SVMI_ECHOC
ID SVMI_ECHOC Reviewed; 308 AA.
AC A8YPR6; A8YPR7; A8YPR8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Snake venom metalloprotease inhibitor 02D01;
DE AltName: Full=02E11;
DE AltName: Full=10F07;
DE AltName: Full=Svmpi-Eoc7;
DE Contains:
DE RecName: Full=Tripeptide pEKW 1;
DE Contains:
DE RecName: Full=Tripeptide pEKW 2;
DE Contains:
DE RecName: Full=Tripeptide pEKW 3;
DE Contains:
DE RecName: Full=Tripeptide pEKW 4;
DE Contains:
DE RecName: Full=Tripeptide pEKW 5;
DE Contains:
DE RecName: Full=Tripeptide pEKW 6;
DE Contains:
DE RecName: Full=Tripeptide pEKW 7;
DE Contains:
DE RecName: Full=Tripeptide pEKW 8;
DE Contains:
DE RecName: Full=Tripeptide pEKW 9;
DE Contains:
DE RecName: Full=Tripeptide pEKW 10;
DE Contains:
DE RecName: Full=Tripeptide pEKW 11;
DE Contains:
DE RecName: Full=Poly-His-poly-Gly peptide 4;
DE Short=pHpG-4;
DE Contains:
DE RecName: Full=Poly-His-poly-Gly peptide 3;
DE Short=pHpG-3;
DE Contains:
DE RecName: Full=Poly-His-poly-Gly peptide 2;
DE Short=pHpG-2;
DE Contains:
DE RecName: Full=Poly-His-poly-Gly peptide 1;
DE Short=pHpG-1;
DE Contains:
DE RecName: Full=C-type natriuretic peptide;
DE Short=CNP;
DE Flags: Precursor;
OS Echis ocellatus (Ocellated saw-scaled viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX NCBI_TaxID=99586;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-41; 51-53; 63-65; 75-77;
RP 87-89; 99-101; 111-113; 123-125; 135-137; 147-149; 159-161 AND 250-277,
RP PYROGLUTAMATE FORMATION AT GLN-39; GLN-51; GLN-63; GLN-75; GLN-87; GLN-99;
RP GLN-111; GLN-123; GLN-135; GLN-147 AND GLN-159, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=18029259; DOI=10.1016/j.bbrc.2007.11.027;
RA Wagstaff S.C., Favreau P., Cheneval O., Laing G.D., Wilkinson M.C.,
RA Miller R.L., Stoecklin R., Harrison R.A.;
RT "Molecular characterisation of endogenous snake venom metalloproteinase
RT inhibitors.";
RL Biochem. Biophys. Res. Commun. 365:650-656(2008).
CC -!- FUNCTION: pEKW and poly-His-poly-Gly peptides may serve as
CC metalloproteinase inhibitors during glandular storage. Their inhibition
CC may be instantly disengaged, by dilution or physiochemical change, when
CC venom is injected into tissue of the prey.
CC {ECO:0000303|PubMed:18029259}.
CC -!- FUNCTION: [C-type natriuretic peptide]: Exhibits hypotensive and
CC vasodepressor activity. Acts by activating natriuretic receptors (NPR1
CC and/or NPR2 and/or NPR3). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: In the C-terminal section; belongs to the natriuretic
CC peptide family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the pHpG family.
CC {ECO:0000305}.
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DR EMBL; AM902491; CAP17273.1; -; mRNA.
DR EMBL; AM902490; CAP17272.1; -; mRNA.
DR EMBL; AM902489; CAP17271.1; -; mRNA.
DR AlphaFoldDB; A8YPR6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
DR GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR InterPro; IPR000663; Natr_peptide.
DR InterPro; IPR030480; Natr_peptide_CS.
DR InterPro; IPR002408; Natriuretic_peptide_brain.
DR Pfam; PF00212; ANP; 1.
DR PRINTS; PR00712; BNATPEPTIDE.
DR PRINTS; PR00710; NATPEPTIDES.
DR SMART; SM00183; NAT_PEP; 1.
