PBAN_AGRIP
ID PBAN_AGRIP Reviewed; 193 AA.
AC O76818; C0HKV1; C0HKV2; C0HKV3; C0HKV4; C0HKV5; C0HKV6; C0HKV7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=PBAN-type neuropeptides;
DE AltName: Full=Pheromone/pyrokinin biosynthesis-activating neuropeptide;
DE Contains:
DE RecName: Full=Diapause hormone {ECO:0000303|PubMed:29466015};
DE Short=DH;
DE Contains:
DE RecName: Full=PBAN precursor-related peptide 1 {ECO:0000305|PubMed:29466015};
DE Short=PBAN-PP-1 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=PBAN precursor-related peptide 2 {ECO:0000305|PubMed:29466015};
DE Short=PBAN-PP-2 {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Alpha-subesophageal ganglion neuropeptide {ECO:0000305|PubMed:29466015};
DE AltName: Full=Alpha-SG neuropeptide {ECO:0000305|PubMed:29466015};
DE Short=Alpha-SGNP {ECO:0000303|PubMed:29466015};
DE Contains:
DE RecName: Full=Beta-subesophageal ganglion neuropeptide {ECO:0000305|PubMed:29466015};
DE AltName: Full=Beta-SG neuropeptide {ECO:0000305|PubMed:29466015};
DE Short=Beta-SGNP {ECO:0000303|PubMed:29466015};
DE AltName: Full=Pyrokinin-1;
DE Contains:
DE RecName: Full=Pheromone biosynthesis-activating neuropeptide {ECO:0000303|PubMed:9753769};
DE Short=Agi-PBAN {ECO:0000303|PubMed:9753769};
DE AltName: Full=Pyrokinin-2;
DE Contains:
DE RecName: Full=Gamma-subesophageal ganglion neuropeptide {ECO:0000305|PubMed:29466015};
DE AltName: Full=Gamma-SG neuropeptide {ECO:0000305|PubMed:29466015};
DE Short=Gamma-SGNP {ECO:0000303|PubMed:29466015};
DE AltName: Full=Pyrokinin-3;
DE Contains:
DE RecName: Full=PBAN precursor-related peptide 3 {ECO:0000305|PubMed:29466015};
DE Short=PBAN-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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION OF PHEROMONE BIOSYNTHESIS-ACTIVATING
RP NEUROPEPTIDE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000303|PubMed:9753769}, and
RC Subesophageal ganglion {ECO:0000303|PubMed:9753769};
RX PubMed=9753769; DOI=10.1016/s0965-1748(98)00033-2;
RA Duportets L., Gadenne C., Dufour M.-C., Couillaud F.;
RT "The pheromone biosynthesis activating neuropeptide (PBAN) of the black
RT cutworm moth, Agrotis ipsilon: immunohistochemistry, molecular
RT characterization and bioassay of its peptide sequence.";
RL Insect Biochem. Mol. Biol. 28:591-599(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-46; 50-74; 75-93;
RP 96-102; 105-122; 161-168 AND 171-184, TISSUE SPECIFICITY, MASS
RP SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND AMIDATION AT ILE-46;
RP LEU-102; LEU-122 AND LEU-168.
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: [Pheromone biosynthesis-activating neuropeptide]: A hormone
CC that controls sex pheromone production in female moths and pheromone
CC responsiveness in male (PubMed:9753769). {ECO:0000269|PubMed:9753769}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9753769}.
CC -!- TISSUE SPECIFICITY: Pheromone biosynthesis-activating neuropeptide:
CC Expressed in the mandibular, maxillary and labial neuromeres of the
CC male and female brain-subesophageal ganglions, in the corpora cardiaca
CC and all around the corpora allata, and at a lower level in the brain
CC near the calyx and pedunculus of the mushroom body (at protein level)
CC (PubMed:9753769). Expressed in larvae and adult of both sexes (at
CC protein level) (PubMed:9753769). Diapause hormone: Expressed in corpora
CC cardiaca (CC), corpora allata (CA) and gnathal ganglion (GNG) (at
CC protein level) (PubMed:29466015). Expression in CC and CA detected in
CC most animals, in GNG in some (at protein level) (PubMed:29466015). PBAN
CC precursor-related peptide 1: Expression not detected in CC, CA, AL or
CC GNG (at protein level) (PubMed:29466015). PBAN precursor-related
CC peptide 2: Expression not detected in CC, CA, AL or GNG (at protein
CC level) (PubMed:29466015). Alpha-subesophageal ganglion neuropeptide:
CC Expressed in corpora cardiaca (CC), corpora allata (CA), antennal lobe
CC (AL) and gnathal ganglion (GNG) (at protein level) (PubMed:29466015).
