GNAS3_BOVIN
ID GNAS3_BOVIN Reviewed; 241 AA.
AC O18979;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Neuroendocrine secretory protein 55;
DE Short=NESP55;
DE Contains:
DE RecName: Full=LSAL tetrapeptide;
DE Contains:
DE RecName: Full=GAIPIRRH peptide;
DE Flags: Precursor;
GN Name=GNAS {ECO:0000250|UniProtKB:O95467};
GN Synonyms=GNAS1 {ECO:0000250|UniProtKB:O95467};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC48752.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9111083; DOI=10.1074/jbc.272.17.11657;
RA Ischia R., Lovisetti-Scamihorn P., Hogue-Angeletti R., Wolkersdorfer M.,
RA Winkler H., Fischer-Colbrie R.;
RT "Molecular cloning and characterization of NESP55, a novel chromogranin-
RT like precursor of a peptide with 5-HT1B receptor antagonist activity.";
RL J. Biol. Chem. 272:11657-11662(1997).
RN [2] {ECO:0000305}
RP KERATAN SULFATE ATTACHMENT.
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 [3]
RP SIGNAL SEQUENCE, SUBCELLULAR LOCATION, AND C-TERMINAL PEPTIDE.
RX PubMed=15627817; DOI=10.1159/000081965;
RA Eder S., Leierer J., Klimaschewski L., Wilhelm A., Volknandt W., Laslop A.,
RA Fischer-Colbrie R.;
RT "Secretion and molecular forms of NESP55, a novel genomically imprinted
RT neuroendocrine-specific protein from AtT-20 cells.";
RL NeuroSignals 13:298-307(2004).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle. Secreted.
CC Note=Neuroendocrine secretory granules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Nesp55 {ECO:0000269|PubMed:9111083};
CC IsoId=O18979-1; Sequence=Displayed;
CC Name=Gnas-1 {ECO:0000305}; Synonyms=Alpha-S2 {ECO:0000305};
CC IsoId=P04896-1; Sequence=External;
CC Name=Gnas-2 {ECO:0000305}; Synonyms=Alpha-S1 {ECO:0000305};
CC IsoId=P04896-2; Sequence=External;
CC -!- TISSUE SPECIFICITY: Highly expressed in adrenal medulla and anterior
CC and posterior pituitary. In the brain, detected in hypothalamus,
CC hippocampus, caudate nucleus, thalamus and, in significantly lower
CC amounts, in the cerebellum. {ECO:0000269|PubMed:9111083}.
CC -!- PTM: Binds keratan sulfate chains. {ECO:0000269|PubMed:10729789}.
CC -!- PTM: May be proteolytically processed to give rise to a number of
CC active peptides. {ECO:0000269|PubMed:9111083}.
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. {ECO:0000305}.
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; U77614; AAC48752.1; -; mRNA.
DR RefSeq; NP_001258700.1; NM_001271771.1. [O18979-1]
DR AlphaFoldDB; O18979; -.
DR STRING; 9913.ENSBTAP00000023246; -.
DR PaxDb; O18979; -.
DR PRIDE; O18979; -.
DR GeneID; 281793; -.
DR KEGG; bta:281793; -.
DR CTD; 2778; -.
DR eggNOG; ENOG502RNKH; Eukaryota.
DR HOGENOM; CLU_100255_0_0_1; -.
DR TreeFam; TF350423; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; ISS:CAFA.
DR GO; GO:0071107; P:response to parathyroid hormone; IEA:InterPro.
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 CHAIN 47..241
FT /note="Neuroendocrine secretory protein 55"
FT /id="PRO_0000253976"
FT PEPTIDE 159..162
FT /note="LSAL tetrapeptide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:9111083"
FT /id="PRO_0000253977"
FT PEPTIDE 234..241
FT /note="GAIPIRRH peptide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:9111083"
FT /id="PRO_0000253978"
FT REGION 71..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..139
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 241 AA; 27494 MW; 736D46C0C2E3C576 CRC64;
MDRRSRPQLG RRARHNYNDL CPPIGRRAAT ALLWLSCSIA LLRALATSST RAQQRAAAQR
RTFLNAHHRS AAQVFPEPPE SDHEDTDFEP SLPECPEYQE EEFDYESETE SESEIESETE
FETESDTAPT TEPETEPEDE PGPVVPKRPT FHQSLTERLS ALRLRSPDAS PSRAPPSTQE
SESPRQGEEP EDKDPRDPEE SEEPKEEEKQ QQHRCKPKKP TRRDPSPESP SKRGAIPIRR
H
