SVMI1_CERCE
ID SVMI1_CERCE Reviewed; 302 AA.
AC A8YPR9; A8YPS0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Snake venom metalloprotease inhibitor 02A10;
DE AltName: Full=01F09;
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=Tripeptide pEKW 12;
DE Contains:
DE RecName: Full=Tripeptide pEKW 13;
DE Contains:
DE RecName: Full=Tripeptide pEKW 14;
DE Contains:
DE RecName: Full=Tripeptide pEKW 15;
DE Contains:
DE RecName: Full=Tripeptide pEKW 16;
DE Contains:
DE RecName: Full=Tripeptide pEKW 17;
DE Contains:
DE RecName: Full=C-type natriuretic peptide;
DE Short=CNP;
DE Flags: Precursor;
GN Name=Svmpi-Cce12;
OS Cerastes cerastes (Horned desert viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Cerastes.
OX NCBI_TaxID=8697;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 48-50; 59-61; 70-72; 81-83;
RP 92-94; 103-105; 114-116; 125-127; 136-138; 147-149; 158-160; 169-171;
RP 180-182; 191-193; 202-204; 213-215 AND 224-226, FUNCTION, PYROGLUTAMATE
RP FORMATION AT GLN-48; GLN-59; GLN-70; GLN-81; GLN-92; GLN-103; GLN-114;
RP GLN-125; GLN-136; GLN-147; GLN-158; GLN-169; GLN-180; GLN-191; GLN-202;
RP GLN-213 AND GLN-224, AND IDENTIFICATION BY MASS 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 peptides may serve as metalloproteinase inhibitors
CC during glandular storage. Their inhibition may be instantly disengaged,
CC by dilution or physiochemical change, when venom is injected into
CC tissue of the victim. {ECO:0000269|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) (By similarity). {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}.
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DR EMBL; AM902492; CAP17274.1; -; mRNA.
DR EMBL; AM902493; CAP17275.1; -; mRNA.
DR AlphaFoldDB; A8YPR9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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.
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..47
FT /evidence="ECO:0000255"
FT /id="PRO_0000335955"
FT PEPTIDE 48..50
FT /note="Tripeptide pEKW 1"
FT /id="PRO_0000335956"
FT PROPEP 51..58
FT /evidence="ECO:0000255"
FT /id="PRO_0000335957"
FT PEPTIDE 59..61
FT /note="Tripeptide pEKW 2"
FT /id="PRO_0000335958"
FT PROPEP 62..69
FT /evidence="ECO:0000255"
FT /id="PRO_0000335959"
FT PEPTIDE 70..72
FT /note="Tripeptide pEKW 3"
FT /id="PRO_0000335960"
FT PROPEP 73..80
FT /evidence="ECO:0000255"
FT /id="PRO_0000335961"
FT PEPTIDE 81..83
FT /note="Tripeptide pEKW 4"
FT /id="PRO_0000335962"
FT PROPEP 84..91
FT /evidence="ECO:0000255"
FT /id="PRO_0000335963"
FT PEPTIDE 92..94
FT /note="Tripeptide pEKW 5"
FT /id="PRO_0000335964"
FT PROPEP 95..102
FT /evidence="ECO:0000255"
FT /id="PRO_0000335965"
FT PEPTIDE 103..105
FT /note="Tripeptide pEKW 6"
FT /id="PRO_0000335966"
FT PROPEP 106..113
FT /evidence="ECO:0000255"
FT /id="PRO_0000335967"
FT PEPTIDE 114..116
FT /note="Tripeptide pEKW 7"
FT /id="PRO_0000335968"
FT PROPEP 117..124
FT /evidence="ECO:0000255"
FT /id="PRO_0000335969"
FT PEPTIDE 125..127
FT /note="Tripeptide pEKW 8"
FT /id="PRO_0000335970"
FT PROPEP 128..135
FT /evidence="ECO:0000255"
FT /id="PRO_0000335971"
FT PEPTIDE 136..138
FT /note="Tripeptide pEKW 9"
FT /id="PRO_0000335972"
FT PROPEP 139..146
FT /evidence="ECO:0000255"
FT /id="PRO_0000335973"
FT PEPTIDE 147..149
FT /note="Tripeptide pEKW 10"
FT /id="PRO_0000335974"
FT PROPEP 150..157
FT /evidence="ECO:0000255"
FT /id="PRO_0000335975"
FT PEPTIDE 158..160
FT /note="Tripeptide pEKW 11"
FT /id="PRO_0000335976"
FT PROPEP 161..168
FT /evidence="ECO:0000255"
FT /id="PRO_0000335977"
FT PEPTIDE 169..171
FT /note="Tripeptide pEKW 12"
FT /id="PRO_0000335978"
FT PROPEP 172..179
FT /evidence="ECO:0000255"
FT /id="PRO_0000335979"
FT PEPTIDE 180..182
FT /note="Tripeptide pEKW 13"
FT /id="PRO_0000335980"
FT PROPEP 183..190
FT /evidence="ECO:0000255"
FT /id="PRO_0000335981"
FT PEPTIDE 191..193
FT /note="Tripeptide pEKW 14"
FT /id="PRO_0000335982"
FT PROPEP 194..201
FT /evidence="ECO:0000255"
FT /id="PRO_0000335983"
FT PEPTIDE 202..204
FT /note="Tripeptide pEKW 15"
FT /id="PRO_0000335984"
FT PROPEP 205..212
FT /evidence="ECO:0000255"
FT /id="PRO_0000335985"
FT PEPTIDE 213..215
FT /note="Tripeptide pEKW 16"
FT /id="PRO_0000335986"
FT PROPEP 216..223
FT /evidence="ECO:0000255"
FT /id="PRO_0000335987"
FT PEPTIDE 224..226
FT /note="Tripeptide pEKW 17"
FT /id="PRO_0000335988"
FT PROPEP 227..273
FT /evidence="ECO:0000255"
FT /id="PRO_0000335989"
FT PEPTIDE 274..293
FT /note="C-type natriuretic peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000335990"
FT PROPEP 294..302
FT /evidence="ECO:0000255"
FT /id="PRO_0000335991"
FT REGION 32..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 59
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 70
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 81
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 92
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 103
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 114
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 125
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 136
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 158
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 169
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 180
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 191
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 202
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 213
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT MOD_RES 224
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:18029259"
FT DISULFID 279..293
FT /evidence="ECO:0000250"
FT VARIANT 85
FT /note="N -> D (in 01F09)"
FT VARIANT 107
FT /note="N -> D (in 01F09)"
FT VARIANT 129
FT /note="N -> D (in 01F09)"
FT VARIANT 140
FT /note="N -> D (in 01F09)"
SQ SEQUENCE 302 AA; 35326 MW; 21ECDFBB3DE941A1 CRC64;
MSVSRLAASG LLLVSLLALA LDGKPVEKWS PWLWPPRPRP PIPPLQQQKW LDPPIPQQQK
WLDPPIPQQQ KWLDPPIPQQ QKWLNPPIPQ QQKWLDPPIP QQQKWLNPPI PQQQKWLNPP
IPQQQKWLNP PIPQQQKWLN PPIPQQQKWL DPPIPQQQKW LDPPIPQQQK WLDPPIPQQQ
KWLNPPIPQQ QKWLDPPIPQ QQKWLDPPIP QQQKWLNPPI PQQQKWQRPL QPEVPSLMEL
HQERQKQGRM MHHDEDPGDA AEGPRRQKKE PGKPEGNGCF GKKIDRINAG FGCPKLPPSG
GH
