ID   SNPF_AGRIP              Reviewed;         139 AA.
AC   C0HKV9; C0HKW0; C0HKW1;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Short neuropeptide F {ECO:0000305|PubMed:29466015};
DE            Short=sNPF {ECO:0000305|PubMed:29466015};
DE   Contains:
DE     RecName: Full=sNPF peptide 1 {ECO:0000305|PubMed:29466015};
DE              Short=sNPF-1 {ECO:0000303|PubMed:29466015};
DE   Contains:
DE     RecName: Full=sNPF peptide 2 {ECO:0000305|PubMed:29466015};
DE              Short=sNPF-2 {ECO:0000303|PubMed:29466015};
DE   Contains:
DE     RecName: Full=sNPF peptide 3 {ECO:0000305|PubMed:29466015};
DE              Short=sNPF-3 {ECO:0000303|PubMed:29466015};
OS   Agrotis ipsilon (Black cutworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Noctuinae; Noctuini; Agrotis.
OX   NCBI_TaxID=56364;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-36; 64-70 AND 98-105,
RP   TISSUE SPECIFICITY, MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY,
RP   AND AMIDATION AT PHE-36; PHE-70 AND PHE-105.
RX   PubMed=29466015; DOI=10.1021/acs.jproteome.7b00779;
RA   Diesner M., Gallot A., Binz H., Gaertner C., Vitecek S., Kahnt J.,
RA   Schachtner J., Jacquin-Joly E., Gadenne C.;
RT   "Mating-induced differential peptidomics of neuropeptides and protein
RT   hormones in Agrotis ipsilon moths.";
RL   J. Proteome Res. 17:1397-1414(2018).
CC   -!- FUNCTION: Plays a role in controlling food intake and regulating body
CC       size. {ECO:0000250|UniProtKB:Q9VIQ0}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: sNPF peptide 1: Expressed in corpora cardiaca (CC),
CC       corpora allata (CA), antennal lobe (AL) and gnathal ganglion (GNG) (at
CC       protein level). Expression in AL detected in all animals, in GNG in
CC       most animals, expression in CC and CA in some animals (at protein
CC       level). sNPF peptide 2: Expressed in corpora cardiaca (CC), corpora
CC       allata (CA), antennal lobe (AL) and gnathal ganglion (GNG) (at protein
CC       level). Expression in AL detected in all animals, in GNG, CC and CA in
CC       most animals (at protein level). sNPF peptide 3: Expressed in corpora
CC       cardiaca (CC), corpora allata (CA), antennal lobe (AL) and gnathal
CC       ganglion (GNG) (at protein level). Expression detected in all animals
CC       (at protein level). {ECO:0000269|PubMed:29466015}.
CC   -!- MASS SPECTROMETRY: [sNPF peptide 1]: Mass=1359.81; Method=MALDI;
CC       Note=Short neuropeptide F 1.; Evidence={ECO:0000269|PubMed:29466015};
CC   -!- MASS SPECTROMETRY: [sNPF peptide 2]: Mass=887.54; Method=MALDI;
CC       Note=Short neuropeptide F 2.; Evidence={ECO:0000269|PubMed:29466015};
CC   -!- MASS SPECTROMETRY: [sNPF peptide 3]: Mass=958.58; Method=MALDI;
CC       Note=Short neuropeptide F 3.; Evidence={ECO:0000269|PubMed:29466015};
CC   -!- SIMILARITY: Belongs to the NPY 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   AlphaFoldDB; C0HKV9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Neuropeptide; Secreted.
FT   PROPEP          1..23
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000444276"
FT   PEPTIDE         26..36
FT                   /note="sNPF peptide 1"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444277"
FT   PROPEP          40..62
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000444278"
FT   PEPTIDE         64..70
FT                   /note="sNPF peptide 2"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444279"
FT   PROPEP          74..96
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000444280"
FT   PEPTIDE         98..105
FT                   /note="sNPF peptide 3"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444281"
FT   PROPEP          109..139
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000444282"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT   MOD_RES         70
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT   MOD_RES         105
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
SQ   SEQUENCE   139 AA;  16066 MW;  CD9D26D836254B34 CRC64;
     MGRARRTVRA PAQHDALGGH ALARKSVRSP SRRLRFGRRS DPDMPPQAPL DEMNELLSLR
     EVRTPVRLRF GRRSEERAVP HIFPQEFLTQ EQDRAVRAPS IRLRFGRRSD NNMFLLPYES
     ALPQEVKANG SVEDDRQQE