ID   NPW_HUMAN               Reviewed;         165 AA.
AC   Q8N729;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 2.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Neuropeptide W;
DE   AltName: Full=Preproprotein L8;
DE            Short=hPPL8;
DE   Contains:
DE     RecName: Full=Neuropeptide W-23;
DE              Short=NPW23;
DE              Short=hL8;
DE   Contains:
DE     RecName: Full=Neuropeptide W-30;
DE              Short=NPW30;
DE              Short=hL8C;
DE   Flags: Precursor;
GN   Name=NPW; Synonyms=PPL8, PPNPW;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND SYNTHESIS OF NPW23 AND
RP   NPW30.
RX   PubMed=12130646; DOI=10.1074/jbc.m205337200;
RA   Shimomura Y., Harada M., Goto M., Sugo T., Matsumoto Y., Abe M.,
RA   Watanabe T., Asami T., Kitada C., Mori M., Onda H., Fujino M.;
RT   "Identification of neuropeptide W as the endogenous ligand for orphan G-
RT   protein-coupled receptors GPR7 and GPR8.";
RL   J. Biol. Chem. 277:35826-35832(2002).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=12401809; DOI=10.1074/jbc.m206396200;
RA   Brezillon S., Lannoy V., Franssen J.-D., Le Poul E., Dupriez V.,
RA   Lucchetti J., Detheux M., Parmentier M.;
RT   "Identification of natural ligands for the orphan G protein-coupled
RT   receptors GPR7 and GPR8.";
RL   J. Biol. Chem. 278:776-783(2003).
RN   [3]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-133.
RX   PubMed=25326458; DOI=10.1074/mcp.m114.043703;
RA   Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L.,
RA   Nilsson J., Larson G.;
RT   "Identification of chondroitin sulfate linkage region glycopeptides reveals
RT   prohormones as a novel class of proteoglycans.";
RL   Mol. Cell. Proteomics 14:41-49(2015).
RN   [4]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-133.
RX   PubMed=36213313; DOI=10.1007/s42485-022-00092-3;
RA   Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K.,
RA   Pandey A.;
RT   "Mass spectrometric analysis of chondroitin sulfate-linked peptides.";
RL   J. Proteins Proteom. 13:187-203(2022).
RN   [5]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-133.
RX   PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617;
RA   Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.;
RT   "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected
RT   Correlation Between Glycan Sulfation and Attachment Site Characteristics.";
RL   Mol. Cell. Proteomics 22:100617-100617(2023).
CC   -!- FUNCTION: Plays a regulatory role in the organization of neuroendocrine
CC       signals accessing the anterior pituitary gland. Stimulates water
CC       drinking and food intake. May play a role in the hypothalamic response
CC       to stress (By similarity). NPW23 activates GPR7 and GPR8 more
CC       efficiently than NPW30. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25326458,
CC       ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}.
CC   -!- TISSUE SPECIFICITY: Detected in cerebrospinal fluid and urine (at
CC       protein level) (PubMed:25326458, PubMed:36213313, PubMed:37453717).
CC       Detected at high levels in the substantia nigra, fetal kidney and
CC       trachea; at lower levels in testis, uterus, ovary and placenta. Not
CC       detectable in many regions of the central nervous system. Also detected
CC       at high levels in lymphoblastic leukemia and colorectal adenocarcinoma.
CC       {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313,
CC       ECO:0000269|PubMed:37453717}.
CC   -!- SIMILARITY: Belongs to the neuropeptide B/W family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC07172.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB084276; BAC07172.1; ALT_INIT; mRNA.
DR   CCDS; CCDS42102.1; -.
DR   RefSeq; NP_001092926.2; NM_001099456.2.
DR   AlphaFoldDB; Q8N729; -.
DR   BioGRID; 129692; 43.
DR   STRING; 9606.ENSP00000456974; -.
DR   GlyGen; Q8N729; 1 site.
DR   PhosphoSitePlus; Q8N729; -.
DR   BioMuta; NPW; -.
DR   jPOST; Q8N729; -.
DR   MassIVE; Q8N729; -.
