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SECP_APIME
ID   SECP_APIME              Reviewed;          77 AA.
AC   P02852; Q8ISJ3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Secapin;
DE   Flags: Precursor;
OS   Apis mellifera (Honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC   Apis.
OX   NCBI_TaxID=7460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=6548708; DOI=10.1111/j.1432-1033.1984.tb08549.x;
RA   Vlasak R., Kreil G.;
RT   "Nucleotide sequence of cloned cDNAs coding for preprosecapin, a major
RT   product of queen-bee venom glands.";
RL   Eur. J. Biochem. 145:279-282(1984).
RN   [2]
RP   SEQUENCE REVISION TO 39.
RA   Kreil G.;
RL   Submitted (JUN-1986) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RA   Zhang S.F., Shi W.J., Zhang C.X., Cheng J.A.;
RT   "Cloning and sequencing of cDNA encoding preprosecapin from the venom of
RT   Apis cerana cerana and Apis mellifera.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 53-77, AND DISULFIDE BOND.
RC   TISSUE=Venom;
RX   PubMed=631126; DOI=10.1111/j.1432-1033.1978.tb12106.x;
RA   Gauldie J., Hanson J.M., Shipolini R.A., Vernon C.A.;
RT   "The structures of some peptides from bee venom.";
RL   Eur. J. Biochem. 83:405-410(1978).
RN   [5]
RP   FUNCTION.
RX   PubMed=1248464; DOI=10.1111/j.1432-1033.1976.tb10030.x;
RA   Gauldie J., Hanson J.M., Rumjanek F.D., Shipolini R.A., Vernon C.A.;
RT   "The peptide components of bee venom.";
RL   Eur. J. Biochem. 61:369-376(1976).
CC   -!- FUNCTION: Serine protease inhibitor which exhibits antifibrinolytic,
CC       antielastolytic and antimicrobial activities (By similarity). Displays
CC       antimicrobial activity against bacteria and fungi (By similarity).
CC       Likely functions in the innate immune response to microbial infection
CC       and possibly in the venom, as an antifibrinolytic agent (By
CC       similarity). Not toxic to mice but does induce slight sedation at
CC       higher doses (from 40 mg/kg) (PubMed:1248464). At a dose of 80 mg/kg,
CC       sedation occurs 15 minutes after injection and is accompanied by
CC       piloerection and hypothermia (PubMed:1248464).
CC       {ECO:0000250|UniProtKB:A0A0K1YW63, ECO:0000269|PubMed:1248464}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:631126,
CC       ECO:0000305|Ref.3}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:631126, ECO:0000269|Ref.3}.
CC   -!- SIMILARITY: Belongs to the secapin family. {ECO:0000305}.
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DR   EMBL; M12598; AAA27733.1; -; mRNA.
DR   EMBL; AY082691; AAL92482.1; -; mRNA.
DR   PIR; A91139; WSHB.
DR   RefSeq; NP_001011618.1; NM_001011618.1.
DR   RefSeq; XP_016767767.1; XM_016912278.1.
DR   AlphaFoldDB; P02852; -.
DR   STRING; 7460.GB52317-PA; -.
DR   EnsemblMetazoa; XM_016912278; XP_016767767; LOC406145.
DR   GeneID; 406145; -.
DR   KEGG; ame:406145; -.
DR   Proteomes; UP000005203; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0035821; P:modulation of process of another organism; IDA:UniProtKB.
DR   InterPro; IPR020128; Secapin.
DR   Pfam; PF17521; Secapin; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Immunity; Innate immunity; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   PROPEP          33..52
FT                   /evidence="ECO:0000269|PubMed:631126"
FT                   /id="PRO_0000022290"
FT   PEPTIDE         53..77
FT                   /note="Secapin"
FT                   /evidence="ECO:0000269|PubMed:631126"
FT                   /id="PRO_0000022291"
FT   DISULFID        61..72
FT                   /evidence="ECO:0000269|PubMed:631126"
FT   CONFLICT        37..39
FT                   /note="MQP -> RQS (in Ref. 1; AAA27733)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75..77
FT                   /note="IVP -> PV (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   77 AA;  8664 MW;  7FD5D7E72DA6B3EA CRC64;
     MKNYSKNATH LITVLLFSFV VILLIIPSKC EAVSNDMQPL EARSADLVPE PRYIIDVPPR
     CPPGSKFIKN RCRVIVP
 
 
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