NPY_XENLA
ID NPY_XENLA Reviewed; 97 AA.
AC P33689; Q68ET5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Pro-neuropeptide Y;
DE Contains:
DE RecName: Full=Neuropeptide Y;
DE AltName: Full=Neuropeptide tyrosine;
DE Short=NPY;
DE Contains:
DE RecName: Full=C-flanking peptide of NPY;
DE Short=CPON;
DE Flags: Precursor;
GN Name=npy;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8439344; DOI=10.1006/bbrc.1993.1141;
RA van Riel M.C.H.M., Tuinhof R., Roubos E.W., Martens G.J.M.;
RT "Cloning and sequence analysis of hypothalamic cDNA encoding Xenopus
RT preproneuropeptide Y.";
RL Biochem. Biophys. Res. Commun. 190:948-951(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9397931; DOI=10.1016/0303-7207(94)90213-5;
RA Griffin D., Minth C.D., Taylor W.L.;
RT "Isolation and characterization of the Xenopus laevis cDNA and genomic
RT homologs of neuropeptide Y.";
RL Mol. Cell. Endocrinol. 101:1-10(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: NPY is implicated in the control of feeding and in secretion
CC of gonadotrophin-release hormone.
CC -!- SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle,
CC neuronal dense core vesicle {ECO:0000250|UniProtKB:P07808}.
CC -!- SIMILARITY: Belongs to the NPY family. {ECO:0000305}.
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DR EMBL; L11294; AAA49913.1; -; mRNA.
DR EMBL; L07413; AAA49917.1; -; mRNA.
DR EMBL; S55577; AAB25447.1; -; mRNA.
DR EMBL; L11296; AAA49914.1; -; mRNA.
DR EMBL; BC080115; AAH80115.1; -; mRNA.
DR PIR; JC1460; JC1460.
DR RefSeq; NP_001081300.1; NM_001087831.1.
DR RefSeq; NP_001161232.1; NM_001167760.1.
DR AlphaFoldDB; P33689; -.
DR DNASU; 397763; -.
DR GeneID; 397763; -.
DR GeneID; 780752; -.
DR KEGG; xla:397763; -.
DR KEGG; xla:780752; -.
DR CTD; 397763; -.
DR CTD; 780752; -.
DR Xenbase; XB-GENE-6254241; npy.L.
DR Xenbase; XB-GENE-942364; npy.S.
DR OMA; QGTMRLW; -.
DR OrthoDB; 1542445at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 397763; Expressed in brain and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0098992; C:neuronal dense core vesicle; ISS:UniProtKB.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00126; PAH; 1.
DR InterPro; IPR001955; Pancreatic_hormone-like.
DR InterPro; IPR020392; Pancreatic_hormone-like_CS.
DR PANTHER; PTHR10533; PTHR10533; 1.
DR Pfam; PF00159; Hormone_3; 1.
DR PRINTS; PR00278; PANCHORMONE.
DR SMART; SM00309; PAH; 1.
DR PROSITE; PS00265; PANCREATIC_HORMONE_1; 1.
DR PROSITE; PS50276; PANCREATIC_HORMONE_2; 1.
PE 3: Inferred from homology;
KW Amidation; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Neuropeptide; Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT PEPTIDE 29..64
FT /note="Neuropeptide Y"
FT /id="PRO_0000025353"
FT PEPTIDE 68..97
FT /note="C-flanking peptide of NPY"
FT /id="PRO_0000025354"
FT MOD_RES 64
FT /note="Tyrosine amide"
FT /evidence="ECO:0000250"
FT CONFLICT 38
FT /note="E -> D (in Ref. 2; AAA49914)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="S -> C (in Ref. 2; AAA49914)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="N -> S (in Ref. 2; AAA49914)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 97 AA; 11378 MW; 48BD85D3E6A463E6 CRC64;
MQGNMRLWMS VLTLCLSMLI CLGTFAEAYP SKPDNPGEDA PAEDMAKYYS ALRHYINLIT
RQRYGKRSSP ETMLSDVWWR ENTENIPRSR FEDPPMW