GNAS3_MOUSE
ID GNAS3_MOUSE Reviewed; 257 AA.
AC Q9Z0F1; Q9QXW5; Q9Z0H2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 138.
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|MGI:MGI:95777};
GN Synonyms=Gnas1 {ECO:0000312|MGI:MGI:95777};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA09026.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NESP55-2).
RX PubMed=9860993; DOI=10.1073/pnas.95.26.15475;
RA Hayward B.E., Moran V., Strain L., Bonthron D.T.;
RT "Bidirectional imprinting of a single gene: human GNAS1 encodes distinct
RT maternally, paternally and biallelically derived proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15475-15480(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAB57280.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM NESP55-2).
RC STRAIN=129/Ola {ECO:0000312|EMBL:CAB57280.1};
RX PubMed=10610704; DOI=10.1006/geno.1999.6022;
RA Kelsey G., Bodle D., Miller H.J., Beechey C.V., Coombes C., Peters J.,
RA Williamson C.M.;
RT "Identification of imprinted loci by methylation-sensitive representational
RT difference analysis: application to mouse distal chromosome 2.";
RL Genomics 62:129-138(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAB83218.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM NESP55-2).
RX PubMed=10749992; DOI=10.1093/hmg/9.5.835;
RA Hayward B.E., Bonthron D.T.;
RT "An imprinted antisense transcript at the human GNAS1 locus.";
RL Hum. Mol. Genet. 9:835-841(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAD55061.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NESP55-2).
RX PubMed=10716699; DOI=10.1073/pnas.97.7.3342;
RA Wroe S.F., Kelsey G., Skinner J.A., Bodle D., Ball S.T., Beechey C.V.,
RA Peters J., Williamson C.M.;
RT "An imprinted transcript, antisense to Nesp, adds complexity to the cluster
RT of imprinted genes at the mouse Gnas locus.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3342-3346(2000).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAD11805.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NESP55-1 AND NESP55-2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAD11805.1};
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.
RN [6] {ECO:0000305, ECO:0000312|EMBL:BAC30214.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NESP55-2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC30214.1};
RC TISSUE=Hypothalamus {ECO:0000312|EMBL:BAC30214.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000250}. Secreted {ECO:0000250}. Note=Neuroendocrine secretory
CC granules. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=Nesp55-1 {ECO:0000269|Ref.5};
CC IsoId=Q9Z0F1-1; Sequence=Displayed;
CC Name=Nesp55-2 {ECO:0000269|Ref.5};
CC IsoId=Q9Z0F1-2; Sequence=VSP_052181;
CC Name=XLas-1; Synonyms=XXL {ECO:0000305};
CC IsoId=Q6R0H7-1; Sequence=External;
CC Name=XLas-2; Synonyms=XXLb1 {ECO:0000305};
CC IsoId=Q6R0H7-2; Sequence=External;
CC Name=XLas-3; Synonyms=XXLb2 {ECO:0000305};
CC IsoId=Q6R0H7-3; Sequence=External;
CC Name=XLas-4;
CC IsoId=Q6R0H7-4; Sequence=External;
CC Name=Gnas-1 {ECO:0000305};
CC IsoId=P63094-1; Sequence=External;
CC Name=Gnas-2 {ECO:0000305};
CC IsoId=P63094-2; Sequence=External;
CC Name=Gnas-3 {ECO:0000305}; Synonyms=NTas {ECO:0000305};
CC IsoId=P63094-3; 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:0000250|UniProtKB:O18979}.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the ALEX protein from an overlapping reading frame.
CC {ECO:0000305}.
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 Nesp55-1]: Shares no sequence similarity with
CC other isoforms (except isoform Nesp55-2) due to a novel first exon
CC containing the entire reading frame spliced to shared exon 2 so that
CC exons 2-13 make up the 3'-UTR.
CC -!- MISCELLANEOUS: [Isoform Nesp55-2]: Shares no sequence similarity with
CC other isoforms (except isoform Nesp55-1) due to a novel first exon
CC containing the entire reading frame spliced to shared exon 2 so that
CC exons 2-13 make up the 3'-UTR. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NESP55 family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ010163; CAA09026.1; -; mRNA.
DR EMBL; AJ245401; CAB57280.1; -; Genomic_DNA.
DR EMBL; AJ251761; CAB83218.1; -; Genomic_DNA.
DR EMBL; AF175305; AAD55061.1; -; mRNA.
DR EMBL; AF107847; AAD11805.1; -; mRNA.
DR EMBL; AF107848; AAD11806.1; -; mRNA.
DR EMBL; AK039035; BAC30214.1; -; mRNA.
DR CCDS; CCDS17149.1; -. [Q9Z0F1-2]
DR RefSeq; NP_062664.2; NM_019690.3. [Q9Z0F1-2]
DR RefSeq; NP_068840.2; NM_022000.3. [Q9Z0F1-2]
DR RefSeq; XP_006498842.1; XM_006498779.3. [Q9Z0F1-2]
DR AlphaFoldDB; Q9Z0F1; -.
DR BioGRID; 199972; 37.
DR iPTMnet; Q9Z0F1; -.
DR MaxQB; Q9Z0F1; -.
DR PRIDE; Q9Z0F1; -.
