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O15130

- NPFF_HUMAN

UniProt

O15130 - NPFF_HUMAN

Protein

Pro-FMRFamide-related neuropeptide FF

Gene

NPFF

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
  1. Functioni

    Morphine modulating peptides. Have wide-ranging physiologic effects, including the modulation of morphine-induced analgesia, elevation of arterial blood pressure, and increased somatostatin secretion from the pancreas. Neuropeptide FF potentiates and sensitizes ASIC1 and ASIC3 channels.1 Publication

    GO - Molecular functioni

    1. receptor binding Source: ProtInc

    GO - Biological processi

    1. acute inflammatory response to antigenic stimulus Source: Ensembl
    2. maternal process involved in female pregnancy Source: Ensembl
    3. negative regulation of appetite Source: Ensembl
    4. negative regulation of heart rate Source: Ensembl
    5. negative regulation of insulin secretion Source: Ensembl
    6. neuropeptide signaling pathway Source: ProtInc
    7. positive regulation of blood pressure Source: Ensembl
    8. positive regulation of cytosolic calcium ion concentration Source: Ensembl
    9. regulation of excitatory postsynaptic membrane potential Source: Ensembl
    10. regulation of membrane depolarization Source: Ensembl
    11. regulation of sensory perception of pain Source: Ensembl
    12. response to drug Source: Ensembl
    13. response to morphine Source: Ensembl
    14. somatostatin secretion Source: Ensembl
    15. spinal cord development Source: Ensembl
    16. synaptic transmission Source: ProtInc
    17. vasopressin secretion Source: Ensembl

    Keywords - Molecular functioni

    Neuropeptide

    Enzyme and pathway databases

    ReactomeiREACT_16973. Orexin and neuropeptides FF and QRFP bind to their respective receptors.
    REACT_18283. G alpha (q) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pro-FMRFamide-related neuropeptide FF
    Alternative name(s):
    FMRFamide-related peptides
    Cleaved into the following 3 chains:
    Neuropeptide SF
    Short name:
    NPSF
    Neuropeptide FF
    Short name:
    NPFF
    Neuropeptide AF
    Short name:
    NPAF
    Gene namesi
    Name:NPFF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:7901. NPFF.

    Subcellular locationi

    GO - Cellular componenti

    1. axon terminus Source: Ensembl
    2. dendrite Source: Ensembl
    3. extracellular region Source: Reactome
    4. extracellular space Source: Ensembl
    5. perikaryon Source: Ensembl
    6. vesicle Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31704.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 6545PRO_0000009898Add
    BLAST
    Peptidei66 – 7611Neuropeptide SFPRO_0000009899Add
    BLAST
    Peptidei69 – 768Neuropeptide FFPRO_0000009900
    Propeptidei79 – 9214PRO_0000009901Add
    BLAST
    Peptidei93 – 11018Neuropeptide AFPRO_0000009902Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei76 – 761Phenylalanine amideBy similarity
    Modified residuei110 – 1101Phenylalanine amideBy similarity

    Keywords - PTMi

    Amidation, Cleavage on pair of basic residues

    Proteomic databases

    PaxDbiO15130.
    PRIDEiO15130.

    Expressioni

    Gene expression databases

    BgeeiO15130.
    CleanExiHS_NPFF.
    GenevestigatoriO15130.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000267017.

    Structurei

    3D structure databases

    ProteinModelPortaliO15130.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG44970.
    HOGENOMiHOG000113843.
    HOVERGENiHBG006519.
    InParanoidiO15130.
    KOiK05247.
    OMAiDSHERWG.
    OrthoDBiEOG75B87K.
    PhylomeDBiO15130.
    TreeFamiTF330924.

    Family and domain databases

    InterProiIPR008065. FMRFamid-related_peptide.
    [Graphical view]
    PANTHERiPTHR15044. PTHR15044. 1 hit.
    PfamiPF15085. NPFF. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038092. FMRFamid-rel_pep_precur. 1 hit.
    PRINTSiPR01682. FMRFAMIDEPEP.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O15130-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDSRQAAALL VLLLLIDGGC AEGPGGQQED QLSAEEDSEP LPPQDAQTSG    50
    SLLHYLLQAM ERPGRSQAFL FQPQRFGRNT QGSWRNEWLS PRAGEGLNSQ 100
    FWSLAAPQRF GKK 113
    Length:113
    Mass (Da):12,440
    Last modified:January 1, 1998 - v1
    Checksum:i1E9D4ED2A69238E3
    GO
    Isoform 2 (identifier: O15130-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: MDSRQAAALLVLLLLIDGGCAEGPGGQQEDQLSA → MVPQPPTTCPWKPVPSPCDLRVQGICPSSFPDTPLAQ

    Note: No experimental confirmation available.

