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Snake venom metalloprotease inhibitor 02D01 (02E11) (10F07) (Svmpi-Eoc7) [Cleaved into: Tripeptide pEKW 1; Tripeptide pEKW 2; Tripeptide pEKW 3; Tripeptide pEKW 4; Tripeptide pEKW 5; Tripeptide pEKW 6; Tripeptide pEKW 7; Tripeptide pEKW 8; Tripeptide pEKW 9; Tripeptide pEKW 10; Tripeptide pEKW 11; Poly-His-poly-Gly peptide 4 (pHpG-4); Poly-His-poly-Gly peptide 3 (pHpG-3); Poly-His-poly-Gly peptide 2 (pHpG-2); Poly-His-poly-Gly peptide 1 (pHpG-1); C-type natriuretic peptide (CNP)]

 SVMI_ECHOC              Reviewed;         308 AA.
A8YPR6; A8YPR7; A8YPR8;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
20-MAY-2008, sequence version 2.
22-NOV-2017, entry version 35.
RecName: Full=Snake venom metalloprotease inhibitor 02D01;
AltName: Full=02E11;
AltName: Full=10F07;
AltName: Full=Svmpi-Eoc7;
Contains:
RecName: Full=Tripeptide pEKW 1;
Contains:
RecName: Full=Tripeptide pEKW 2;
Contains:
RecName: Full=Tripeptide pEKW 3;
Contains:
RecName: Full=Tripeptide pEKW 4;
Contains:
RecName: Full=Tripeptide pEKW 5;
Contains:
RecName: Full=Tripeptide pEKW 6;
Contains:
RecName: Full=Tripeptide pEKW 7;
Contains:
RecName: Full=Tripeptide pEKW 8;
Contains:
RecName: Full=Tripeptide pEKW 9;
Contains:
RecName: Full=Tripeptide pEKW 10;
Contains:
RecName: Full=Tripeptide pEKW 11;
Contains:
RecName: Full=Poly-His-poly-Gly peptide 4;
Short=pHpG-4;
Contains:
RecName: Full=Poly-His-poly-Gly peptide 3;
Short=pHpG-3;
Contains:
RecName: Full=Poly-His-poly-Gly peptide 2;
Short=pHpG-2;
Contains:
RecName: Full=Poly-His-poly-Gly peptide 1;
Short=pHpG-1;
Contains:
RecName: Full=C-type natriuretic peptide;
Short=CNP;
Flags: Precursor;
Echis ocellatus (Ocellated saw-scaled viper).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata;
Toxicofera; Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
NCBI_TaxID=99586;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-41; 51-53; 63-65;
75-77; 87-89; 99-101; 111-113; 123-125; 135-137; 147-149; 159-161 AND
250-277, PYROGLUTAMATE FORMATION AT GLN-39; GLN-51; GLN-63; GLN-75;
GLN-87; GLN-99; GLN-111; GLN-123; GLN-135; GLN-147 AND GLN-159, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Venom, and Venom gland;
PubMed=18029259; DOI=10.1016/j.bbrc.2007.11.027;
Wagstaff S.C., Favreau P., Cheneval O., Laing G.D., Wilkinson M.C.,
Miller R.L., Stoecklin R., Harrison R.A.;
"Molecular characterisation of endogenous snake venom
metalloproteinase inhibitors.";
Biochem. Biophys. Res. Commun. 365:650-656(2008).
-!- FUNCTION: pEKW and poly-His-poly-Gly peptides may serve as
metalloproteinase inhibitors during glandular storage. Their
inhibition may be instantly disengaged, by dilution or
physiochemical change, when venom is injected into tissue of the
prey. {ECO:0000303|PubMed:18029259}.
-!- FUNCTION: C-type natriuretic peptide: exhibits hypotensive and
vasodepressor activity. Acts by activating natriuretic receptors
(NPR1 and/or NPR2 and/or NPR3). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the venom gland.
-!- SIMILARITY: In the C-terminal section; belongs to the natriuretic
peptide family. {ECO:0000305}.
-!- SIMILARITY: In the central section; belongs to the pHpG family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AM902491; CAP17273.1; -; mRNA.
EMBL; AM902490; CAP17272.1; -; mRNA.
EMBL; AM902489; CAP17271.1; -; mRNA.
SMR; A8YPR6; -.
PRIDE; A8YPR6; -.
HOVERGEN; HBG073115; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005179; F:hormone activity; IEA:InterPro.
GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
InterPro; IPR000663; Natr_peptide.
InterPro; IPR030480; Natr_peptide_CS.
InterPro; IPR002408; Natriuretic_peptide_brain.
Pfam; PF00212; ANP; 1.