DR PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Hypotensive agent; Metalloenzyme inhibitor;
KW Metalloprotease inhibitor; Protease inhibitor; Pyrrolidone carboxylic acid;
KW Repeat; Secreted; Signal; Toxin; Vasoactive; Vasodilator.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..38
FT /evidence="ECO:0000255"
FT /id="PRO_0000335926"
FT PEPTIDE 39..41
FT /note="Tripeptide pEKW 1"
FT /id="PRO_0000335927"
FT PROPEP 42..50
FT /evidence="ECO:0000255"
FT /id="PRO_0000335928"
FT PEPTIDE 51..53
FT /note="Tripeptide pEKW 2"
FT /id="PRO_0000335929"
FT PROPEP 54..62
FT /evidence="ECO:0000255"
FT /id="PRO_0000335930"
FT PEPTIDE 63..65
FT /note="Tripeptide pEKW 3"
FT /id="PRO_0000335931"
FT PROPEP 66..74
FT /evidence="ECO:0000255"
FT /id="PRO_0000335932"
FT PEPTIDE 75..77
FT /note="Tripeptide pEKW 4"
FT /id="PRO_0000335933"
FT PROPEP 78..86
FT /evidence="ECO:0000255"
FT /id="PRO_0000335934"
FT PEPTIDE 87..89
FT /note="Tripeptide pEKW 5"
FT /id="PRO_0000335935"
FT PROPEP 90..98
FT /evidence="ECO:0000255"
FT /id="PRO_0000335936"
FT PEPTIDE 99..101
FT /note="Tripeptide pEKW 6"
FT /id="PRO_0000335937"
FT PROPEP 102..110
FT /evidence="ECO:0000255"
FT /id="PRO_0000335938"
FT PEPTIDE 111..113
FT /note="Tripeptide pEKW 7"
FT /id="PRO_0000335939"
FT PROPEP 114..122
FT /evidence="ECO:0000255"
FT /id="PRO_0000335940"
FT PEPTIDE 123..125
FT /note="Tripeptide pEKW 8"
FT /id="PRO_0000335941"
FT PROPEP 126..134
FT /evidence="ECO:0000255"
FT /id="PRO_0000335942"
FT PEPTIDE 135..137
FT /note="Tripeptide pEKW 9"
FT /id="PRO_0000335943"
FT PROPEP 138..146
FT /evidence="ECO:0000255"
FT /id="PRO_0000335944"
FT PEPTIDE 147..149
FT /note="Tripeptide pEKW 10"
FT /id="PRO_0000335945"
FT PROPEP 150..158
FT /evidence="ECO:0000255"
FT /id="PRO_0000335946"
FT PEPTIDE 159..161
FT /note="Tripeptide pEKW 11"
FT /id="PRO_0000335947"
FT PROPEP 162..249
FT /evidence="ECO:0000255"
FT /id="PRO_0000335948"
FT PEPTIDE 250..277
FT /note="Poly-His-poly-Gly peptide 4"
FT /id="PRO_0000335949"
FT PEPTIDE 250..276
FT /note="Poly-His-poly-Gly peptide 3"
FT /id="PRO_0000335950"
FT PEPTIDE 251..277
FT /note="Poly-His-poly-Gly peptide 2"
FT /id="PRO_0000335951"
FT PEPTIDE 251..276
FT /note="Poly-His-poly-Gly peptide 1"
FT /id="PRO_0000335952"
FT PROPEP 278..286
FT /evidence="ECO:0000255"
FT /id="PRO_0000335953"
FT PEPTIDE 287..308
FT /note="C-type natriuretic peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000335954"
FT REGION 172..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 51
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 63
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 75
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 87
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 99
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 111
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 123
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 135
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 147
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 159
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT DISULFID 292..308
FT /evidence="ECO:0000250"
FT VARIANT 46..69
FT /note="Missing (in 10F07)"
FT VARIANT 47
FT /note="P -> A (in 02E11)"
FT VARIANT 50..109
FT /note="Missing (in 02E11)"
FT VARIANT 73
FT /note="L -> M (in 10F07)"
FT VARIANT 109
FT /note="M -> L (in 10F07)"
FT VARIANT 119..121
FT /note="PPM -> APL (in 10F07)"
FT VARIANT 131..133
FT /note="APL -> PPM (in 10F07)"
FT VARIANT 200..201
FT /note="Missing (in 02E11)"
FT VARIANT 223
FT /note="G -> GAA (in 02E11)"
FT VARIANT 223
FT /note="G -> GAAA (in 10F07)"
SQ SEQUENCE 308 AA; 32722 MW; 71CA03BA9DEA2C50 CRC64;
MFVSRLAASG LLLLSLLALS LDGKPLPQRQ PHHIQPMEQK WLAPDAPPLE QKWLAPDAPP
LEQKWLAPAA PPLEQKWLAP DAPPMEQKWL APDAPPMEQK WLAPDAPPME QKWLAPDAPP
MEQKWLAPDA APLEQKWLAP DAPPMEQKWL APDAPPMEQK WQPQIPSLME QRQLSSGGTT
ALRQELSPRA EAASGPAVVG GGGGGGGGSK AALALPKPPK AKGAAAATSR LMRDLRPDGK
QASQKWGRLV DHDHDHHHHH HPGSSVGGGG GGGGGGARRL KGLAKKGVAK GCFGLKLDRI
GSMSGLGC
