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SECP_TETBN
ID   SECP_TETBN              Reviewed;          57 AA.
AC   A0A6M6RE84;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Secapin {ECO:0000305};
DE   AltName: Full=U17-myrmicitoxin-Tb1a {ECO:0000303|PubMed:30149710};
DE            Short=U17-MYRTX-Tb1a {ECO:0000303|PubMed:30149710};
DE   Flags: Precursor;
OS   Tetramorium bicarinatum (Tramp ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Tetramorium.
OX   NCBI_TaxID=219812 {ECO:0000312|EMBL:QJZ31624.1};
RN   [1] {ECO:0000312|EMBL:QJZ31624.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-54, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, MASS SPECTROMETRY, AND
RP   AMIDATION AT ALA-56.
RC   TISSUE=Venom gland {ECO:0000269|PubMed:30149710};
RX   PubMed=30149710; DOI=10.1021/acs.jproteome.8b00452;
RA   Touchard A., Tene N., Song P.C.T., Lefranc B., Leprince J., Treilhou M.,
RA   Bonnafe E.;
RT   "Deciphering the Molecular Diversity of an Ant Venom Peptidome through a
RT   Venomics Approach.";
RL   J. Proteome Res. 17:3503-3516(2018).
CC   -!- FUNCTION: Non-toxic peptide. {ECO:0000250|UniProtKB:P02852}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30149710}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:30149710}.
CC   -!- PTM: O-glycosylated. {ECO:0000269|PubMed:30149710}.
CC   -!- MASS SPECTROMETRY: Mass=2670.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:30149710};
CC   -!- SIMILARITY: Belongs to the secapin family. {ECO:0000305}.
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DR   EMBL; MN450157; QJZ31624.1; -; mRNA.
DR   AlphaFoldDB; A0A6M6RE84; -.
DR   SMR; A0A6M6RE84; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   InterPro; IPR020128; Secapin.
DR   Pfam; PF17521; Secapin; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..33
FT                   /evidence="ECO:0000305|PubMed:30149710"
FT                   /id="PRO_0000453047"
FT   PEPTIDE         34..56
FT                   /note="Secapin"
FT                   /evidence="ECO:0000269|PubMed:30149710"
FT                   /id="PRO_0000453048"
FT   MOD_RES         56
FT                   /note="Alanine amide"
FT                   /evidence="ECO:0000269|PubMed:30149710"
FT   DISULFID        42..53
FT                   /evidence="ECO:0000250|UniProtKB:P02852"
SQ   SEQUENCE   57 AA;  6341 MW;  E0B68E51182682A1 CRC64;
     MEKNRTNIFS VYLMITFLLI SIFITMVMSD GEATIINAPN RCPPGHVVVK GRCRIAG
 
 
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