ID NPFF_HUMAN Reviewed; 113 AA. AC O15130; Q3SXL4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 07-SEP-2016, entry version 124. DE RecName: Full=Pro-FMRFamide-related neuropeptide FF; DE AltName: Full=FMRFamide-related peptides; DE Contains: DE RecName: Full=Neuropeptide SF; DE Short=NPSF; DE Contains: DE RecName: Full=Neuropeptide FF; DE Short=NPFF; DE Contains: DE RecName: Full=Neuropeptide AF; DE Short=NPAF; DE Flags: Precursor; GN Name=NPFF; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=9224703; DOI=10.1016/S0014-5793(97)00557-7; RA Perry S.J., Yi-Kung Huang E., Cronk D., Bagust J., Sharma R., RA Walker R.J., Wilson S., Burke J.F.; RT "A human gene encoding morphine modulating peptides related to NPFF RT and FMRFamide."; RL FEBS Lett. 409:426-430(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION. RX PubMed=11587714; DOI=10.1016/S0028-3908(01)00107-1; RA Catarsi S., Babinski K., Seguela P.; RT "Selective modulation of heteromeric ASIC proton-gated channels by RT neuropeptide FF."; RL Neuropharmacology 41:592-600(2001). CC -!- FUNCTION: Morphine modulating peptides. Have wide-ranging CC physiologic effects, including the modulation of morphine-induced CC analgesia, elevation of arterial blood pressure, and increased CC somatostatin secretion from the pancreas. Neuropeptide FF CC potentiates and sensitizes ASIC1 and ASIC3 channels. CC {ECO:0000269|PubMed:11587714}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O15130-1; Sequence=Displayed; CC Name=2; CC IsoId=O15130-2; Sequence=VSP_056475; CC Note=No experimental confirmation available.; CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF005271; AAB64288.1; -; mRNA. DR EMBL; AC023509; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471054; EAW96721.1; -; Genomic_DNA. DR EMBL; BC104234; AAI04235.1; -; mRNA. DR EMBL; BC104235; AAI04236.1; -; mRNA. DR CCDS; CCDS8862.1; -. [O15130-1] DR RefSeq; NP_001307225.1; NM_001320296.1. [O15130-2] DR RefSeq; NP_003708.1; NM_003717.3. [O15130-1] DR UniGene; Hs.733076; -. DR ProteinModelPortal; O15130; -. DR BioGrid; 114175; 1. DR IntAct; O15130; 1. DR STRING; 9606.ENSP00000267017; -. DR BioMuta; NPFF; -. DR PaxDb; O15130; -. DR PRIDE; O15130; -. DR Ensembl; ENST00000267017; ENSP00000267017; ENSG00000139574. [O15130-1] DR GeneID; 8620; -. DR KEGG; hsa:8620; -. DR UCSC; uc001sdw.1; human. [O15130-1] DR CTD; 8620; -. DR GeneCards; NPFF; -. DR HGNC; HGNC:7901; NPFF. DR MIM; 604643; gene. DR neXtProt; NX_O15130; -. DR PharmGKB; PA31704; -. DR eggNOG; ENOG410J2TH; Eukaryota. DR eggNOG; ENOG410Z134; LUCA. DR GeneTree; ENSGT00390000015021; -. DR HOGENOM; HOG000113843; -. DR HOVERGEN; HBG006519; -. DR InParanoid; O15130; -. DR KO; K05247; -. DR OMA; GLNSQFW; -. DR OrthoDB; EOG091G0YN1; -. DR PhylomeDB; O15130; -. DR TreeFam; TF330924; -. DR Reactome; R-HSA-389397; Orexin and neuropeptides FF and QRFP bind to their respective receptors. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR SIGNOR; O15130; -. DR GeneWiki; NPFF; -. DR GenomeRNAi; 8620; -. DR PRO; PR:O15130; -. DR Proteomes; UP000005640; Chromosome 12. DR CleanEx; HS_NPFF; -. DR Genevisible; O15130; HS. DR GO; GO:0043679; C:axon terminus; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0030425; C:dendrite; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0043204; C:perikaryon; IBA:GO_Central. DR GO; GO:0098794; C:postsynapse; IEA:GOC. DR GO; GO:0031982; C:vesicle; IEA:Ensembl. DR GO; GO:0001664; F:G-protein coupled receptor binding; IBA:GO_Central. DR GO; GO:0005184; F:neuropeptide hormone activity; IBA:GO_Central. DR GO; GO:0005102; F:receptor binding; TAS:ProtInc. DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IEA:Ensembl. DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc. DR GO; GO:0060079; P:excitatory postsynaptic potential; IBA:GO_Central. DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl. DR GO; GO:0032099; P:negative regulation of appetite; IEA:Ensembl. DR GO; GO:0010459; P:negative regulation of heart rate; IEA:Ensembl. DR GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl. DR GO; GO:0007218; P:neuropeptide signaling pathway; TAS:ProtInc. DR GO; GO:0045777; P:positive regulation of blood pressure; IEA:Ensembl. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl. DR GO; GO:0003254; P:regulation of membrane depolarization; IEA:Ensembl. DR GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0043278; P:response to morphine; IEA:Ensembl. DR GO; GO:0070253; P:somatostatin secretion; IEA:Ensembl. DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl. DR GO; GO:0030103; P:vasopressin secretion; IEA:Ensembl. DR InterPro; IPR008065; NPFF. DR PANTHER; PTHR15044:SF0; PTHR15044:SF0; 1. DR Pfam; PF15085; NPFF; 1. DR PIRSF; PIRSF038092; FMRFamid-rel_pep_precur; 1. DR PRINTS; PR01682; FMRFAMIDEPEP. PE 3: Inferred from homology; KW Alternative splicing; Amidation; Cleavage on pair of basic residues; KW Complete proteome; Neuropeptide; Polymorphism; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 20 {ECO:0000255}. FT PROPEP 21 65 FT /FTId=PRO_0000009898. FT PEPTIDE 66 76 Neuropeptide SF. FT /FTId=PRO_0000009899. FT PEPTIDE 69 76 Neuropeptide FF. FT /FTId=PRO_0000009900. FT PROPEP 79 92 FT /FTId=PRO_0000009901. FT PEPTIDE 93 110 Neuropeptide AF. FT /FTId=PRO_0000009902. FT MOD_RES 76 76 Phenylalanine amide. {ECO:0000250}. FT MOD_RES 110 110 Phenylalanine amide. {ECO:0000250}. FT VAR_SEQ 1 34 MDSRQAAALLVLLLLIDGGCAEGPGGQQEDQLSA -> MVP FT QPPTTCPWKPVPSPCDLRVQGICPSSFPDTPLAQ (in FT isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_056475. FT VARIANT 88 88 W -> R (in dbSNP:rs35822762). FT /FTId=VAR_049183. SQ SEQUENCE 113 AA; 12440 MW; 1E9D4ED2A69238E3 CRC64; MDSRQAAALL VLLLLIDGGC AEGPGGQQED QLSAEEDSEP LPPQDAQTSG SLLHYLLQAM ERPGRSQAFL FQPQRFGRNT QGSWRNEWLS PRAGEGLNSQ FWSLAAPQRF GKK //