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Neurosecretory protein VGF [Cleaved into: Neuroendocrine regulatory peptide-1 (NERP-1); Neuroendocrine regulatory peptide-2 (NERP-2); Antimicrobial peptide VGF[554-577]]

 VGF_HUMAN               Reviewed;         615 AA.
O15240; Q9UDW8;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
23-SEP-2008, sequence version 2.
27-SEP-2017, entry version 119.
RecName: Full=Neurosecretory protein VGF;
Contains:
RecName: Full=Neuroendocrine regulatory peptide-1;
Short=NERP-1;
Contains:
RecName: Full=Neuroendocrine regulatory peptide-2;
Short=NERP-2;
Contains:
RecName: Full=Antimicrobial peptide VGF[554-577];
Flags: Precursor;
Name=VGF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=9344675; DOI=10.1006/geno.1997.4945;
Canu N., Possenti R., Ricco A.S., Rocchi M., Levi A.;
"Cloning, structural organization analysis and chromosomal assignment
of the human gene for neurosecretory protein VGF.";
Genomics 45:443-446(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 554-577, FUNCTION, AND AMIDATION AT PRO-577.
PubMed=23250050; DOI=10.1074/mcp.M112.017400;
Sasaki K., Osaki T., Minamino N.;
"Large-scale identification of endogenous secretory peptides using
electron transfer dissociation mass spectrometry.";
Mol. Cell. Proteomics 12:700-709(2013).
[6]
FUNCTION OF PEPTIDES NERP-1 AND NERP-2, PYROGLUTAMATE FORMATION AT
GLN-310, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19194657; DOI=10.1007/s00018-009-8796-0;
Toshinai K., Nakazato M.;
"Neuroendocrine regulatory peptide-1 and -2: novel bioactive peptides
processed from VGF.";
Cell. Mol. Life Sci. 66:1939-1945(2009).
[7]
PHOSPHORYLATION AT SER-420 AND THR-424.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
-!- FUNCTION: May be involved in the regulation of cell-cell
interactions or in synatogenesis during the maturation of the
nervous system. {ECO:0000250}.
-!- FUNCTION: NERP peptides are involved in the control of body fluid
homeostasis by regulating vasopressin release.
{ECO:0000269|PubMed:19194657}.
-!- FUNCTION: Antimicrobial peptide VGF[554-577]: Has bactericidal
activity against M. luteus, and antifungal activity against P.
Pastoris. {ECO:0000269|PubMed:23250050}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19194657}.
Cytoplasmic vesicle, secretory vesicle
{ECO:0000269|PubMed:19194657}. Note=Stored in secretory vesicles
and then secreted, NERP peptides colocalize with vasopressin in
the storage granules of hypothalamus.
-!- TISSUE SPECIFICITY: Central and peripheral nervous systems,
synthesized exclusively in neuronal and neuroendocrine cells.
{ECO:0000269|PubMed:19194657}.
-!- PTM: Multiple peptides are derived from VGF, with activities in
synaptic plasticity, antidepression, penile erection, autonomic
activation, and increases in energy expenditure. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; Y12661; CAA73210.1; -; Genomic_DNA.
EMBL; AC004876; AAD45830.1; -; Genomic_DNA.
EMBL; CH471197; EAW50201.1; -; Genomic_DNA.
EMBL; BC063835; AAH63835.1; -; mRNA.
CCDS; CCDS5712.1; -.
RefSeq; NP_003369.2; NM_003378.3.
RefSeq; XP_005250618.1; XM_005250561.4.
RefSeq; XP_011514851.1; XM_011516549.2.
RefSeq; XP_016868068.1; XM_017012579.1.
UniGene; Hs.587325; -.
ProteinModelPortal; O15240; -.
SMR; O15240; -.
BioGrid; 113268; 5.
IntAct; O15240; 2.
STRING; 9606.ENSP00000249330; -.
iPTMnet; O15240; -.
PhosphoSitePlus; O15240; -.
BioMuta; VGF; -.
EPD; O15240; -.
MaxQB; O15240; -.
PaxDb; O15240; -.
PeptideAtlas; O15240; -.
PRIDE; O15240; -.
Ensembl; ENST00000249330; ENSP00000249330; ENSG00000128564.
Ensembl; ENST00000445482; ENSP00000400884; ENSG00000128564.
GeneID; 7425; -.
KEGG; hsa:7425; -.
UCSC; uc003uxx.5; human.
CTD; 7425; -.
DisGeNET; 7425; -.
EuPathDB; HostDB:ENSG00000128564.6; -.
GeneCards; VGF; -.
HGNC; HGNC:12684; VGF.
HPA; HPA055177; -.
HPA; HPA072505; -.
MIM; 602186; gene.
neXtProt; NX_O15240; -.