    Show »
    Length:116
    Mass (Da):12,991
    Checksum:i0E1EB094309C3105
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti88 – 881W → R.
    Corresponds to variant rs35822762 [ dbSNP | Ensembl ].
    VAR_049183

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3434MDSRQ…DQLSA → MVPQPPTTCPWKPVPSPCDL RVQGICPSSFPDTPLAQ in isoform 2. 1 PublicationVSP_056475Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005271 mRNA. Translation: AAB64288.1.
    AC023509 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96721.1.
    BC104234 mRNA. Translation: AAI04235.1.
    BC104235 mRNA. Translation: AAI04236.1.
    CCDSiCCDS8862.1.
    RefSeqiNP_003708.1. NM_003717.2.
    XP_005269263.1. XM_005269206.2.
    UniGeneiHs.733076.

    Genome annotation databases

    EnsembliENST00000267017; ENSP00000267017; ENSG00000139574.
    ENST00000609999; ENSP00000476489; ENSG00000139574.
    GeneIDi8620.
    KEGGihsa:8620.
    UCSCiuc001sdw.1. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005271 mRNA. Translation: AAB64288.1 .
    AC023509 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW96721.1 .
    BC104234 mRNA. Translation: AAI04235.1 .
    BC104235 mRNA. Translation: AAI04236.1 .
    CCDSi CCDS8862.1.
    RefSeqi NP_003708.1. NM_003717.2.
    XP_005269263.1. XM_005269206.2.
    UniGenei Hs.733076.

    3D structure databases

    ProteinModelPortali O15130.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000267017.

    Proteomic databases

    PaxDbi O15130.
    PRIDEi O15130.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267017 ; ENSP00000267017 ; ENSG00000139574 .
    ENST00000609999 ; ENSP00000476489 ; ENSG00000139574 .
    GeneIDi 8620.
    KEGGi hsa:8620.
    UCSCi uc001sdw.1. human.

    Organism-specific databases

    CTDi 8620.
    GeneCardsi GC12M053896.
    HGNCi HGNC:7901. NPFF.
    MIMi 604643. gene.
    neXtProti NX_O15130.
    PharmGKBi PA31704.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44970.
    HOGENOMi HOG000113843.
    HOVERGENi HBG006519.
    InParanoidi O15130.
    KOi K05247.
    OMAi DSHERWG.
    OrthoDBi EOG75B87K.
    PhylomeDBi O15130.
    TreeFami TF330924.

    Enzyme and pathway databases

    Reactomei REACT_16973. Orexin and neuropeptides FF and QRFP bind to their respective receptors.
    REACT_18283. G alpha (q) signalling events.

    Miscellaneous databases

    GeneWikii NPFF.
    GenomeRNAii 8620.
    NextBioi 32299.
    PROi O15130.
    SOURCEi Search...

    Gene expression databases

    Bgeei O15130.
    CleanExi HS_NPFF.
    Genevestigatori O15130.

    Family and domain databases

    InterProi IPR008065. FMRFamid-related_peptide.
    [Graphical view ]
    PANTHERi PTHR15044. PTHR15044. 1 hit.
    Pfami PF15085. NPFF. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038092. FMRFamid-rel_pep_precur. 1 hit.
    PRINTSi PR01682. FMRFAMIDEPEP.
    ProtoNeti Search...

    Publicationsi

    1. "A human gene encoding morphine modulating peptides related to NPFF and FMRFamide."
      Perry S.J., Yi-Kung Huang E., Cronk D., Bagust J., Sharma R., Walker R.J., Wilson S., Burke J.F.
      FEBS Lett. 409:426-430(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. "Selective modulation of heteromeric ASIC proton-gated channels by neuropeptide FF."
      Catarsi S., Babinski K., Seguela P.
      Neuropharmacology 41:592-600(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiNPFF_HUMAN
    AccessioniPrimary (citable) accession number: O15130
    Secondary accession number(s): Q3SXL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3