ID   SVMI1_ATHSQ             Reviewed;          24 AA.
AC   P0C7K4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Poly-His-poly-Gly peptide 1;
DE            Short=pHpG-1;
OS   Atheris squamigera (Variable bush viper).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Viperinae; Atheris.
OX   NCBI_TaxID=110225;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=17206746; DOI=10.1002/rcm.2853;
RA   Favreau P., Cheneval O., Menin L., Michalet S., Gaertner H., Principaud F.,
RA   Thai R., Menez A., Bulet P., Stoecklin R.;
RT   "The venom of the snake genus Atheris contains a new class of peptides with
RT   clusters of histidine and glycine residues.";
RL   Rapid Commun. Mass Spectrom. 21:406-412(2007).
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=2336.98; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17206746};
CC   -!- SIMILARITY: Belongs to the pHpG family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P0C7K4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Metalloenzyme inhibitor;
KW   Metalloprotease inhibitor; Protease inhibitor; Secreted.
FT   PEPTIDE         1..24
FT                   /note="Poly-His-poly-Gly peptide 1"
FT                   /id="PRO_0000335992"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   24 AA;  2338 MW;  EB5E5E5E47BD0B4A CRC64;
     EDDHHHHHHH HHGVGGGGGG GGGG