NPVF_SHEEP
ID NPVF_SHEEP Reviewed; 196 AA.
AC B2KKR4; A8VJ96; B2LT47;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Pro-FMRFamide-related neuropeptide VF;
DE AltName: Full=FMRFamide-related peptides {ECO:0000250|UniProtKB:Q9HCQ7};
DE Contains:
DE RecName: Full=Neuropeptide NPSF {ECO:0000250|UniProtKB:Q9HCQ7};
DE Contains:
DE RecName: Full=Neuropeptide RFRP-1 {ECO:0000250|UniProtKB:Q9HCQ7};
DE Contains:
DE RecName: Full=Neuropeptide RFRP-2 {ECO:0000250|UniProtKB:Q9HCQ7};
DE Contains:
DE RecName: Full=Neuropeptide NPVF {ECO:0000250|UniProtKB:Q9HCQ7};
DE AltName: Full=Neuropeptide RFRP-3 {ECO:0000303|PubMed:18617613, ECO:0000303|PubMed:19808777};
DE Flags: Precursor;
GN Name=NPVF {ECO:0000250|UniProtKB:Q9HCQ7};
GN Synonyms=RFRP {ECO:0000312|EMBL:ABS44877.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABS44877.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=18752651; DOI=10.1111/j.1365-2826.2008.01784.x;
RA Dardente H., Birnie M., Lincoln G.A., Hazlerigg D.G.;
RT "RFamide-related peptide and its cognate receptor in the sheep: cDNA
RT cloning, mRNA distribution in the hypothalamus and the effect of
RT photoperiod.";
RL J. Neuroendocrinol. 20:1252-1259(2008).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABW24663.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-161, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18617612; DOI=10.1210/en.2008-0581;
RA Smith J.T., Coolen L.M., Kriegsfeld L.J., Sari I.P.,
RA Jaafarzadehshirazi M.R., Maltby M., Bateman K., Goodman R.L.,
RA Tilbrook A.J., Ubuka T., Bentley G.E., Clarke I.J., Lehman M.N.;
RT "Variation in kisspeptin and RFamide-related peptide (RFRP) expression and
RT terminal connections to gonadotropin-releasing hormone neurons in the
RT brain: a novel medium for seasonal breeding in the sheep.";
RL Endocrinology 149:5770-5782(2008).
RN [3] {ECO:0000305, ECO:0000312|EMBL:ACB87372.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-183.
RC TISSUE=Brain {ECO:0000312|EMBL:ACB87372.1};
RA Arreguin-Arevalo J.A., Nett T.M.;
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18617613; DOI=10.1210/en.2008-0575;
RA Clarke I.J., Sari I.P., Qi Y., Smith J.T., Parkington H.C., Ubuka T.,
RA Iqbal J., Li Q., Tilbrook A., Morgan K., Pawson A.J., Tsutsui K.,
RA Millar R.P., Bentley G.E.;
RT "Potent action of RFamide-related peptide-3 on pituitary gonadotropes
RT indicative of a hypophysiotropic role in the negative regulation of
RT gonadotropin secretion.";
RL Endocrinology 149:5811-5821(2008).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=19808777; DOI=10.1210/en.2009-0775;
RA Sari I.P., Rao A., Smith J.T., Tilbrook A.J., Clarke I.J.;
RT "Effect of RF-amide-related peptide-3 on luteinizing hormone and follicle-
RT stimulating hormone synthesis and secretion in ovine pituitary
RT gonadotropes.";
RL Endocrinology 150:5549-5556(2009).
