SVMI2_ATHNI
ID SVMI2_ATHNI Reviewed; 30 AA.
AC P0C7K6;
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 2;
DE Short=pHpG 2;
OS Atheris nitschei (Great lakes 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=110224;
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=3071.39; 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; P0C7K6; -.
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..30
FT /note="Poly-His-poly-Gly peptide 2"
FT /id="PRO_0000335994"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 30 AA; 3073 MW; 9EE78B9E9246E4A1 CRC64;
EDDHDHHHHH HHHHHHHGVG GGGGGGGGGA