OpenTargets; ENSG00000128564; -.
PharmGKB; PA37305; -.
eggNOG; ENOG410IKTZ; Eukaryota.
eggNOG; ENOG410YR85; LUCA.
GeneTree; ENSGT00390000017745; -.
HOGENOM; HOG000120127; -.
HOVERGEN; HBG006806; -.
InParanoid; O15240; -.
OMA; NYIEHVL; -.
OrthoDB; EOG091G0H7O; -.
PhylomeDB; O15240; -.
TreeFam; TF338498; -.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
GenomeRNAi; 7425; -.
PRO; PR:O15240; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000128564; -.
CleanEx; HS_VGF; -.
ExpressionAtlas; O15240; baseline and differential.
Genevisible; O15240; HS.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005179; F:hormone activity; IBA:GO_Central.
GO; GO:0005184; F:neuropeptide hormone activity; IEA:Ensembl.
GO; GO:0033500; P:carbohydrate homeostasis; IBA:GO_Central.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0048167; P:regulation of synaptic plasticity; IBA:GO_Central.
GO; GO:0051591; P:response to cAMP; IEP:UniProtKB.
GO; GO:0009409; P:response to cold; IEA:Ensembl.
GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0019953; P:sexual reproduction; IEA:Ensembl.
InterPro; IPR026128; VGF.
PANTHER; PTHR15159; PTHR15159; 1.
1: Evidence at protein level;
Amidation; Antibiotic; Antimicrobial;
Cleavage on pair of basic residues; Complete proteome;
Cytoplasmic vesicle; Direct protein sequencing; Growth factor;
Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome;
Secreted; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 615 Neurosecretory protein VGF.
/FTId=PRO_0000022655.
PEPTIDE 281 306 Neuroendocrine regulatory peptide-1.
/FTId=PRO_0000403364.
PEPTIDE 310 347 Neuroendocrine regulatory peptide-2.
/FTId=PRO_0000403365.
PEPTIDE 554 577 Antimicrobial peptide VGF[554-577].
/FTId=PRO_0000422072.
COMPBIAS 353 447 Asp/Glu-rich (acidic).
MOD_RES 310 310 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:19194657}.
MOD_RES 420 420 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 424 424 Phosphothreonine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 577 577 Proline amide.
{ECO:0000269|PubMed:23250050}.
CONFLICT 129 131 PES -> AGE (in Ref. 1; CAA73210).
{ECO:0000305}.
CONFLICT 282 282 P -> A (in Ref. 1; CAA73210).
{ECO:0000305}.
CONFLICT 387 387 E -> EA (in Ref. 1; CAA73210).
{ECO:0000305}.
CONFLICT 393 393 E -> D (in Ref. 1; CAA73210).
{ECO:0000305}.
CONFLICT 481 481 K -> N (in Ref. 1; CAA73210).
{ECO:0000305}.
CONFLICT 485 485 N -> K (in Ref. 1; CAA73210).
{ECO:0000305}.
CONFLICT 512 515 APAP -> PPS (in Ref. 1; CAA73210).
{ECO:0000305}.
CONFLICT 585 586 RA -> HAQ (in Ref. 1; CAA73210).
{ECO:0000305}.
SEQUENCE 615 AA; 67258 MW; 198097C5622AC087 CRC64;
MKALRLSASA LFCLLLINGL GAAPPGRPEA QPPPLSSEHK EPVAGDAVPG PKDGSAPEVR
GARNSEPQDE GELFQGVDPR ALAAVLLQAL DRPASPPAPS GSQQGPEEEA AEALLTETVR
SQTHSLPAPE SPEPAAPPRP QTPENGPEAS DPSEELEALA SLLQELRDFS PSSAKRQQET
AAAETETRTH TLTRVNLESP GPERVWRASW GEFQARVPER APLPPPAPSQ FQARMPDSGP
LPETHKFGEG VSSPKTHLGE ALAPLSKAYQ GVAAPFPKAR RPESALLGGS EAGERLLQQG
LAQVEAGRRQ AEATRQAAAQ EERLADLASD LLLQYLLQGG ARQRGLGGRG LQEAAEERES
AREEEEAEQE RRGGEERVGE EDEEAAEAEA EAEEAERARQ NALLFAEEED GEAGAEDKRS
QEETPGHRRK EAEGTEEGGE EEDDEEMDPQ TIDSLIELST KLHLPADDVV SIIEEVEEKR
KRKKNAPPEP VPPPRAAPAP THVRSPQPPP PAPAPARDEL PDWNEVLPPW DREEDEVYPP
GPYHPFPNYI RPRTLQPPSA LRRRHYHHAL PPSRHYPGRE AQARRAQEEA EAEERRLQEQ
EELENYIEHV LLRRP


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