DR   PaxDb; 9606-ENSP00000330070; -.
DR   PeptideAtlas; Q8N729; -.
DR   ProteomicsDB; 72259; -.
DR   Antibodypedia; 54421; 125 antibodies from 17 providers.
DR   DNASU; 283869; -.
DR   Ensembl; ENST00000566435.4; ENSP00000456974.3; ENSG00000183971.10.
DR   Ensembl; ENST00000709296.1; ENSP00000517604.1; ENSG00000291946.1.
DR   GeneID; 283869; -.
DR   KEGG; hsa:283869; -.
DR   MANE-Select; ENST00000566435.4; ENSP00000456974.3; NM_001099456.3; NP_001092926.2.
DR   UCSC; uc059pez.1; human.
DR   AGR; HGNC:30509; -.
DR   CTD; 283869; -.
DR   DisGeNET; 283869; -.
DR   GeneCards; NPW; -.
DR   HGNC; HGNC:30509; NPW.
DR   HPA; ENSG00000183971; Tissue enhanced (liver).
DR   MIM; 607997; gene.
DR   neXtProt; NX_Q8N729; -.
DR   OpenTargets; ENSG00000183971; -.
DR   PharmGKB; PA142671248; -.
DR   VEuPathDB; HostDB:ENSG00000183971; -.
DR   eggNOG; ENOG502SW0V; Eukaryota.
DR   GeneTree; ENSGT00940000158204; -.
DR   HOGENOM; CLU_121719_0_0_1; -.
DR   InParanoid; Q8N729; -.
DR   OMA; SGAWYKH; -.
DR   OrthoDB; 5324516at2759; -.
DR   PhylomeDB; Q8N729; -.
DR   TreeFam; TF333179; -.
DR   PathwayCommons; Q8N729; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; Q8N729; -.
DR   BioGRID-ORCS; 283869; 15 hits in 1141 CRISPR screens.
DR   ChiTaRS; NPW; human.
DR   GeneWiki; NPW; -.
DR   GenomeRNAi; 283869; -.
DR   Pharos; Q8N729; Tbio.
DR   PRO; PR:Q8N729; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q8N729; Protein.
DR   Bgee; ENSG00000183971; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 91 other cell types or tissues.
DR   ExpressionAtlas; Q8N729; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR   GO; GO:0007631; P:feeding behavior; IDA:HGNC-UCL.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:HGNC-UCL.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR013297; Neuropept_BW_pre.
DR   InterPro; IPR013299; Neuropept_W_pre.
DR   PANTHER; PTHR28553; NEUROPEPTIDE B; 1.
DR   PANTHER; PTHR28553:SF2; NEUROPEPTIDE W; 1.
DR   Pfam; PF15180; NPBW; 1.
DR   PRINTS; PR01888; NROPEPTIDEBW.
DR   PRINTS; PR01890; PPNRPEPTIDEW.
DR   Genevisible; Q8N729; HS.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Glycoprotein; Neuropeptide;
KW   Proteoglycan; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         33..62
FT                   /note="Neuropeptide W-30"
FT                   /id="PRO_0000019843"
FT   PEPTIDE         33..55
FT                   /note="Neuropeptide W-23"
FT                   /id="PRO_0000019844"
FT   PROPEP          65..165
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000019845"
FT   REGION          106..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        133
FT                   /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT                   /evidence="ECO:0000269|PubMed:25326458,
FT                   ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717"
FT   VARIANT         149
FT                   /note="D -> A (in dbSNP:rs2286472)"
FT                   /id="VAR_050292"
SQ   SEQUENCE   165 AA;  18048 MW;  F426AF4B7FB6E604 CRC64;
     MAWRPGERGA PASRPRLALL LLLLLLPLPS GAWYKHVASP RYHTVGRAAG LLMGLRRSPY
     LWRRALRAAA GPLARDTLSP EPAAREAPLL LPSWVQELWE TRRRSSQAGI PVRAPRSPRA
     PEPALEPESL DFSGAGQRLR RDVSRPAVDP AANRLGLPCL APGPF
//