| Tag |
Content |
LipidDB ID |
LipidDB-10090-00381 |
Entry Name |
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UniProt Accession |
|
Theoretical PI |
5.18 |
Molecular Weight |
98535.02 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta |
Protein Synonyms/Alias |
GMP-PDE beta; 3.1.4.35; |
Gene Name |
Pde6b |
Gene Synonyms/Alias |
Mpb; Pdeb; rd; |
Created Date |
01-NOV-1991 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
853 | Canonical | PAPKSSTCCIL**** | [1][2] | S-Geranylgeranylation |
|
Organism |
Mus musculus (Mouse) |
NCBI Taxa ID |
10090 |
Reference |
[1] Anant JS, Ong OC, Xie HY, Clarke S, O'Brien PJ, Fung BK. In vivo differential prenylation of retinal cyclic GMP phosphodiesterase catalytic subunits. J BiolChem. 1992 Jan 15;267(2):687-90.[ PMID:1309771]
[2] Qin N, Pittler SJ, Baehr W. In vitro isoprenylation and membrane associationof mouse rod photoreceptor cGMP phosphodiesterase alpha and beta subunitsexpressed in bacteria. J Biol Chem. 1992 Apr 25;267(12):8458-63.[ PMID:1314827]
|
Functional Description |
This protein participates in processes of transmission and amplification of the visual signal. Necessary for the formation of a functional phosphodiesterase holoenzyme. |
Sequence Annotation |
Domain: 71 220 GAF 1.
Domain: 252 429 GAF 2.
Active site: 557 557 Proton donor.
Metal binding site: 561 561 Divalent metal cation 1.
Metal binding site: 597 597 Divalent metal cation 1.
Metal binding site: 598 598 Divalent metal cation 1.
Metal binding site: 598 598 Divalent metal cation 2.
Metal binding site: 718 718 Divalent metal cation 1.
Modified residue: 2 2 N-acetylserine.
|
Protein Length |
856 AA. |
Protein Sequence
(Canonical) |
MSLSEEQVRS FLDGNPTFAH QYFGKKLSPE NVAGACEDGW LADCGSLREL CQVEESAALF 60
ELVQDMQESV NMERVVFKIL RRLCTILHAD RCSLFMYRQR NGIAELATRL FSVQPDSLLE 120
DCLVPPDSEI VFPLDIGIVG HVAQTKKMIN VQDVAECPHF SSFADELTDY VTKNILSTPI 180
MNGKDVVAVI MAVNKLDGPC FTSEDEDVFT KYLNFATLNL KIYHLSYLHN CETRRGQVLL 240
WSANKVFEEL TDIERQFHKA FYTVRAYLNC ERYSVGLLDM TKEKEFFDVW PVLMGEAQPY 300
SGPRTPDGRE IVFYKVIDYI LHGKEDIKVI PTPPADHWAL ASGLPTYVAE SGFICNIMNA 360
SADEMFNFQE GPLDDSGWVI KNVLSMPIVN KKEEIVGVAT FYNRKDGKPF DDQDEVLMES 420
LTQFLGWSVL NTDTYDKMNK LENRKDIAQD MVLYHVRCDK DEIQEILPTR DRLGKEPADC 480
EEDELGKILK EELPGPTKFD IYEFHFSDLE CTELELVKCG IQMYYELGVV RKFQIPQEVL 540
VRFLFSVSKA YRRITYHNWR HGFNVAQTMF TLLMTGKLKS YYTDLEAFAM VTAGLCHDID 600
HRGTNNLYQM KSQNPLAKLH GSSILERHHL EFGKFLLAEE SLNIYQNLNR RQHEHVIHLM 660
DIAIIATDLA LYFKKRTMFQ KIVDESKNYE DKKSWVEYLS LETTRKEIVM AMMMTACDLS 720
AITKPWEVQS KVALLVAAEF WEQGDLERTV LDQQPIPMMD RNKAAELPKL QVGFIDFVCT 780
FVYKEFSRFH EEILPMFDRL QNNRKEWKAL ADEYEAKVKA LEEEKKKEED RVAAKKVGTE 840
VCNGGPAPKS STCCIL 856
|
FASTA
(Canonical) |
>LipidDB-10090-00381|P23440
MSLSEEQVRSFLDGNPTFAHQYFGKKLSPENVAGACEDGWLADCGSLRELCQVEESAALF
ELVQDMQESVNMERVVFKILRRLCTILHADRCSLFMYRQRNGIAELATRLFSVQPDSLLE
DCLVPPDSEIVFPLDIGIVGHVAQTKKMINVQDVAECPHFSSFADELTDYVTKNILSTPI
MNGKDVVAVIMAVNKLDGPCFTSEDEDVFTKYLNFATLNLKIYHLSYLHNCETRRGQVLL
WSANKVFEELTDIERQFHKAFYTVRAYLNCERYSVGLLDMTKEKEFFDVWPVLMGEAQPY
SGPRTPDGREIVFYKVIDYILHGKEDIKVIPTPPADHWALASGLPTYVAESGFICNIMNA
SADEMFNFQEGPLDDSGWVIKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDDQDEVLMES
LTQFLGWSVLNTDTYDKMNKLENRKDIAQDMVLYHVRCDKDEIQEILPTRDRLGKEPADC
EEDELGKILKEELPGPTKFDIYEFHFSDLECTELELVKCGIQMYYELGVVRKFQIPQEVL
VRFLFSVSKAYRRITYHNWRHGFNVAQTMFTLLMTGKLKSYYTDLEAFAMVTAGLCHDID
HRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKFLLAEESLNIYQNLNRRQHEHVIHLM
DIAIIATDLALYFKKRTMFQKIVDESKNYEDKKSWVEYLSLETTRKEIVMAMMMTACDLS
AITKPWEVQSKVALLVAAEFWEQGDLERTVLDQQPIPMMDRNKAAELPKLQVGFIDFVCT
FVYKEFSRFHEEILPMFDRLQNNRKEWKALADEYEAKVKALEEEKKKEEDRVAAKKVGTE
VCNGGPAPKSSTCCIL
|
Gene Ontology |
GO:0005886; C:plasma membrane; TAS:Reactome GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC GO:0046872; F:metal ion binding; IEA:UniProtKB-KW GO:0051480; P:cytosolic calcium ion homeostasis; IEA:Ensembl GO:0009583; P:detection of light stimulus; IMP:MGI GO:0046037; P:GMP metabolic process; IEA:Ensembl GO:0060041; P:retina development in camera-type eye; IMP:MGI GO:0007165; P:signal transduction; IEA:InterPro GO:0007601; P:visual perception; IEA:UniProtKB-KW |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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