SVMI_BOTFO
ID SVMI_BOTFO Reviewed; 18 AA.
AC P0DL08;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 1.
DT 25-MAY-2022, entry version 12.
DE RecName: Full=Poly-His-poly-Gly peptide 1;
DE Short=pHpG-1;
OS Bothrops fonsecai (Fonseca's lancehead) (Rhinocerophis fonsecai).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=157549;
RN [1]
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=22869554; DOI=10.1074/mcp.m112.019331;
RA Tashima A.K., Zelanis A., Kitano E.S., Ianzer D., Melo R.L., Rioli V.,
RA Sant'anna S.S., Schenberg A.C., Camargo A.C., Serrano S.M.T.;
RT "Peptidomics of three Bothrops snake venoms: insights into the molecular
RT diversification of proteomes and peptidomes.";
RL Mol. Cell. Proteomics 11:1245-1262(2012).
CC -!- FUNCTION: May serve as a metalloproteinase inhibitor during glandular
CC storage. Their inhibition may be instantly disengaged, by dilution or
CC physiochemical change, when venom is injected into tissue of the
CC victim. {ECO:0000250|UniProtKB:A8YPR6}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MASS SPECTROMETRY: Mass=1506.6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:22869554};
CC -!- MISCELLANEOUS: Poly-His-poly-Gly peptide are encoded by two gene
CC families: snake venom metalloprotease inhibitors and bradykinin-
CC potentiating-C-type natriuretic peptides (BPP-CNP).
CC -!- SIMILARITY: Belongs to the pHpG family. {ECO:0000305}.
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DR AlphaFoldDB; P0DL08; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Secreted.
FT PEPTIDE 1..18
FT /note="Poly-His-poly-Gly peptide 1"
FT /id="PRO_0000421922"
SQ SEQUENCE 18 AA; 1508 MW; 28AB26262D264B44 CRC64;
HHDHHAAVGG GGGGGGGA