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

 GNAS3_HUMAN             Reviewed;         245 AA.
O95467; B2RB88; E1P5G2; O95417;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
27-SEP-2017, entry version 115.
RecName: Full=Neuroendocrine secretory protein 55;
Short=NESP55;
Contains:
RecName: Full=LHAL tetrapeptide;
Contains:
RecName: Full=GPIPIRRH peptide;
Flags: Precursor;
Name=GNAS {ECO:0000312|HGNC:HGNC:4392};
Synonyms=GNAS1 {ECO:0000312|EMBL:CAA08889.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000312|EMBL:CAA08889.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9860993; DOI=10.1073/pnas.95.26.15475;
Hayward B.E., Moran V., Strain L., Bonthron D.T.;
"Bidirectional imprinting of a single gene: human GNAS1 encodes
distinct maternally, paternally and biallelically derived proteins.";
Proc. Natl. Acad. Sci. U.S.A. 95:15475-15480(1998).
[2] {ECO:0000312|EMBL:CAB83214.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10749992; DOI=10.1093/hmg/9.5.835;
Hayward B.E., Bonthron D.T.;
"An imprinted antisense transcript at the human GNAS1 locus.";
Hum. Mol. Genet. 9:835-841(2000).
[3] {ECO:0000312|EMBL:AAF63226.1}
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).
[4] {ECO:0000312|EMBL:AAD11804.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6] {ECO:0000312|EMBL:AAD11804.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
INVOLVEMENT IN PHP1B.
PubMed=11067869; DOI=10.1172/JCI10431;
Liu J., Litman D., Rosenberg M.J., Yu S., Biesecker L.G.,
Weinstein L.S.;
"A GNAS1 imprinting defect in pseudohypoparathyroidism type IB.";
J. Clin. Invest. 106:1167-1174(2000).
[8]
INVOLVEMENT IN PHP1B.
PubMed=11294659; DOI=10.1086/320117;
Bastepe M., Lane A.H., Jueppner H.;
"Paternal uniparental isodisomy of chromosome 20q -- and the resulting
changes in GNAS1 methylation -- as a plausible cause of
pseudohypoparathyroidism.";
Am. J. Hum. Genet. 68:1283-1289(2001).
[9]
INVOLVEMENT IN PHP1B.
PubMed=11029463; DOI=10.1074/jbc.M006032200;
Wu W.-I., Schwindinger W.F., Aparicio L.F., Levine M.A.;
"Selective resistance to parathyroid hormone caused by a novel
uncoupling mutation in the carboxyl terminus of G alpha(s). A cause of
pseudohypoparathyroidism type Ib.";
J. Biol. Chem. 276:165-171(2001).
[10]
INVOLVEMENT IN PHP1B.
PubMed=12858292; DOI=10.1086/377136;
Jan de Beur S., Ding C., Germain-Lee E., Cho J., Maret A.,
Levine M.A.;
"Discordance between genetic and epigenetic defects in
pseudohypoparathyroidism type 1b revealed by inconsistent loss of
maternal imprinting at GNAS1.";
Am. J. Hum. Genet. 73:314-322(2003).
[11]
INVOLVEMENT IN AIMAH1.
PubMed=12727968; DOI=10.1210/jc.2002-021362;
Fragoso M.C.B.V., Domenice S., Latronico A.C., Martin R.M.,
Pereira M.A.A., Zerbini M.C.N., Lucon A.M., Mendonca B.B.;
"Cushing's syndrome secondary to adrenocorticotropin-independent
macronodular adrenocortical hyperplasia due to activating mutations of
GNAS1 gene.";
J. Clin. Endocrinol. Metab. 88:2147-2151(2003).
[12]
INVOLVEMENT IN PHP1B.
PubMed=14561710; DOI=10.1172/JCI19159;
Bastepe M., Froehlich L.F., Hendy G.N., Indridason O.S., Josse R.G.,
Koshiyama H., Koerkkoe J., Nakamoto J.M., Rosenbloom A.L.,
Slyper A.H., Sugimoto T., Tsatsoulis A., Crawford J.D., Jueppner H.;
"Autosomal dominant pseudohypoparathyroidism type Ib is associated
with a heterozygous microdeletion that likely disrupts a putative
imprinting control element of GNAS.";
J. Clin. Invest. 112:1255-1263(2003).
[13]
INVOLVEMENT IN PHP1B.
PubMed=15800843; DOI=10.1086/429932;
Linglart A., Gensure R.C., Olney R.C., Jueppner H., Bastepe M.;
"A novel STX16 deletion in autosomal dominant pseudohypoparathyroidism
type Ib redefines the boundaries of a cis-acting imprinting control
element of GNAS.";
Am. J. Hum. Genet. 76:804-814(2005).
