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CAPA_AGRIP
ID   CAPA_AGRIP              Reviewed;         157 AA.
AC   C0HKS6; C0HKS7; C0HKS8; C0HKS9; C0HKT0;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=CAPA peptides {ECO:0000305};
DE   Contains:
DE     RecName: Full=CAPA-periviscerokinin 1 {ECO:0000305|PubMed:29466015};
DE              Short=CAPA-PVK-1 {ECO:0000303|PubMed:29466015};
DE   Contains:
DE     RecName: Full=CAPA-periviscerokinin 2 {ECO:0000305|PubMed:29466015};
DE              Short=CAPA-PVK-2 {ECO:0000303|PubMed:29466015};
DE   Contains:
DE     RecName: Full=CAPA-periviscerokinin 3 {ECO:0000305|PubMed:29466015};
DE              Short=CAPA-PVK-3 {ECO:0000303|PubMed:29466015};
DE   Contains:
DE     RecName: Full=CAPA-trypto-pyrokinin {ECO:0000305|PubMed:29466015};
DE     AltName: Full=CAPA-tryptoPK {ECO:0000303|PubMed:29466015};
DE   Contains:
DE     RecName: Full=CAPA-precursor-related peptide 3 {ECO:0000305|PubMed:29466015};
DE              Short=CAPA-PP-3 {ECO:0000303|PubMed:29466015};
DE   Flags: Precursor;
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 31-42; 69-76; 79-85; 88-103
RP   AND 106-117, TISSUE SPECIFICITY, MASS SPECTROMETRY, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AMIDATION AT VAL-42; VAL-76; LEU-85 AND LEU-117, AND
RP   PYROGLUTAMATE FORMATION AT GLN-69.
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: [CAPA-trypto-pyrokinin]: Myoactive.
CC       {ECO:0000250|UniProtKB:P82693}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: CAPA-periviscerokinin 1: Expressed in corpora
CC       cardiaca (CC), corpora allata (CA), antennal lobe (AL) and gnathal
CC       ganglion (GNG) (at protein level). Expression detected in most animals
CC       in CC and CA and in some animals in AL and GNG (at protein level).
CC       CAPA-periviscerokinin 2: Expressed in corpora cardiaca (CC), corpora
CC       allata (CA), antennal lobe (AL) and gnathal ganglion (GNG) (at protein
CC       level). For non-pyroglutamate form, expression in AL detected in all
CC       animals, in CC, CA and GNG in most animals (at protein level). For
CC       pyroglutamate form, expression in CC and CA detected in most animals,
CC       in AL and GNG in some animals (at protein level). CAPA-periviscerokinin
CC       3: Expressed in corpora cardiaca (CC), corpora allata (CA), antennal
CC       lobe (AL) and gnathal ganglion (GNG). Expression detected in most
CC       animals in CC and CA and in some animals in AL and GNG (at protein
CC       level). CAPA-precursor-related peptide 3: Expressed in corpora cardiaca
CC       (CC), corpora allata (CA), antennal lobe (AL) and gnathal ganglion
CC       (GNG) (at protein level). Expression in CC and CA detected in some
CC       animals, expression in Al and GNG detected in few animals (at protein
CC       level). CAPA-trypto-pyrokinin: Expressed in corpora cardiaca (CC),
CC       corpora allata (CA), antennal lobe (AL) and gnathal ganglion (GNG) (at
CC       protein level). Expression in CC, CA and GNG detected in most animals,
CC       in AL in some animals (at protein level).
CC       {ECO:0000269|PubMed:29466015}.
CC   -!- MASS SPECTROMETRY: [CAPA-periviscerokinin 1]: Mass=1420.78;
CC       Mass_error=0.01; Method=MALDI; Note=Periviscerokinin 1.;
CC       Evidence={ECO:0000269|PubMed:29466015};
CC   -!- MASS SPECTROMETRY: [CAPA-periviscerokinin 2]: Mass=992.55;
CC       Mass_error=0.01; Method=MALDI; Note=Periviscerokinin 2.;
CC       Evidence={ECO:0000269|PubMed:29466015};
CC   -!- MASS SPECTROMETRY: [CAPA-periviscerokinin 2]: Mass=975.51;
CC       Mass_error=0.01; Method=MALDI; Note=Pyroglutamate-modified
CC       periviscerokinin 2.; Evidence={ECO:0000269|PubMed:29466015};
CC   -!- MASS SPECTROMETRY: [CAPA-periviscerokinin 3]: Mass=816.47;
CC       Mass_error=0.01; Method=MALDI; Note=Periviscerokinin 3.;
CC       Evidence={ECO:0000269|PubMed:29466015};
CC   -!- MASS SPECTROMETRY: [CAPA-precursor-related peptide 3]: Mass=1831.87;
CC       Mass_error=0.01; Method=MALDI; Note=CAPA-PP 3.;
CC       Evidence={ECO:0000269|PubMed:29466015};
CC   -!- MASS SPECTROMETRY: [CAPA-trypto-pyrokinin]: Mass=1376.70;
CC       Mass_error=0.01; Method=MALDI; Note=Pyrokinin.;
CC       Evidence={ECO:0000269|PubMed:29466015};
CC   -!- SIMILARITY: Belongs to the pyrokinin family. {ECO:0000255}.
CC   -!- CAUTION: Further mature peptides might exist. {ECO:0000305}.
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DR   AlphaFoldDB; C0HKS6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR001484; Pyrokinin_CS.
DR   PROSITE; PS00539; PYROKININ; 1.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Neuropeptide; Pyrrolidone carboxylic acid; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..28
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000444214"
FT   PEPTIDE         31..42
FT                   /note="CAPA-periviscerokinin 1"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444215"
FT   PROPEP          45..66
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000444216"
FT   PEPTIDE         69..76
FT                   /note="CAPA-periviscerokinin 2"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444217"
FT   PEPTIDE         79..85
FT                   /note="CAPA-periviscerokinin 3"
FT                   /evidence="ECO:0000303|PubMed:29466015"
FT                   /id="PRO_0000444218"
FT   PEPTIDE         88..103
FT                   /note="CAPA-precursor-related peptide 3"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444219"
FT   PEPTIDE         106..117
FT                   /note="CAPA-trypto-pyrokinin"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT                   /id="PRO_0000444220"
FT   PROPEP          120..157
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000444221"
FT   REGION          131..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         42
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT   MOD_RES         69
FT                   /note="Pyrrolidone carboxylic acid; partial"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT   MOD_RES         76
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT   MOD_RES         85
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
FT   MOD_RES         117
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:29466015"
SQ   SEQUENCE   157 AA;  18230 MW;  0F2CAB8391A39F46 CRC64;
     MQPTMRIIVS MALLAYAVAS AYHSNVKLRR DGKMVLYPFP RVGRASGNTW QLPLNDLYPE
     YEPAQVKRQL YAFPRVGRDP VMSRLGRSDL SRVESHEFQP MAVRRTESPG MWFGPRLGRA
     FKNDDDEITI QNESNDHSEP EQTELIHEDR RKRQTLN
 
 
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