NEUPP_BOMMO
ID NEUPP_BOMMO Reviewed; 372 AA.
AC B9WZ56;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Putative neuropeptide precursor protein {ECO:0000303|PubMed:19540422};
DE Short=BmK5 {ECO:0000303|PubMed:19540422};
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] {ECO:0000305, ECO:0000312|EMBL:BAH22627.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=p50T; TISSUE=Subesophageal ganglion;
RX PubMed=19540422; DOI=10.1016/j.peptides.2009.03.023;
RA Mitsumasu K., Tanaka Y., Niimi T., Yamashita O., Yaginuma T.;
RT "Novel gene encoding precursor protein consisting of possible several
RT neuropeptides expressed in brain and frontal ganglion of the silkworm,
RT Bombyx mori.";
RL Peptides 30:1233-1240(2009).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19540422,
CC ECO:0000305}. Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in the brain and frontal ganglion and in
CC the axons connecting to the corpus cardiacum and corpus allatum (at
CC protein level). Detected in the brain-subesophageal ganglion (brain-SG)
CC complex, fat body, midgut and ovary. Expression in the brain-SG complex
CC is 2-3 times higher than in the other tissues.
CC {ECO:0000269|PubMed:19540422}.
CC -!- DEVELOPMENTAL STAGE: Detected at low levels in newly hatched larvae
CC with higher levels in the fifth instar larvae which continue into the
CC early and middle pupal stages. Expression then decreases by 6-day-old
CC pupal stage and reduces further in the adult stage (at protein level).
CC Expressed in the embryonic, larval and pupal-adult development stages.
CC Detected in male embryos 6 days after oviposition with expression in
CC female embryos starting later around day 8.
CC {ECO:0000269|PubMed:19540422}.
CC -!- PTM: May be proteolytically processed to give rise to a number of
CC active peptides. {ECO:0000303|PubMed:19540422}.
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DR EMBL; AB162718; BAH22627.1; -; mRNA.
DR RefSeq; NP_001153662.1; NM_001160190.1.
DR AlphaFoldDB; B9WZ56; -.
DR SMR; B9WZ56; -.
DR STRING; 7091.BGIBMGA008978-TA; -.
DR EnsemblMetazoa; BGIBMGA008978-RA; BGIBMGA008978-TA; BGIBMGA008978.
DR GeneID; 100301494; -.
DR KEGG; bmor:100301494; -.
DR CTD; 100301494; -.
DR eggNOG; ENOG502TB3T; Eukaryota.
DR HOGENOM; CLU_750637_0_0_1; -.
DR InParanoid; B9WZ56; -.
DR OMA; ENWDQTK; -.
DR OrthoDB; 980077at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..372
FT /note="Putative neuropeptide precursor protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000412719"
FT REGION 18..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 42011 MW; 715296DBB3C8DDCF CRC64;
MLLFSLTAIT AVLAVSAVPT PSNNKDGSTI SELPENWDQT KDDNRSLFLN KSDKNDLEPY
PLALSEEGNQ DGYDQTVDQR FDSPQSNGEL DNLIMRPELY GEPPAMEGLA SAFDLQRRKR
GSGTKVGGAG AATKVVTKSG SGKKNLKPED QAALSPIDLM TQHEAQRRKR GSGTKVGGAA
ASAKTATKNS GGNKKNFRPI SERRKRDSGL SAADVRALLN LWEAQERRKQ EYANQFAADR
YYGRVNPDEE QPEVDENGDL WYNEPVVIGP HDRDYPHHSY FSEQNRMALA RGYPDLYQVG
PNELAQRYEE ARRKRQYANK MKRFMVAKKR SDNMMHQNNY RPRDDLYTLA ELLRSAPRVQ
EQDIPVYRRL IL