GNAS3_RAT
ID GNAS3_RAT Reviewed; 256 AA.
AC Q792G6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Neuroendocrine secretory protein 55;
DE Short=NESP55;
DE Contains:
DE RecName: Full=LHAL tetrapeptide;
DE Contains:
DE RecName: Full=GPIPIRRH peptide;
DE Flags: Precursor;
GN Name=Gnas {ECO:0000312|RGD:2716}; Synonyms=Gnas1 {ECO:0000312|RGD:2716};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAF63227.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10729789; DOI=10.1159/000054535;
RA Weiss U., Ischia R., Eder S., Lovisetti-Scamihorn P., Bauer R.,
RA Fischer-Colbrie R.;
RT "Neuroendocrine secretory protein 55 (NESP55): alternative splicing onto
RT transcripts of the GNAS gene and posttranslational processing of a
RT maternally expressed protein.";
RL Neuroendocrinology 71:177-186(2000).
RN [2] {ECO:0000312|EMBL:AAD11801.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New England Deaconess Hospital {ECO:0000312|EMBL:AAD11801.1};
RA Wang Y.Z., Kehlenbach R.H., Huttner W.B.;
RT "Molecular characterization of XL2, a neuroendocrine-specific luminal
RT Golgi-resident protein.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle {ECO:0000250}. Secreted {ECO:0000250}. Note=Neuroendocrine
CC secretory granules. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=Nesp55 {ECO:0000269|PubMed:10729789, ECO:0000269|Ref.2};
CC IsoId=Q792G6-1; Sequence=Displayed;
CC Name=XLas-1;
CC IsoId=Q63803-1; Sequence=External;
CC Name=Gnas-1 {ECO:0000305};
CC IsoId=P63095-1; Sequence=External;
CC Name=Gnas-2 {ECO:0000305};
CC IsoId=P63095-2; Sequence=External;
CC Name=Gnas-3 {ECO:0000305}; Synonyms=GsaN1 {ECO:0000305};
CC IsoId=P63095-3; Sequence=External;
CC -!- PTM: Binds keratan sulfate chains. {ECO:0000250|UniProtKB:O18979}.
CC -!- PTM: May be proteolytically processed to give rise to a number of
CC active peptides. {ECO:0000269|PubMed:10729789}.
CC -!- MISCELLANEOUS: The GNAS locus is imprinted in a complex manner, giving
CC rise to distinct paternally, maternally and biallelically expressed
CC proteins. The XLas isoforms are paternally derived, the Gnas isoforms
CC are biallelically derived and the Nesp55 isoforms are maternally
CC derived.
CC -!- MISCELLANEOUS: [Isoform Nesp55]: Shares no sequence similarity with
CC other isoforms due to a novel first exon containing the entire reading
CC frame spliced to shared exon 2 so that exons 2-13 make up the 3'-UTR.
CC -!- SIMILARITY: Belongs to the NESP55 family. {ECO:0000255}.
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DR EMBL; AF105254; AAF63227.1; -; mRNA.
DR EMBL; AF107844; AAD11801.1; -; mRNA.
DR EMBL; AF107845; AAD11803.1; -; mRNA.
DR RefSeq; NP_001153125.1; NM_001159653.1.
DR RefSeq; NP_001153128.1; NM_001159656.1.
DR AlphaFoldDB; Q792G6; -.
DR BioGRID; 247005; 8.
DR STRING; 10116.ENSRNOP00000033065; -.
DR PaxDb; Q792G6; -.
DR GeneID; 24896; -.
DR KEGG; rno:24896; -.
DR UCSC; RGD:2716; rat. [Q792G6-1]
DR CTD; 2778; -.
DR RGD; 2716; Gnas.
DR eggNOG; ENOG502RNKH; Eukaryota.
DR OrthoDB; 1550241at2759; -.
DR PhylomeDB; Q792G6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030142; C:COPI-coated Golgi to ER transport vesicle; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:RGD.
DR GO; GO:0031224; C:intrinsic component of membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0055037; C:recycling endosome; IDA:RGD.
DR GO; GO:0001726; C:ruffle; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISO:RGD.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:RGD.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI:RGD.
DR GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; IPI:RGD.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IDA:RGD.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:RGD.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0031852; F:mu-type opioid receptor binding; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISO:RGD.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; ISO:RGD.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:RGD.
DR GO; GO:0051216; P:cartilage development; ISO:RGD.
DR GO; GO:0050890; P:cognition; ISO:RGD.
DR GO; GO:0048589; P:developmental growth; ISO:RGD.
DR GO; GO:0006306; P:DNA methylation; ISO:RGD.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISO:RGD.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; ISO:RGD.
DR GO; GO:0001958; P:endochondral ossification; ISO:RGD.
DR GO; GO:0006112; P:energy reserve metabolic process; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0071514; P:genomic imprinting; ISO:RGD.
DR GO; GO:0060789; P:hair follicle placode formation; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0035814; P:negative regulation of renal sodium excretion; IMP:RGD.
DR GO; GO:0070527; P:platelet aggregation; ISO:RGD.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:RGD.
DR GO; GO:0040032; P:post-embryonic body morphogenesis; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:2000828; P:regulation of parathyroid hormone secretion; ISO:RGD.
DR GO; GO:0009966; P:regulation of signal transduction; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0071107; P:response to parathyroid hormone; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
DR InterPro; IPR009434; NESP55.
DR Pfam; PF06390; NESP55; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cleavage on pair of basic residues;
KW Cytoplasmic vesicle; Glycoprotein; Proteoglycan; Reference proteome;
KW Secreted; Signal; Synapse.
FT SIGNAL 1..46
FT /evidence="ECO:0000250"
FT CHAIN 47..256
FT /note="Neuroendocrine secretory protein 55"
FT /id="PRO_0000253973"
FT PEPTIDE 170..173
FT /note="LHAL tetrapeptide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:10729789"
FT /id="PRO_0000253974"
FT PEPTIDE 249..256
FT /note="GPIPIRRH peptide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:10729789"
FT /id="PRO_0000253975"
FT REGION 61..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 256 AA; 29219 MW; 8484C98FF3CF147F CRC64;
MDRRSRAHQW RRARHNYNDL CPPIGRRAAT ALLWLSCSIA LLRALASSNA RAQQRAAQRR
SFLNAHHRSA AAAAAAQVLP ESSESESDHE HEEAEPELAR PECLEYDQDD YETETDSETE
PESDIQSETE FETEPETEPE TAPTTEPETE PEDERGPRGA TFNQSLTQRL HALKLQSADA
SPRRAQPTTQ EPESASEGEE PQREPLDEDP RDPEESEERR EANRQPRRCK TRRPARRRDQ
SPESPPRKGP IPIRRH
