVPDRAFSRT KDSKAFRQMG 600
IDDSSKDNRG AQDALNPEDE VDEFLGRAID ARSIDQLRKD HVRRFLLTFQ REDLEKKYSR 660
KVDPRFGAYV ACALLVFCFI CFIQLLVFPY STLILGIYAA IFLLLLVTVL ICAVCSCGSF 720
FPKALQRLSR NIVRSRVHST AVGIFSVLLV FISAIANMFT CNHTPIRTCA ARMLNLTPAD 780
VTACHLQQLN YSLGLDAPLC EGTAPTCSFP EYFVGNVLLS LLASSVFLHI SSIGKLAMTF 840
ILGFTYLVLL LLGPPAAIFD NYDLLLGVHG LASSNETFDG LDCPAVGRVA LKYMTPVILL 900
VFALALYLHA QQVESTARLD FLWKLQATGE KEEMEELQAY NRRLLHNILP KDVAAHFLAR 960
ERRNDELYYQ SCECVAVMFA SIANFSEFYV ELEANNEGVE CLRLLNEIIA DFDEIISEER 1020
FRQLEKIKTI GSTYMAASGL NASTYDQVGR SHITALADYA MRLMEQMKHI NEHSFNNFQM 1080
KIGLNMGPVV AGVIGARKPQ YDIWGNTVNV SSRMDSTGVP DRIQVTTDLY QVLAAKGYQL 1140
ECRGVVKVKG KGEMTTYFLN GGPSS 1165 
Gene Ontology
 GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; TAS:MGI.
 GO:0004016; F:adenylate cyclase activity; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0019901; F:protein kinase binding; ISS:BHF-UCL.
 GO:0007190; P:activation of adenylate cyclase activity; TAS:MGI.
 GO:0035556; P:intracellular signal transduction; IEA:InterPro. 
Interpro
 IPR001054; A/G_cyclase.
 IPR018297; A/G_cyclase_CS.
 IPR009398; Adenylate_cyclase-like. 
Pfam
 PF06327; DUF1053
 PF00211; Guanylate_cyc 
SMART
 SM00044; CYCc 
PROSITE
 PS00452; GUANYLATE_CYCLASE_1
 PS50125; GUANYLATE_CYCLASE_2 
PRINTS