DR ProteomicsDB; 271240; -. [Q9Z0F1-1]
DR ProteomicsDB; 271241; -. [Q9Z0F1-2]
DR Antibodypedia; 4152; 809 antibodies from 44 providers.
DR DNASU; 14683; -.
DR Ensembl; ENSMUST00000109095; ENSMUSP00000104723; ENSMUSG00000027523. [Q9Z0F1-2]
DR Ensembl; ENSMUST00000109096; ENSMUSP00000104724; ENSMUSG00000027523. [Q9Z0F1-2]
DR Ensembl; ENSMUST00000180362; ENSMUSP00000136180; ENSMUSG00000027523. [Q9Z0F1-2]
DR GeneID; 14683; -.
DR UCSC; uc008oer.1; mouse. [Q9Z0F1-2]
DR CTD; 2778; -.
DR MGI; MGI:95777; Gnas.
DR VEuPathDB; HostDB:ENSMUSG00000027523; -.
DR GeneTree; ENSGT00940000156300; -.
DR HOGENOM; CLU_100255_0_0_1; -.
DR BioGRID-ORCS; 14683; 12 hits in 74 CRISPR screens.
DR ChiTaRS; Gnas; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000027523; Expressed in superior cervical ganglion and 269 other tissues.
DR ExpressionAtlas; Q9Z0F1; baseline and differential.
DR Genevisible; Q9Z0F1; MM.
DR GO; GO:0030142; C:COPI-coated Golgi to ER transport vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISO:MGI.
DR GO; GO:0031224; C:intrinsic component of membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISO:MGI.
DR GO; GO:0010856; F:adenylate cyclase activator activity; ISO:MGI.
DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; ISO:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; ISO:MGI.
DR GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; ISO:MGI.
DR GO; GO:0031748; F:D1 dopamine receptor binding; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
DR GO; GO:0031681; F:G-protein beta-subunit binding; ISO:MGI.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0031852; F:mu-type opioid receptor binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISO:MGI.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IGI:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:MGI.
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:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0071870; P:cellular response to catecholamine stimulus; ISO:MGI.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:MGI.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0048589; P:developmental growth; ISO:MGI.
DR GO; GO:0006306; P:DNA methylation; IMP:MGI.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:MGI.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR GO; GO:0001958; P:endochondral ossification; IMP:MGI.
DR GO; GO:0006112; P:energy reserve metabolic process; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0071514; P:genomic imprinting; IMP:MGI.
DR GO; GO:0060789; P:hair follicle placode formation; ISO:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:UniProtKB.
DR GO; GO:0035814; P:negative regulation of renal sodium excretion; ISO:MGI.
DR GO; GO:0070527; P:platelet aggregation; ISO:MGI.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:MGI.
DR GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:2000828; P:regulation of parathyroid hormone secretion; IMP:MGI.
DR GO; GO:0009966; P:regulation of signal transduction; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0071107; P:response to parathyroid hormone; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
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.
FT SIGNAL 1..46
FT /evidence="ECO:0000250"
FT CHAIN 47..257
FT /note="Neuroendocrine secretory protein 55"
FT /id="PRO_0000253970"
FT PEPTIDE 170..173
FT /note="LHAL tetrapeptide"
FT /evidence="ECO:0000250|UniProtKB:O18979, ECO:0000255"
FT /id="PRO_0000253971"
FT PEPTIDE 250..257
FT /note="GPIPIRRH peptide"
FT /evidence="ECO:0000250|UniProtKB:O18979, ECO:0000255"
FT /id="PRO_0000253972"
FT REGION 61..257
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..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 141..144
FT /note="Missing (in isoform Nesp55-2)"
FT /evidence="ECO:0000303|PubMed:10716699,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9860993,
FT ECO:0000303|Ref.5"
FT /id="VSP_052181"
FT CONFLICT 8
FT /note="Q -> H (in Ref. 5; AAD11805)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="Q -> H (in Ref. 4; AAD55061)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="V -> A (in Ref. 5; AAD11805)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="E -> Q (in Ref. 5; AAD11805)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="I -> F (in Ref. 5; AAD11805)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="G -> E (in Ref. 5; AAD11805)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="Q -> E (in Ref. 5; AAD11805)"
FT /evidence="ECO:0000305"
FT CONFLICT 216..217
FT /note="EP -> S (in Ref. 5; AAD11805)"
FT /evidence="ECO:0000305"
FT CONFLICT 221..223
FT /note="KEE -> REA (in Ref. 5; AAD11805)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 257 AA; 29301 MW; 358956FD262C17EF CRC64;
MDRRSRAQQW RRARHNYNDL CPPIGRRAAT ALLWLSCSIA LLRALASSNA RAQQRAAQRR
SFLNAHHRSA AAAAAAQVLP ESSESESDHE HEEVEPELAR PECLEYDQDD YETETDSETE
PESDIESETE IETEPETEPE TAPTTEPETE PEDERGPRGA TFNQSLTQRL HALKLQSADA
SPRRAQPTTQ EPESASEGEE PQRGPLDQDP RDPEEEPEER KEENRQPRRC KTRRPARRRD
QSPESPPRKG PIPIRRH