[14]
INVOLVEMENT IN PHP1B.
PubMed=15592469; DOI=10.1038/ng1487;
Bastepe M., Froehlich L.F., Linglart A., Abu-Zahra H.S., Tojo K.,
Ward L.M., Jueppner H.;
"Deletion of the NESP55 differentially methylated region causes loss
of maternal GNAS imprints and pseudohypoparathyroidism type Ib.";
Nat. Genet. 37:25-27(2005).
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
{ECO:0000250}. Secreted {ECO:0000250}. Note=Neuroendocrine
secretory granules. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=Nesp55 {ECO:0000269|PubMed:10729789,
ECO:0000269|PubMed:10749992, ECO:0000269|PubMed:9860993,
ECO:0000269|Ref.4};
IsoId=O95467-1; 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=Q5JWF2-1; Sequence=External;
Note=Gene prediction confirmed by EST data.;
Name=XLas-2;
IsoId=Q5JWF2-2; Sequence=External;
Note=Gene prediction confirmed by EST data.;
Name=XLas-3;
IsoId=Q5JWF2-3; Sequence=External;
Name=Gnas-1 {ECO:0000305}; Synonyms=Alpha-S2 {ECO:0000305}, GNASl
{ECO:0000305}, Alpha-S-long {ECO:0000305};
IsoId=P63092-1, P04895-1;
Sequence=External;
Name=Gnas-2 {ECO:0000305}; Synonyms=Alpha-S1 {ECO:0000305}, GNASs
{ECO:0000305}, Alpha-S-short {ECO:0000305};
IsoId=P63092-2, P04895-2;
Sequence=External;
Name=3;
IsoId=P63092-3; Sequence=External;
Note=No experimental confirmation available.;
-!- 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}.
-!- DISEASE: ACTH-independent macronodular adrenal hyperplasia 1
(AIMAH1) [MIM:219080]: A rare adrenal defect characterized by
multiple, bilateral, non-pigmented, benign, adrenocortical
nodules. It results in excessive production of cortisol leading to
ACTH-independent Cushing syndrome. Clinical manifestations of
Cushing syndrome include facial and truncal obesity, abdominal
striae, muscular weakness, osteoporosis, arterial hypertension,
diabetes. {ECO:0000269|PubMed:12727968}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Pseudohypoparathyroidism 1B (PHP1B) [MIM:603233]: A
disorder characterized by end-organ resistance to parathyroid
hormone, hypocalcemia and hyperphosphatemia. Patients affected
with PHP1B lack developmental defects characteristic of Albright
hereditary osteodystrophy, and typically show no other endocrine
abnormalities besides resistance to PTH.
{ECO:0000269|PubMed:11029463, ECO:0000269|PubMed:11067869,
ECO:0000269|PubMed:11294659, ECO:0000269|PubMed:12858292,
ECO:0000269|PubMed:14561710, ECO:0000269|PubMed:15592469,
ECO:0000269|PubMed:15800843}. Note=The disease is caused by
mutations affecting the gene represented in this entry. Most
affected individuals have defects in methylation of the gene. In
some cases microdeletions involving the STX16 appear to cause loss
of methylation at exon A/B of GNAS, resulting in PHP1B. Paternal
uniparental isodisomy have also been observed.
-!- DISEASE: GNAS hyperfunction (GNASHYP) [MIM:139320]: This condition
is characterized by increased trauma-related bleeding tendency,
prolonged bleeding time, brachydactyly and mental retardation.
Both the XLas isoforms and the ALEX protein are mutated which
strongly reduces the interaction between them and this may allow
unimpeded activation of the XLas isoforms. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: This protein is produced by a bicistronic gene
which also produces the ALEX protein from an overlapping reading
frame. {ECO:0000305}.
-!- 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; AJ009849; CAA08889.1; -; Genomic_DNA.
EMBL; AJ251760; CAB83214.1; -; Genomic_DNA.
EMBL; AF105253; AAF63226.1; -; mRNA.
EMBL; AF107846; AAD11804.1; -; Genomic_DNA.
EMBL; AK314549; BAG37135.1; -; mRNA.
EMBL; CH471077; EAW75466.1; -; Genomic_DNA.
EMBL; CH471077; EAW75457.1; -; Genomic_DNA.
CCDS; CCDS13471.1; -. [O95467-1]
RefSeq; NP_000507.1; NM_000516.5.
RefSeq; NP_001070956.1; NM_001077488.3.
RefSeq; NP_001070957.1; NM_001077489.3.
RefSeq; NP_001296790.1; NM_001309861.1.
