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Neuroendocrine secretory protein 55 (NESP55) [Cleaved into: LHAL tetrapeptide; GPIPIRRH peptide]

 GNAS3_RAT               Reviewed;         256 AA.
Q792G6;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
22-NOV-2017, entry version 78.
RecName: Full=Neuroendocrine secretory protein 55;
Short=NESP55;
Contains:
RecName: Full=LHAL tetrapeptide;
Contains:
RecName: Full=GPIPIRRH peptide;
Flags: Precursor;
Name=Gnas {ECO:0000312|RGD:2716};
Synonyms=Gnas1 {ECO:0000312|RGD:2716};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000312|EMBL:AAF63227.1}
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10729789; DOI=10.1159/000054535;
Weiss U., Ischia R., Eder S., Lovisetti-Scamihorn P., Bauer R.,
Fischer-Colbrie R.;
"Neuroendocrine secretory protein 55 (NESP55): alternative splicing
onto transcripts of the GNAS gene and posttranslational processing of
a maternally expressed protein.";
Neuroendocrinology 71:177-186(2000).
[2] {ECO:0000312|EMBL:AAD11801.1}
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=New England Deaconess Hospital {ECO:0000312|EMBL:AAD11801.1};
Wang Y.Z., Kehlenbach R.H., Huttner W.B.;
"Molecular characterization of XL2, a neuroendocrine-specific luminal
Golgi-resident protein.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
synaptic vesicle {ECO:0000250}. Secreted {ECO:0000250}.
Note=Neuroendocrine secretory granules. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=Nesp55 {ECO:0000269|PubMed:10729789, ECO:0000269|Ref.2};
IsoId=Q792G6-1; Sequence=Displayed;
Note=Shares no sequence similarity with other isoforms due to a
novel first exon containing the entire reading frame spliced to
shared exon 2 so that exons 2-13 make up the 3'-UTR.;
Name=XLas-1;
IsoId=Q63803-1; Sequence=External;
Name=Gnas-1 {ECO:0000305};
IsoId=P63095-1; Sequence=External;
Name=Gnas-2 {ECO:0000305};
IsoId=P63095-2; Sequence=External;
Name=Gnas-3 {ECO:0000305}; Synonyms=GsaN1 {ECO:0000305};
IsoId=P63095-3; Sequence=External;
-!- PTM: Binds keratan sulfate chains. {ECO:0000250|UniProtKB:O18979}.
-!- PTM: May be proteolytically processed to give rise to a number of
active peptides. {ECO:0000269|PubMed:10729789}.
-!- MISCELLANEOUS: The GNAS locus is imprinted in a complex manner,
giving rise to distinct paternally, maternally and biallelically
expressed proteins. The XLas isoforms are paternally derived, the
Gnas isoforms are biallelically derived and the Nesp55 isoforms
are maternally derived.
-!- SIMILARITY: Belongs to the NESP55 family. {ECO:0000255}.
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EMBL; AF105254; AAF63227.1; -; mRNA.
EMBL; AF107844; AAD11801.1; -; mRNA.
EMBL; AF107845; AAD11803.1; -; mRNA.
RefSeq; NP_001153125.1; NM_001159653.1.
RefSeq; NP_001153128.1; NM_001159656.1.
UniGene; Rn.127731; -.
UniGene; Rn.31; -.
SMR; Q792G6; -.
BioGrid; 247005; 1.
STRING; 10116.ENSRNOP00000033065; -.
PaxDb; Q792G6; -.
PRIDE; Q792G6; -.
GeneID; 24896; -.
KEGG; rno:24896; -.
UCSC; RGD:2716; rat. [Q792G6-1]
CTD; 2778; -.
RGD; 2716; Gnas.
eggNOG; ENOG410IK62; Eukaryota.
eggNOG; ENOG41115SI; LUCA.
HOGENOM; HOG000276539; -.
HOVERGEN; HBG081561; -.
KO; K04632; -.
PhylomeDB; Q792G6; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; ISO:RGD.
GO; GO:0005768; C:endosome; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:RGD.
GO; GO:0031224; C:intrinsic component of membrane; ISO:RGD.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0001726; C:ruffle; IDA:RGD.
GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
GO; GO:0032588; C:trans-Golgi network membrane; ISO:RGD.
GO; GO:0031982; C:vesicle; IDA:RGD.
GO; GO:0043014; F:alpha-tubulin binding; IDA:RGD.
GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI:RGD.
GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; IPI:RGD.
GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD.
GO; GO:0031681; F:G-protein beta-subunit binding; IDA:RGD.
GO; GO:0005525; F:GTP binding; IDA:RGD.
GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:RGD.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
GO; GO:0031852; F:mu-type opioid receptor binding; IDA:RGD.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0004871; F:signal transducer activity; IDA:RGD.
GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISO:RGD.
GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISO:RGD.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:RGD.
GO; GO:0060348; P:bone development; ISO:RGD.
GO; GO:0055074; P:calcium ion homeostasis; IMP:RGD.
GO; GO:0051216; P:cartilage development; ISO:RGD.
GO; GO:0050890; P:cognition; ISO:RGD.
GO; GO:0048589; P:developmental growth; ISO:RGD.
GO; GO:0006306; P:DNA methylation; ISO:RGD.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISO:RGD.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; ISO:RGD.
GO; GO:0001958; P:endochondral ossification; ISO:RGD.
GO; GO:0006112; P:energy reserve metabolic process; ISO:RGD.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:RGD.
GO; GO:0071514; P:genetic imprinting; ISO:RGD.
GO; GO:0060789; P:hair follicle placode formation; ISO:RGD.
GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
GO; GO:0040015; P:negative regulation of multicellular organism growth; ISO:RGD.
GO; GO:0035814; P:negative regulation of renal sodium excretion; IMP:RGD.
GO; GO:0070527; P:platelet aggregation; ISO:RGD.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; IMP:RGD.
GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:RGD.
GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:RGD.
GO; GO:0040032; P:post-embryonic body morphogenesis; ISO:RGD.
GO; GO:0009791; P:post-embryonic development; ISO:RGD.
GO; GO:2000828; P:regulation of parathyroid hormone secretion; ISO:RGD.
GO; GO:0009966; P:regulation of signal transduction; ISO:RGD.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0042493; P:response to drug; ISO:RGD.
GO; GO:0071107; P:response to parathyroid hormone; ISO:RGD.
GO; GO:0001501; P:skeletal system development; ISO:RGD.
GO; GO:0043588; P:skin development; ISO:RGD.
GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
InterPro; IPR009434; NESP55.
Pfam; PF06390; NESP55; 1.
2: Evidence at transcript level;
Alternative splicing; Cell junction;
Cleavage on pair of basic residues; Complete proteome;
Cytoplasmic vesicle; Glycoprotein; Proteoglycan; Reference proteome;
Secreted; Signal; Synapse.
SIGNAL 1 46 {ECO:0000250}.
CHAIN 47 256 Neuroendocrine secretory protein 55.
/FTId=PRO_0000253973.
PEPTIDE 170 173 LHAL tetrapeptide. {ECO:0000255,
ECO:0000303|PubMed:10729789}.
/FTId=PRO_0000253974.
PEPTIDE 249 256 GPIPIRRH peptide. {ECO:0000255,
ECO:0000303|PubMed:10729789}.
/FTId=PRO_0000253975.
COMPBIAS 81 221 Glu-rich. {ECO:0000255}.
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


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