CC Expression in CC, CA and GNG detected in most animals, expression in AL
CC detected in few (at protein level) (PubMed:29466015). Beta-
CC subesophageal ganglion neuropeptide: Expressed in corpora cardiaca
CC (CC), corpora allata (CA), antennal lobe (AL) and gnathal ganglion
CC (GNG) (at protein level) (PubMed:29466015). Expression in CC, CA and
CC GNG detected in most animals, expression in AL detected in few (at
CC protein level) (PubMed:29466015). Gamma-subesophageal ganglion
CC neuropeptide: Expressed in corpora cardiaca (CC), corpora allata (CA),
CC antennal lobe (AL) and gnathal ganglion (GNG) (at protein level)
CC (PubMed:29466015). Expression in CC, CA and GNG detected in all
CC animals, expression in AL detected in some (at protein level)
CC (PubMed:29466015). PBAN precursor-related peptide 3: Expressed in
CC corpora cardiaca (CC), corpora allata (CA), antennal lobe (AL) and
CC gnathal ganglion (GNG) (at protein level) (PubMed:29466015). Expression
CC in CC, CA and GNG detected in most animals, expression in AL detected
CC in some animals (at protein level) (PubMed:29466015).
CC {ECO:0000269|PubMed:29466015, ECO:0000269|PubMed:9753769}.
CC -!- MASS SPECTROMETRY: [Diapause hormone]: Mass=2844.31; Mass_error=0.01;
CC Method=MALDI; Note=Diapause hormone.;
CC Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [PBAN precursor-related peptide 1]: Mass=2901.54;
CC Mass_error=0.01; Method=MALDI; Note=PBAN precursor-related peptide 1.;
CC Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [PBAN precursor-related peptide 2]: Mass=2318.01;
CC Mass_error=0.01; Method=MALDI; Note=PBAN precursor-related peptide 2.;
CC Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Alpha-subesophageal ganglion neuropeptide]:
CC Mass=816.47; Mass_error=0.01; Method=MALDI; Note=Alpha-subesophageal
CC ganglion neuropeptide.; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Beta-subesophageal ganglion neuropeptide]:
CC Mass=2190.06; Mass_error=0.01; Method=MALDI; Note=Beta-subesophageal
CC ganglion neuropeptide.; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [Gamma-subesophageal ganglion neuropeptide]:
CC Mass=964.50; Mass_error=0.01; Method=MALDI; Note=Gamma-subesophageal
CC ganglion neuropeptide.; Evidence={ECO:0000269|PubMed:29466015};
CC -!- MASS SPECTROMETRY: [PBAN precursor-related peptide 3]: Mass=1633.90;
CC Mass_error=0.01; Method=MALDI; Note=PBAN precursor-related peptide 3.;
CC Evidence={ECO:0000269|PubMed:29466015};
CC -!- MISCELLANEOUS: Juvenile hormone seems to allow PBAN release, which then
CC induces pheromone biosynthesis.
CC -!- SIMILARITY: Belongs to the pyrokinin family. {ECO:0000305}.
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DR EMBL; AJ009674; CAA08774.1; -; mRNA.
DR AlphaFoldDB; O76818; -.
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 GO; GO:0042811; P:pheromone biosynthetic process; IEA:InterPro.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR InterPro; IPR008730; PBAN.
DR InterPro; IPR001484; Pyrokinin_CS.
DR Pfam; PF05874; PBAN; 1.
DR PROSITE; PS00539; PYROKININ; 3.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW Hormone; Neuropeptide; Pheromone response; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:29466015"
FT PEPTIDE 20..46
FT /note="Diapause hormone"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444160"
FT PEPTIDE 50..74
FT /note="PBAN precursor-related peptide 1"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444161"
FT PEPTIDE 75..93
FT /note="PBAN precursor-related peptide 2"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444162"
FT PEPTIDE 96..102
FT /note="Alpha-subesophageal ganglion neuropeptide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000029916"
FT PEPTIDE 105..122
FT /note="Beta-subesophageal ganglion neuropeptide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000029917"
FT PEPTIDE 126..158
FT /note="Pheromone biosynthesis-activating neuropeptide"
FT /evidence="ECO:0000303|PubMed:9753769"
FT /id="PRO_0000029918"
FT PEPTIDE 161..168
FT /note="Gamma-subesophageal ganglion neuropeptide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000029919"
FT PEPTIDE 171..184
FT /note="PBAN precursor-related peptide 3"
FT /evidence="ECO:0000269|PubMed:29466015"
FT /id="PRO_0000444163"
FT PROPEP 186..193
FT /evidence="ECO:0000305"
FT /id="PRO_0000444164"
FT REGION 124..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 102
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 122
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
FT MOD_RES 158
FT /note="Leucine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 168
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:29466015"
SQ SEQUENCE 193 AA; 22014 MW; 7F66D4080430DE18 CRC64;
MYGAVLPGLF FIFISCVVAS SNDVKDGGAD RGAHSDRGGM WFGPRIGKRS LRMATEDNRQ
AFFKLLEAAD ALKYYYDQLP YEMQADEPEA RVTKKVIFTP KLGRSLSYED KMFDNVEFTP
RLGRRLADDT PATPADQEMY RPDPEQIDSR TKYFSPRLGR TMNFSPRLGR ELAYEMLPSK
VRVVRSTNKT QST