RefSeq; NP_057676.1; NM_016592.3. [O95467-1]
RefSeq; NP_536351.1; NM_080426.3.
RefSeq; XP_016883310.1; XM_017027821.1. [O95467-1]
RefSeq; XP_016883311.1; XM_017027822.1. [O95467-1]
UniGene; Hs.125898; -.
ProteinModelPortal; O95467; -.
SMR; O95467; -.
BioGrid; 109040; 91.
iPTMnet; O95467; -.
BioMuta; NPEPL1; -.
PeptideAtlas; O95467; -.
PRIDE; O95467; -.
DNASU; 2778; -.
Ensembl; ENST00000313949; ENSP00000323571; ENSG00000087460. [O95467-1]
Ensembl; ENST00000371075; ENSP00000360115; ENSG00000087460. [O95467-1]
Ensembl; ENST00000371098; ENSP00000360139; ENSG00000087460. [O95467-1]
GeneID; 2778; -.
KEGG; hsa:2778; -.
UCSC; uc002xzt.5; human. [O95467-1]
CTD; 2778; -.
DisGeNET; 2778; -.
EuPathDB; HostDB:ENSG00000087460.23; -.
GeneCards; GNAS; -.
HGNC; HGNC:4392; GNAS.
HPA; CAB010337; -.
HPA; HPA018122; -.
MalaCards; GNAS; -.
MIM; 139320; gene+phenotype.
MIM; 219080; phenotype.
MIM; 603233; phenotype.
neXtProt; NX_O95467; -.
OpenTargets; ENSG00000087460; -.
PharmGKB; PA175; -.
GeneTree; ENSGT00770000120503; -.
HOGENOM; HOG000276539; -.
HOVERGEN; HBG081561; -.
KO; K04632; -.
ChiTaRS; GNAS; human.
GeneWiki; GNAS_complex_locus; -.
GenomeRNAi; 2778; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000087460; -.
CleanEx; HS_GNAS; -.
ExpressionAtlas; O95467; baseline and differential.
Genevisible; O95467; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0007565; P:female pregnancy; NAS:UniProtKB.
GO; GO:0040015; P:negative regulation of multicellular organism growth; ISS:UniProtKB.
GO; GO:0009306; P:protein secretion; NAS:UniProtKB.
GO; GO:0071107; P:response to parathyroid hormone; IMP:UniProtKB.
InterPro; IPR009434; NESP55.
Pfam; PF06390; NESP55; 1.
2: Evidence at transcript level;
Alternative splicing; Cleavage on pair of basic residues;
Complete proteome; Cushing syndrome; Cytoplasmic vesicle;
Glycoprotein; Proteoglycan; Reference proteome; Secreted; Signal.
SIGNAL 1 46 {ECO:0000250}.
CHAIN 47 245 Neuroendocrine secretory protein 55.
/FTId=PRO_0000253967.
PEPTIDE 163 166 LHAL tetrapeptide. {ECO:0000255,
ECO:0000303|PubMed:10729789}.
/FTId=PRO_0000253968.
PEPTIDE 238 245 GPIPIRRH peptide. {ECO:0000255,
ECO:0000303|PubMed:10729789}.
/FTId=PRO_0000253969.
COMPBIAS 78 142 Glu-rich. {ECO:0000255}.
CONFLICT 26 26 R -> C (in Ref. 4; AAD11804).
{ECO:0000305}.
CONFLICT 41 41 L -> D (in Ref. 4; AAD11804).
{ECO:0000305}.
CONFLICT 72 72 G -> GR (in Ref. 4; AAD11804).
{ECO:0000305}.
CONFLICT 133 133 P -> PETAP (in Ref. 4). {ECO:0000305}.
CONFLICT 171 171 P -> A (in Ref. 4; AAD11804).
{ECO:0000305}.
CONFLICT 211 219 KEEKQRRRC -> REENSSDSS (in Ref. 4;
AAD11804). {ECO:0000305}.
CONFLICT 230 230 S -> F (in Ref. 4; AAD11804).
{ECO:0000305}.
SEQUENCE 245 AA; 28029 MW; 4F02B8B1115089E2 CRC64;
MDRRSRAQQW RRARHNYNDL CPPIGRRAAT ALLWLSCSIA LLRALATSNA RAQQRAAAQQ
RRSFLNAHHR SGAQVFPESP ESESDHEHEE ADLELSLPEC LEYEEEFDYE TESETESEIE
SETDFETEPE TAPTTEPETE PEDDRGPVVP KHSTFGQSLT QRLHALKLRS PDASPSRAPP
STQEPQSPRE GEELKPEDKD PRDPEESKEP KEEKQRRRCK PKKPTRRDAS PESPSKKGPI
PIRRH


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