CC -!- FUNCTION: Neuropeptide RFRP-1 acts as a potent negative regulator of
CC gonadotropin synthesis and secretion. Neuropeptides NPSF and NPVF
CC efficiently inhibit forskolin-induced production of cAMP, but RFRP-2
CC shows no inhibitory activity. Neuropeptide NPVF blocks morphine-induced
CC analgesia (By similarity). May act in concert with kisspeptin, through
CC opposing affects, to regulate the activity of gonadotropin-releasing
CC hormone (GnRH) neurons across the seasons, leading to an annual change
CC in fertility and the cyclical seasonal transition from non-breeding to
CC breeding season. {ECO:0000250, ECO:0000269|PubMed:18617612,
CC ECO:0000269|PubMed:18617613, ECO:0000269|PubMed:19808777}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in hypothalamus, where it is localized to
CC the dorsomedial hypothalamic nucleus (DMH), paraventricular nucleus
CC (PVN), and to neuronal projections from the PVN to the neurosecretory
CC zone of the median eminence. {ECO:0000269|PubMed:18617612,
CC ECO:0000269|PubMed:18617613, ECO:0000269|PubMed:18752651}.
CC -!- INDUCTION: Expression moderately increased by a longer photoperiod.
CC {ECO:0000269|PubMed:18752651}.
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000255}.
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DR EMBL; EF494241; ABS44877.1; -; mRNA.
DR EMBL; EU177779; ABW24663.1; -; mRNA.
DR EMBL; EU580134; ACB87372.1; -; mRNA.
DR RefSeq; NP_001120740.1; NM_001127268.1.
DR AlphaFoldDB; B2KKR4; -.
DR STRING; 9940.ENSOARP00000010970; -.
DR Ensembl; ENSOART00000011128; ENSOARP00000010970; ENSOARG00000010230.
DR GeneID; 100127217; -.
DR KEGG; oas:100127217; -.
DR CTD; 64111; -.
DR eggNOG; ENOG502S5H9; Eukaryota.
DR HOGENOM; CLU_120051_0_0_1; -.
DR OMA; NKMPHSA; -.
DR OrthoDB; 1553087at2759; -.
DR Proteomes; UP000002356; Chromosome 4.
DR Bgee; ENSOARG00000010230; Expressed in ovary and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032277; P:negative regulation of gonadotropin secretion; IEA:Ensembl.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR026297; FMRFamide-related/fGRP.
DR PANTHER; PTHR14403; PTHR14403; 1.
PE 2: Evidence at transcript level;
KW Amidation; Cleavage on pair of basic residues; Neuropeptide;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..57
FT /evidence="ECO:0000255"
FT /id="PRO_0000401173"
FT PEPTIDE 58..92
FT /note="Neuropeptide NPSF"
FT /evidence="ECO:0000250"
FT /id="PRO_0000401174"
FT PEPTIDE 81..92
FT /note="Neuropeptide RFRP-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000401175"
FT PROPEP 95..99
FT /evidence="ECO:0000255"
FT /id="PRO_0000401176"
FT PEPTIDE 101..112
FT /note="Neuropeptide RFRP-2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000401177"
FT PROPEP 115..121
FT /evidence="ECO:0000255"
FT /id="PRO_0000401178"
FT PEPTIDE 124..131
FT /note="Neuropeptide NPVF"
FT /evidence="ECO:0000250|UniProtKB:Q9HCQ7"
FT /id="PRO_0000401179"
FT PROPEP 134..196
FT /evidence="ECO:0000255"
FT /id="PRO_0000401180"
FT MOD_RES 92
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9HCQ7"
FT MOD_RES 131
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:Q9HCQ7"
FT CONFLICT 32..34
FT /note="IPS -> MPN (in Ref. 3; ACB87372)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="L -> R (in Ref. 3; ACB87372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 196 AA; 22525 MW; 17DC3AA77CDB3A11 CRC64;
MEIISLKRFI LLMLATSSLL TSNIFCTDES RIPSLYSKKN YDKYSEPRGD LGWEKERSLT
FEEVKDWGPK IKMNTPAVNK MPPSAANLPL RFGRNMEEER STRVMAHLPL RLGKNREDSL
SRRVPNLPQR FGRTIAAKSI TKTLSNLLQQ SMHSPSTNGL LYSMTCRPQE IQNPGQKNLR
RLGFQKIDDA ELKQEK
