PBAN_HELZE
ID PBAN_HELZE Reviewed; 194 AA.
AC P11159; Q25200;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=PBAN-type neuropeptides;
DE AltName: Full=Pheromone/pyrokinin biosynthesis-activating neuropeptide;
DE Contains:
DE RecName: Full=Diapause hormone homolog;
DE Short=DH;
DE AltName: Full=Pyrokinin-1;
DE Contains:
DE RecName: Full=Alpha-SG neuropeptide;
DE Contains:
DE RecName: Full=Beta-SG neuropeptide;
DE AltName: Full=Pyrokinin-2;
DE Contains:
DE RecName: Full=Pheromone biosynthesis-activating neuropeptide;
DE Short=Hez-PBAN;
DE AltName: Full=Pyrokinin-3;
DE Contains:
DE RecName: Full=Gamma-SG neuropeptide;
DE AltName: Full=Pyrokinin-4;
DE Flags: Precursor;
OS Helicoverpa zea (Corn earworm moth) (Heliothis zea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Helicoverpa.
OX NCBI_TaxID=7113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND AMIDATION AT LEU-47; LEU-103; LEU-123; LEU-159 AND
RP LEU-169.
RC TISSUE=Head;
RX PubMed=8022813; DOI=10.1073/pnas.91.14.6506;
RA Ma P.W., Knipple D.C., Roelofs W.L.;
RT "Structural organization of the Helicoverpa zea gene encoding the precursor
RT protein for pheromone biosynthesis-activating neuropeptide and other
RT neuropeptides.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6506-6510(1994).
RN [2]
RP PROTEIN SEQUENCE OF 127-159, FUNCTION, AND SYNTHESIS.
RC TISSUE=Brain, and Subesophageal ganglion;
RX PubMed=17802237; DOI=10.1126/science.244.4906.796;
RA Raina A.K., Jaffe H., Kempe T.G., Keim P., Blacher R.W., Fales H.M.,
RA Riley C.T., Klun J.A., Ridgway R.L., Hayes D.K.;
RT "Identification of a neuropeptide hormone that regulates sex pheromone
RT production in female moths.";
RL Science 244:796-798(1989).
RN [3]
RP STRUCTURE BY NMR OF 127-159, AND AMIDATION AT LEU-159.
RX PubMed=8791159; DOI=10.1111/j.1399-3011.1996.tb01085.x;
RA Clark B.A., Prestwich G.D.;
RT "Evidence for a C-terminal turn in PBAN. An NMR and distance geometry
RT study.";
RL Int. J. Pept. Protein Res. 47:361-368(1996).
CC -!- FUNCTION: A hormone that controls sex pheromone production in females
CC and pheromone responsiveness in male. Also mediates visceral muscle
CC contractile activity (myotropic activity).
CC {ECO:0000269|PubMed:17802237, ECO:0000269|PubMed:8022813}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8022813}.
CC -!- TISSUE SPECIFICITY: Expressed in the subesophageal ganglions. Not found
CC in corpora cardiaca, corpora allata and thoracic ganglia.
CC {ECO:0000269|PubMed:8022813}.
CC -!- MISCELLANEOUS: Juvenile hormone seems to allow PBAN release, which then
CC induces pheromone biosynthesis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pyrokinin family. {ECO:0000305}.
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DR EMBL; U08109; AAA20661.1; -; mRNA.
DR PIR; A55756; A55756.
DR AlphaFoldDB; P11159; -.
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; 4.
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..23
FT /evidence="ECO:0000255"
FT PEPTIDE 24..47
FT /note="Diapause hormone homolog"
FT /evidence="ECO:0000255"
FT /id="PRO_0000029936"
FT PROPEP 51..94
FT /id="PRO_0000029937"
FT PEPTIDE 97..103
FT /note="Alpha-SG neuropeptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000029938"
FT PEPTIDE 106..123
FT /note="Beta-SG neuropeptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000029939"
FT PEPTIDE 127..159
FT /note="Pheromone biosynthesis-activating neuropeptide"
FT /id="PRO_0000029940"
FT PEPTIDE 162..169
FT /note="Gamma-SG neuropeptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000029941"
FT PROPEP 172..194
FT /id="PRO_0000029942"
FT MOD_RES 47
FT /note="Leucine amide"
FT /evidence="ECO:0000305|PubMed:8022813"
FT MOD_RES 103
FT /note="Leucine amide"
FT /evidence="ECO:0000305|PubMed:8022813"
FT MOD_RES 123
FT /note="Leucine amide"
FT /evidence="ECO:0000305|PubMed:8022813"
FT MOD_RES 159
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:8791159,
FT ECO:0000305|PubMed:8022813"
FT MOD_RES 169
FT /note="Leucine amide"
FT /evidence="ECO:0000305|PubMed:8022813"
SQ SEQUENCE 194 AA; 22373 MW; B120B81B39B4B5D3 CRC64;
MFNQTQLFVF LAVFTTSSVL GNNNDVKDGA ASGAHSDRLG LWFGPRLGKR SLRISTEDNR
QAFFKLLEAA DALKYYYDQL PYEMQADEPE TRVTKKVIFT PKLGRSLAYD DKSFENVEFT
PRLGRRLSDD MPATPADQEM YRQDPEQIDS RTKYFSPRLG RTMNFSPRLG RELSYDMMPN
KIRVVRSTNK TRST
