VGF_BOVIN
ID VGF_BOVIN Reviewed; 618 AA.
AC P86435;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 29-SEP-2021, entry version 46.
DE RecName: Full=Neurosecretory protein VGF {ECO:0000250|UniProtKB:P20156};
DE Contains:
DE RecName: Full=Peptide V {ECO:0000303|PubMed:7988466};
DE AltName: Full=AQEE-30;
DE AltName: Full=VGF-derived peptide {ECO:0000303|PubMed:7988466};
DE Contains:
DE RecName: Full=Neuroendocrine regulatory peptide-1;
DE Short=NERP-1;
DE Contains:
DE RecName: Full=Neuroendocrine regulatory peptide-2;
DE Short=NERP-2;
DE Flags: Precursor;
GN Name=VGF {ECO:0000250|UniProtKB:P20156};
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}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000269|PubMed:19390049};
RX PubMed=19390049; DOI=10.1126/science.1169588;
RG The bovine genome sequencing and analysis consortium;
RT "The genome sequence of taurine cattle: a window to ruminant biology and
RT evolution.";
RL Science 324:522-528(2009).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 390-502.
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 481-618.
RC STRAIN=Hereford; TISSUE=Brain;
RX PubMed=17087818; DOI=10.1186/1471-2164-7-283;
RA Jann O.C., Aerts J., Jones M., Hastings N., Law A., McKay S., Marques E.,
RA Prasad A., Yu J., Moore S.S., Floriot S., Mahe M.F., Eggen A., Silveri L.,
RA Negrini R., Milanesi E., Ajmone-Marsan P., Valentini A., Marchitelli C.,
RA Savarese M.C., Janitz M., Herwig R., Hennig S., Gorni C., Connor E.E.,
RA Sonstegard T.S., Smith T., Drogemuller C., Williams J.L.;
RT "A second generation radiation hybrid map to aid the assembly of the bovine
RT genome sequence.";
RL BMC Genomics 7:283-283(2006).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 589-618, AND MASS SPECTROMETRY.
RC TISSUE=Pituitary {ECO:0000269|PubMed:7988466};
RX PubMed=7988466; DOI=10.1210/endo.135.6.7988466;
RA Liu J.W., Andrews P.C., Mershon J.L., Yan C., Allen D.L., Ben-Jonathan N.;
RT "Peptide V: a VGF-derived neuropeptide purified from bovine posterior
RT pituitary.";
RL Endocrinology 135:2742-2748(1994).
RN [5] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Colgrave M.L., Xi L., Lehnert S., Wijffels G.;
RT "Neuropeptidomics of the bovine hypothalamus.";
RL Submitted (DEC-2009) to UniProtKB.
CC -!- FUNCTION: [Neurosecretory protein VGF]: Secreted polyprotein that is
CC packaged and proteolytically processed by prohormone convertases PCSK1
CC and PCSK2 in a cell-type-specific manner (By similarity). VGF and
CC peptides derived from its processing play many roles in neurogenesis
CC and neuroplasticity associated with learning, memory, depression and
CC chronic pain (By similarity). {ECO:0000250|UniProtKB:P20156}.
CC -!- FUNCTION: [Neuroendocrine regulatory peptide-1]: Plays a role in the
CC control of body fluid homeostasis by regulating vasopressin release.
CC Suppresses presynaptic glutamatergic neurons connected to vasopressin
CC neurons. {ECO:0000250|UniProtKB:P20156}.
CC -!- FUNCTION: [Neuroendocrine regulatory peptide-2]: Plays a role in the
CC control of body fluid homeostasis by regulating vasopressin release.
CC Activates GABAergic interneurons which are inhibitory neurons of the
CC nervous system and thereby suppresses presynaptic glutamatergic neurons
CC (By similarity). Stimulates also feeding behavior in an orexin-
CC dependent manner in the hypothalamus (By similarity). Functions as a
CC positive regulator for the activation of orexin neurons resulting in
CC elevated gastric acid secretion and gastric emptying (By similarity).
