PBAN_BOMMO
ID PBAN_BOMMO Reviewed; 192 AA.
AC P09971; Q17211; Q17234;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=PBAN-type neuropeptides;
DE AltName: Full=Neo-PBAN;
DE AltName: Full=Pheromone/pyrokinin biosynthesis-activating neuropeptide;
DE Contains:
DE RecName: Full=Diapause hormone;
DE Short=DH;
DE AltName: Full=DH-PBAN;
DE Contains:
DE RecName: Full=Alpha-SG neuropeptide;
DE Short=Alpha-SGNP;
DE Contains:
DE RecName: Full=Beta-SG neuropeptide;
DE Short=Beta-SGNP;
DE Contains:
DE RecName: Full=Pheromone biosynthesis-activating neuropeptide I;
DE Short=Bom-PBAN-I;
DE Short=PBAN-I;
DE AltName: Full=Melanization and reddish coloration hormone I;
DE Short=MRCH-I;
DE Contains:
DE RecName: Full=Pheromone biosynthesis-activating neuropeptide II;
DE Short=PBAN-II;
DE Contains:
DE RecName: Full=Gamma-SG neuropeptide;
DE Short=Gamma-SGNP;
DE Flags: Precursor;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Asagiri, and Kinshu X Showa; TISSUE=Subesophageal ganglion;
RX PubMed=1280417; DOI=10.1016/0006-291x(92)91547-4;
RA Kawano T., Kataoka H., Nagasawa H., Isogai A., Suzuki A.;
RT "cDNA cloning and sequence determination of the pheromone biosynthesis
RT activating neuropeptide of the silkworm, Bombyx mori.";
RL Biochem. Biophys. Res. Commun. 189:221-226(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 97-103 AND 161-168,
RP AMIDATION AT LEU-47, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND SYNTHESIS.
RC STRAIN=p50T; TISSUE=Brain, and Subesophageal ganglion;
RX PubMed=8475067; DOI=10.1073/pnas.90.8.3251;
RA Sato Y., Oguchi M., Menjo N., Imai K., Saito H., Ikeda M., Isobe M.,
RA Yamashita O.;
RT "Precursor polyprotein for multiple neuropeptides secreted from the
RT suboesophageal ganglion of the silkworm Bombyx mori: characterization of
RT the cDNA encoding the diapause hormone precursor and identification of
RT additional peptides.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3251-3255(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-109.
RX PubMed=7893764; DOI=10.1016/0167-4781(94)00238-x;
RA Xu W.H., Sato Y., Ikeda M., Yamashita O.;
RT "Molecular characterization of the gene encoding the precursor protein of
RT diapause hormone and pheromone biosynthesis activating neuropeptide (DH-
RT PBAN) of the silkworm, Bombyx mori and its distribution in some insects.";
RL Biochim. Biophys. Acta 1261:83-89(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=J106; TISSUE=Subesophageal ganglion;
RX PubMed=9362122; DOI=10.1271/bbb.61.1745;
RA Kawano T., Kataoka H., Nagasawa H., Isogai A., Suzuki A.;
RT "Molecular cloning of a new type of cDNA for pheromone biosynthesis
RT activating neuropeptide in the silkworm, Bombyx mori.";
RL Biosci. Biotechnol. Biochem. 61:1745-1747(1997).
RN [5]
RP PROTEIN SEQUENCE OF 125-158.
RX PubMed=1368584; DOI=10.1271/bbb1961.54.2495;
RA Kitamura A., Nagasawa H., Kataoka H., Ando T., Suzuki A.;
RT "Amino acid sequence of pheromone biosynthesis activating neuropeptide-II
RT (PBAN-II) of the silkmoth, Bombyx mori.";
RL Agric. Biol. Chem. 54:2495-2497(1990).
RN [6]
RP PROTEIN SEQUENCE OF 126-158, AND AMIDATION AT LEU-158.
RC TISSUE=Head;
RX PubMed=2775285; DOI=10.1016/0006-291x(89)92168-2;
RA Kitamura A., Nagasawa H., Kataoka H., Inoue T., Matsumoto S., Ando T.,
RA Suzuki A.;
RT "Amino acid sequence of pheromone-biosynthesis-activating neuropeptide
RT (PBAN) of the silkworm, Bombyx mori.";
RL Biochem. Biophys. Res. Commun. 163:520-526(1989).
RN [7]
RP PROTEIN SEQUENCE OF 126-158.
RX PubMed=8512566; DOI=10.1006/bbrc.1993.1675;
RA Nachman R.J., Kuniyoshi H., Roberts V.A., Holman G.M., Suzuki A.;
RT "Active conformation of the pyrokinin/PBAN neuropeptide family for
RT pheromone biosynthesis in the silkworm.";
RL Biochem. Biophys. Res. Commun. 193:661-666(1993).
RN [8]
RP PROTEIN SEQUENCE OF 126-140.
