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BXB1_BOMMO
ID   BXB1_BOMMO              Reviewed;          89 AA.
AC   P26733;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Bombyxin B-1;
DE            Short=BBX-B1;
DE   AltName: Full=4K-prothoracicotropic hormone;
DE            Short=4K-PTTH;
DE   Contains:
DE     RecName: Full=Bombyxin B-1 B chain;
DE   Contains:
DE     RecName: Full=Bombyxin B-1 A chain;
DE   Flags: Precursor;
GN   Name=BBXB1;
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 [GENOMIC DNA].
RX   PubMed=2674935; DOI=10.1073/pnas.86.18.6843;
RA   Kawakami A., Iwami M., Nagasawa H., Suzuki A., Ishizaki H.;
RT   "Structure and organization of four clustered genes that encode bombyxin,
RT   an insulin-related brain secretory peptide of the silkmoth Bombyx mori.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:6843-6847(1989).
CC   -!- FUNCTION: Brain peptide responsible for activation of prothoracic
CC       glands to produce ecdysone in insects.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Silk worm has two kinds of PTTH: 4K-PTTH and 22K-PTTH;
CC       there are many forms of 4K-PTTH.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA27824.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M26068; AAA27824.1; ALT_INIT; Genomic_DNA.
DR   PIR; A21182; A21182.
DR   PIR; C41391; IPMTB1.
DR   RefSeq; NP_001121791.1; NM_001128319.1.
DR   AlphaFoldDB; P26733; -.
DR   STRING; 7091.BGIBMGA014498-TA; -.
DR   GeneID; 100169719; -.
DR   KEGG; bmor:100169719; -.
DR   CTD; 100169719; -.
DR   eggNOG; ENOG502SESX; Eukaryota.
DR   HOGENOM; CLU_125164_2_0_1; -.
DR   InParanoid; P26733; -.
DR   OrthoDB; 1638932at2759; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   InterPro; IPR017097; Bombyxin.
DR   InterPro; IPR027285; Bombyxin_B.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 2.
DR   PIRSF; PIRSF037038; Bombyxin; 1.
DR   PIRSF; PIRSF500313; Bombyxin_B; 1.
DR   PRINTS; PR02003; BOMBYXIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         20..45
FT                   /note="Bombyxin B-1 B chain"
FT                   /id="PRO_0000015989"
FT   PROPEP          48..66
FT                   /note="C peptide like"
FT                   /id="PRO_0000015990"
FT   PEPTIDE         69..89
FT                   /note="Bombyxin B-1 A chain"
FT                   /id="PRO_0000015991"
FT   DISULFID        29..75
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        41..88
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        74..79
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   89 AA;  9945 MW;  91941FF579D3DDF9 CRC64;
     MKTSVMFMLV IVISLMCSGE AQEVARTYCG RHLADTLADL CFGVEKRGGA QYAPYFWTRQ
     YLGSRGKRGV VDECCFRPCT LDVLLSYCG
 
 
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