CC {ECO:0000250|UniProtKB:P20156}.
CC -!- SUBCELLULAR LOCATION: [Neurosecretory protein VGF]: Secreted
CC {ECO:0000250|UniProtKB:O15240}. Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000250|UniProtKB:O15240}. Note=Stored in secretory vesicles and
CC then secreted, NERP peptides colocalize with vasopressin in the storage
CC granules of hypothalamus. {ECO:0000250|UniProtKB:O15240}.
CC -!- PTM: Multiple peptides are derived from VGF, with activities in
CC synaptic plasticity, antidepression, penile erection, autonomic
CC activation, and increases in energy expenditure. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: [Peptide V]: Mass=3706.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7988466};
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DR EMBL; AAFC03118060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAFC03131609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DV909837; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CO873651; -; NOT_ANNOTATED_CDS; mRNA.
DR STRING; 9913.ENSBTAP00000013014; -.
DR PaxDb; P86435; -.
DR PeptideAtlas; P86435; -.
DR eggNOG; ENOG502S5N4; Eukaryota.
DR InParanoid; P86435; -.
DR OrthoDB; 1064302at2759; -.
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:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR InterPro; IPR026128; VGF.
DR PANTHER; PTHR15159; PTHR15159; 1.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Coiled coil;
KW Cytoplasmic vesicle; Direct protein sequencing; Growth factor;
KW Phosphoprotein; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..618
FT /note="Neurosecretory protein VGF"
FT /id="PRO_0000391696"
FT PEPTIDE 282..306
FT /note="Neuroendocrine regulatory peptide-1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403375"
FT PEPTIDE 310..347
FT /note="Neuroendocrine regulatory peptide-2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000403376"
FT PEPTIDE 589..618
FT /note="Peptide V"
FT /id="PRO_0000391697"
FT REGION 21..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 301..332
FT /evidence="ECO:0000255"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..236
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..454
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 310
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:O15240"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15240"
FT MOD_RES 425
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15240"
FT CONFLICT 422
FT /note="R -> Q (in Ref. 2; DV909837)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="V -> E (in Ref. 3; CO873651)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="A -> K (in Ref. 3; CO873651)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="V -> G (in Ref. 3; CO873651)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="R -> G (in Ref. 3; CO873651)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 618 AA; 67620 MW; 02B75828423DFCD3 CRC64;
MKSLRLPATV LFCLLLLIKG LGAAPPGHPE AQPPPPSSEH KEPVAGDAVL GSKDVSALEV
RAARNSEPQD EGELFQGVDP RALAAVLLQA LDRPASPPAP GGSQQRPEEE TAESLLTETV
RSQTHSLPVP ETQAPAAPPR PQTQENGAEA PDPSEELEAL ASLLQELRDF SPSSAKRQQE
TAAAETETRT HTLTRVNLES PGPERVWRAS WGEFQARVPE RAPLPPPAPP QFQARVPESG
PLPEAHQFGG GSSPKTHLGE ALAPLSKAYQ GLAAPFPKAR RPETSLLGGT EAGERLLQQG
LAQVEAGRRQ AEATRQAAAQ EERLADLASD LLLQYLLQGG ARQRGLGGRG LQEEEGGGRE
TARQQEEAEQ ERRGGEERVG EEDEEAAEAE AEAEEAERAR QNALLFAEEE EGEAGAEDKR
SREETPGHRR KEAEGAEEGG AEDEDDDEEM DPQTIDSLIE LSTKLHLPAD DVVSIIEEVE
EKRKRKKNAP PEPVPPPRAA PAPTHARSPK TPPPAPAPDR EELPDGNEEL PPRDRXENEV
FSPVPYHPFP NYIRARTVQP PPASRRRHYH HALPPSRHYP DREAQARRAQ EEAEAEERRL
QEQEELENYI EHVLLRRP