RC TISSUE=Head;
RX PubMed=3896851; DOI=10.1016/0014-5793(85)80853-x;
RA Matsumoto S., Isogai A., Suzuki A.;
RT "N-terminal amino acid sequence of an insect neurohormone, melanization and
RT reddish coloration hormone (MRCH): heterogeneity and sequence homology with
RT human insulin-like growth factor II.";
RL FEBS Lett. 189:115-118(1985).
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). Identical to MRCH which is
CC implicated in the formation of both melanin in the cuticle and
CC ommochrome in the epidermis of armyworm species.
CC {ECO:0000269|PubMed:8475067}.
CC -!- FUNCTION: Diapause hormone (DH) is responsible for induction of
CC embryonic diapause. {ECO:0000269|PubMed:8475067}.
CC -!- FUNCTION: The three SGNPS are far less active than DH in inducing
CC diapause eggs. Beta-SGNP expressed higher pban activity than PBAN-I,
CC but alpha- and gamma-SGNP were far less active in pheromonotropic
CC activity. {ECO:0000269|PubMed:8475067}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8475067}.
CC -!- TISSUE SPECIFICITY: Expression is restricted to the subesophageal
CC ganglion. {ECO:0000269|PubMed:8475067}.
CC -!- SIMILARITY: Belongs to the pyrokinin family. {ECO:0000305}.
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DR EMBL; S50045; AAB24327.1; -; mRNA.
DR EMBL; D28810; BAA05971.1; -; mRNA.
DR EMBL; D13437; BAA02699.1; -; mRNA.
DR EMBL; D16230; BAA03755.1; -; Genomic_DNA.
DR EMBL; D28764; BAA05954.1; -; mRNA.
DR PIR; A23992; A23992.
DR PIR; JC1354; JC1354.
DR PIR; JC5865; JC5865.
DR RefSeq; NP_001037321.1; NM_001043856.1.
DR RefSeq; XP_012547317.1; XM_012691863.1.
DR AlphaFoldDB; P09971; -.
DR SMR; P09971; -.
DR STRING; 7091.BGIBMGA001651-TA; -.
DR GeneID; 692749; -.
DR KEGG; bmor:692749; -.
DR CTD; 692749; -.
DR eggNOG; ENOG502TBQ8; Eukaryota.
DR HOGENOM; CLU_1403744_0_0_1; -.
DR OrthoDB; 1434163at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0016084; F:myostimulatory hormone activity; IMP:UniProtKB.
DR GO; GO:0005184; F:neuropeptide hormone activity; IMP:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IMP:UniProtKB.
DR GO; GO:0042811; P:pheromone biosynthetic process; IEA:InterPro.
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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PEPTIDE 24..47
FT /note="Diapause hormone"
FT /id="PRO_0000029921"
FT PROPEP 51..94
FT /id="PRO_0000029922"
FT PEPTIDE 97..103
FT /note="Alpha-SG neuropeptide"
FT /id="PRO_0000029923"
FT PEPTIDE 106..122
FT /note="Beta-SG neuropeptide"
FT /id="PRO_0000029924"
FT PEPTIDE 125..158
FT /note="Pheromone biosynthesis-activating neuropeptide II"
FT /id="PRO_0000029925"
FT PEPTIDE 126..158
FT /note="Pheromone biosynthesis-activating neuropeptide I"
FT /id="PRO_0000029926"
FT PEPTIDE 161..168
FT /note="Gamma-SG neuropeptide"
FT /id="PRO_0000029927"
FT PROPEP 171..192
FT /id="PRO_0000029928"
FT MOD_RES 47
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:8475067"
FT MOD_RES 103
FT /note="Leucine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 122
FT /note="Leucine amide"
FT /evidence="ECO:0000250"
FT MOD_RES 158
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:2775285"
FT MOD_RES 168
FT /note="Leucine amide"
FT /evidence="ECO:0000250"
FT VARIANT 109
FT /note="K -> N (in strain: J106)"
FT /evidence="ECO:0000269|PubMed:7893764"
FT VARIANT 126
FT /note="L -> PL (in MRCH-III)"
FT VARIANT 139
FT /note="M -> I (in strain: Daizo and J106)"
FT VARIANT 146
FT /note="E -> V (in strain: J106)"
FT CONFLICT 111
FT /note="Q -> R (in Ref. 3; BAA03755)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 22326 MW; A4FA0969CDC178F3 CRC64;
MYKTNIVFNV LALALFSIFF ASCTDMKDES DRGAHSERGA LWFGPRLGKR SMKPSTEDNR
QTFLRLLEAA DALKFYYDQL PYERQADEPE TKVTKKIIFT PKLGRSVAKP QTHESLEFIP
RLGRRLSEDM PATPADQEMY QPDPEEMESR TRYFSPRLGR TMSFSPRLGR ELSYDYPTKY
RVARSVNKTM DN
