PLCB3
entrez
5331
canonical
uniprot
Q01970
canonical
ensembl
ENSG00000149782
resolver
ensp
ENSP00000279230
resolver
ensp
ENSP00000324660
resolver
ensp
ENSP00000443631
resolver
ensp
ENSP00000683092
resolver
genesymbol
PLCB3
resolver
hgnc
HGNC:9056
resolver
uniprot
A5PKZ6
resolver
uniprot
G5E960
resolver
uniprot
Q8N1A4
resolver
uniprot_entry
PLCB3_HUMAN
resolver
uniprot_sec
A5PKZ6
resolver
uniprot_sec
G5E960
resolver
uniprot_sec
Q8N1A4
resolver
activity_regulation
ACTIVITY REGULATION: Activated by G(q)/G(11) G alpha proteins in response to ligand-binding to G protein-coupled receptors. {ECO:0000269|PubMed:20966218, ECO:0000269|PubMed:37991948}.
uniprot
proteins
amino_acid_sequence
MAGAQPGVHALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNFMAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDSAGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGDEGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIVDGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEPFDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLIYTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQLGSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVEDTKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLGDGPLVACASNGHAPGSSGHLSGADSESQEENTQL
uniprot
proteins
disease_involvement
DISEASE: Spondylometaphyseal dysplasia with corneal dystrophy (SMDCD) [MIM:618961]: An autosomal recessive disorder characterized by postnatal growth deficiency, profound limb shortening with proximal and distal segments involvement, narrow chest, radiological abnormalities involving the spine, pelvis and metaphyses, corneal clouding, and intellectual disability. {ECO:0000269|PubMed:29122926}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.4.11
uniprot
proteins
function
FUNCTION: Catalyzes the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (PubMed:20966218, PubMed:29122926, PubMed:37172014, PubMed:37991948, PubMed:9188725). Key transducer of G protein-coupled receptor signaling: activated by G(q)/G(11) G alpha proteins downstream of G protein-coupled receptors activation (PubMed:20966218, PubMed:37991948). In neutrophils, participates in a phospholipase C-activating N-formyl peptide-activated GPCR (G protein-coupled receptor) signaling pathway by promoting RASGRP4 activation by DAG, to promote neutrophil functional responses (By similarity). In conjunction with OSBPL2, it may contribute to the control of keratinocyte proliferation and differentiation, probably through the regulation of the ERK pathway and the cell cycle (PubMed:38701954). {ECO:0000250|UniProtKB:P51432, ECO:0000269|PubMed:20966218, ECO:0000269|PubMed:29122926, ECO:0000269|PubMed:37172014, ECO:0000269|PubMed:37991948, ECO:0000269|PubMed:38701954, ECO:0000269|PubMed:9188725}.
uniprot
proteins
mass_dalton
138799
uniprot
proteins
mutagenesis
MUTAGEN 258; /note="R->Q: Reduced ability to promote the GTPase activity of G(q)/G(11) G alpha proteins."; /evidence="ECO:0000269|PubMed:20966218"; MUTAGEN 260; /note="N->A: Reduced ability to promote the GTPase activity of G(q)/G(11) G alpha proteins."; /evidence="ECO:0000269|PubMed:20966218"; MUTAGEN 855; /note="Y->A: Abolished ability to transduce G(q)/G(11) G alpha signaling."; /evidence="ECO:0000269|PubMed:20966218"; MUTAGEN 859; /note="L->A: Abolished ability to transduce G(q)/G(11) G alpha signaling without affecting the phospholipase activity."; /evidence="ECO:0000269|PubMed:20966218"; MUTAGEN 861; /note="N->A: Abolished ability to transduce G(q)/G(11) G alpha signaling."; /evidence="ECO:0000269|PubMed:20966218"; MUTAGEN 862; /note="P->A: Abolished ability to transduce G(q)/G(11) G alpha signaling."; /evidence="ECO:0000269|PubMed:20966218"; MUTAGEN 863; /note="I->A: Abolished ability to transduce G(q)/G(11) G alpha signaling."; /evidence="ECO:0000269|PubMed:20966218
uniprot
proteins
pubmed
1333955
uniprot
proteins
pubmed
15143197
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20966218
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
29122926
uniprot
proteins
pubmed
37172014
uniprot
proteins
pubmed
37991948
uniprot
proteins
pubmed
38701954
uniprot
proteins
pubmed
7607669
uniprot
proteins
pubmed
7612006
uniprot
proteins
pubmed
9188725
uniprot
proteins
sequence_length
1234
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29122926}. Membrane {ECO:0000269|PubMed:37172014}; Peripheral membrane protein {ECO:0000269|PubMed:37172014}; Cytoplasmic side {ECO:0000305|PubMed:37172014}. Nucleus {ECO:0000250|UniProtKB:P51432}. Note=An heterotetramer composed of GNG2 and GNB1 increases the concentration of PLCB3 on the membrane surface, where its substrate PIP2 resides, by orienting its catalytic site. {ECO:0000269|PubMed:37172014}.
uniprot
proteins