PRINTS; PR00712; BNATPEPTIDE.
PRINTS; PR00710; NATPEPTIDES.
SMART; SM00183; NAT_PEP; 1.
PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Direct protein sequencing;
Disulfide bond; Hypotensive agent; Metalloenzyme inhibitor;
Metalloprotease inhibitor; Protease inhibitor;
Pyrrolidone carboxylic acid; Repeat; Secreted; Signal; Toxin;
Vasoactive; Vasodilator.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 38 {ECO:0000255}.
/FTId=PRO_0000335926.
PEPTIDE 39 41 Tripeptide pEKW 1.
/FTId=PRO_0000335927.
PROPEP 42 50 {ECO:0000255}.
/FTId=PRO_0000335928.
PEPTIDE 51 53 Tripeptide pEKW 2.
/FTId=PRO_0000335929.
PROPEP 54 62 {ECO:0000255}.
/FTId=PRO_0000335930.
PEPTIDE 63 65 Tripeptide pEKW 3.
/FTId=PRO_0000335931.
PROPEP 66 74 {ECO:0000255}.
/FTId=PRO_0000335932.
PEPTIDE 75 77 Tripeptide pEKW 4.
/FTId=PRO_0000335933.
PROPEP 78 86 {ECO:0000255}.
/FTId=PRO_0000335934.
PEPTIDE 87 89 Tripeptide pEKW 5.
/FTId=PRO_0000335935.
PROPEP 90 98 {ECO:0000255}.
/FTId=PRO_0000335936.
PEPTIDE 99 101 Tripeptide pEKW 6.
/FTId=PRO_0000335937.
PROPEP 102 110 {ECO:0000255}.
/FTId=PRO_0000335938.
PEPTIDE 111 113 Tripeptide pEKW 7.
/FTId=PRO_0000335939.
PROPEP 114 122 {ECO:0000255}.
/FTId=PRO_0000335940.
PEPTIDE 123 125 Tripeptide pEKW 8.
/FTId=PRO_0000335941.
PROPEP 126 134 {ECO:0000255}.
/FTId=PRO_0000335942.
PEPTIDE 135 137 Tripeptide pEKW 9.
/FTId=PRO_0000335943.
PROPEP 138 146 {ECO:0000255}.
/FTId=PRO_0000335944.
PEPTIDE 147 149 Tripeptide pEKW 10.
/FTId=PRO_0000335945.
PROPEP 150 158 {ECO:0000255}.
/FTId=PRO_0000335946.
PEPTIDE 159 161 Tripeptide pEKW 11.
/FTId=PRO_0000335947.
PROPEP 162 249 {ECO:0000255}.
/FTId=PRO_0000335948.
PEPTIDE 250 277 Poly-His-poly-Gly peptide 4.
/FTId=PRO_0000335949.
PEPTIDE 250 276 Poly-His-poly-Gly peptide 3.
/FTId=PRO_0000335950.
PEPTIDE 251 277 Poly-His-poly-Gly peptide 2.
/FTId=PRO_0000335951.
PEPTIDE 251 276 Poly-His-poly-Gly peptide 1.
/FTId=PRO_0000335952.
PROPEP 278 286 {ECO:0000255}.
/FTId=PRO_0000335953.
PEPTIDE 287 308 C-type natriuretic peptide.
{ECO:0000250}.
/FTId=PRO_0000335954.
COMPBIAS 25 166 Pro-rich.
COMPBIAS 252 261 His-rich.
COMPBIAS 263 276 Gly-rich.
MOD_RES 39 39 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:18029259}.
MOD_RES 51 51 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:18029259}.
MOD_RES 63 63 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:18029259}.
MOD_RES 75 75 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:18029259}.
MOD_RES 87 87 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:18029259}.
MOD_RES 99 99 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:18029259}.
MOD_RES 111 111 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:18029259}.
MOD_RES 123 123 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:18029259}.
MOD_RES 135 135 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:18029259}.
MOD_RES 147 147 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:18029259}.
MOD_RES 159 159 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:18029259}.
DISULFID 292 308 {ECO:0000250}.
VARIANT 46 69 Missing (in 10F07).
VARIANT 47 47 P -> A (in 02E11).
VARIANT 50 109 Missing (in 02E11).
VARIANT 73 73 L -> M (in 10F07).
VARIANT 109 109 M -> L (in 10F07).
VARIANT 119 121 PPM -> APL (in 10F07).
VARIANT 131 133 APL -> PPM (in 10F07).
VARIANT 200 201 Missing (in 02E11).
VARIANT 223 223 G -> GAA (in 02E11).
VARIANT 223 223 G -> GAAA (in 10F07).
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


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