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Protein

Snake venom metalloprotease inhibitor 02D01

Gene
N/A
Organism
Echis ocellatus (Ocellated saw-scaled viper)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.1 Publication
C-type natriuretic peptide: exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3).By similarity

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHypotensive agent, Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor, Toxin, Vasoactive, Vasodilator

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Snake venom metalloprotease inhibitor 02D01
Alternative name(s):
02E11
10F07
Svmpi-Eoc7
Cleaved into the following 16 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEchis ocellatus (Ocellated saw-scaled viper)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri99586 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeEchis

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 23Sequence analysisAdd BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000033592624 – 38Sequence analysisAdd BLAST15
<p>This subsection of the ‘PTM / Processing’ section describes the position and length of an active peptide in the mature protein.<p><a href='/help/peptide' target='_top'>More...</a></p>PeptideiPRO_000033592739 – 41Tripeptide pEKW 13
PropeptideiPRO_000033592842 – 50Sequence analysis9
PeptideiPRO_000033592951 – 53Tripeptide pEKW 23
PropeptideiPRO_000033593054 – 62Sequence analysis9
PeptideiPRO_000033593163 – 65Tripeptide pEKW 33
PropeptideiPRO_000033593266 – 74Sequence analysis9
PeptideiPRO_000033593375 – 77Tripeptide pEKW 43
PropeptideiPRO_000033593478 – 86Sequence analysis9
PeptideiPRO_000033593587 – 89Tripeptide pEKW 53
PropeptideiPRO_000033593690 – 98Sequence analysis9
PeptideiPRO_000033593799 – 101Tripeptide pEKW 63
PropeptideiPRO_0000335938102 – 110Sequence analysis9
PeptideiPRO_0000335939111 – 113Tripeptide pEKW 73
PropeptideiPRO_0000335940114 – 122Sequence analysis9
PeptideiPRO_0000335941123 – 125Tripeptide pEKW 83
PropeptideiPRO_0000335942126 – 134Sequence analysis9
PeptideiPRO_0000335943135 – 137Tripeptide pEKW 93
PropeptideiPRO_0000335944138 – 146Sequence analysis9
PeptideiPRO_0000335945147 – 149Tripeptide pEKW 103
PropeptideiPRO_0000335946150 – 158Sequence analysis9
PeptideiPRO_0000335947159 – 161Tripeptide pEKW 113
PropeptideiPRO_0000335948162 – 249Sequence analysisAdd BLAST88
PeptideiPRO_0000335949250 – 277Poly-His-poly-Gly peptide 4Add BLAST28
PeptideiPRO_0000335950250 – 276Poly-His-poly-Gly peptide 3Add BLAST27
PeptideiPRO_0000335951251 – 277Poly-His-poly-Gly peptide 2Add BLAST27
PeptideiPRO_0000335952251 – 276Poly-His-poly-Gly peptide 1Add BLAST26
PropeptideiPRO_0000335953278 – 286Sequence analysis9
PeptideiPRO_0000335954287 – 308C-type natriuretic peptideBy similarityAdd BLAST22

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei39Pyrrolidone carboxylic acid1 Publication1
Modified residuei51Pyrrolidone carboxylic acid1 Publication1
Modified residuei63Pyrrolidone carboxylic acid1 Publication1
Modified residuei75Pyrrolidone carboxylic acid1 Publication1
Modified residuei87Pyrrolidone carboxylic acid1 Publication1
Modified residuei99Pyrrolidone carboxylic acid1 Publication1
Modified residuei111Pyrrolidone carboxylic acid1 Publication1
Modified residuei123Pyrrolidone carboxylic acid1 Publication1
Modified residuei135Pyrrolidone carboxylic acid1 Publication1
Modified residuei147Pyrrolidone carboxylic acid1 Publication1
Modified residuei159Pyrrolidone carboxylic acid1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi292 ↔ 308By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
A8YPR6

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed by the venom gland.

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
A8YPR6

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi25 – 166Pro-richAdd BLAST142
Compositional biasi252 – 261His-rich10
Compositional biasi263 – 276Gly-richAdd BLAST14

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

In the C-terminal section; belongs to the natriuretic peptide family.Curated
In the central section; belongs to the pHpG family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG073115

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000663 Natr_peptide
IPR030480 Natr_peptide_CS
IPR002408 Natriuretic_peptide_brain

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00212 ANP, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00712 BNATPEPTIDE
PR00710 NATPEPTIDES

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00183 NAT_PEP, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00263 NATRIURETIC_PEPTIDE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

A8YPR6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFVSRLAASG LLLLSLLALS LDGKPLPQRQ PHHIQPMEQK WLAPDAPPLE
60 70 80 90 100
QKWLAPDAPP LEQKWLAPAA PPLEQKWLAP DAPPMEQKWL APDAPPMEQK
110 120 130 140 150
WLAPDAPPME QKWLAPDAPP MEQKWLAPDA APLEQKWLAP DAPPMEQKWL
160 170 180 190 200
APDAPPMEQK WQPQIPSLME QRQLSSGGTT ALRQELSPRA EAASGPAVVG
210 220 230 240 250
GGGGGGGGSK AALALPKPPK AKGAAAATSR LMRDLRPDGK QASQKWGRLV
260 270 280 290 300
DHDHDHHHHH HPGSSVGGGG GGGGGGARRL KGLAKKGVAK GCFGLKLDRI

GSMSGLGC
Length:308
Mass (Da):32,722
Last modified:May 20, 2008 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i71CA03BA9DEA2C50
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti46 – 69Missing in 10F07. Add BLAST24
Natural varianti47P → A in 02E11. 1
Natural varianti50 – 109Missing in 02E11. Add BLAST60
Natural varianti73L → M in 10F07. 1
Natural varianti109M → L in 10F07. 1
Natural varianti119 – 121PPM → APL in 10F07. 3
Natural varianti131 – 133APL → PPM in 10F07. 3
Natural varianti200 – 201Missing in 02E11. 2
Natural varianti223G → GAA in 02E11. 1
Natural varianti223G → GAAA in 10F07. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AM902491 mRNA Translation: CAP17273.1
AM902490 mRNA Translation: CAP17272.1
AM902489 mRNA Translation: CAP17271.1

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM902491 mRNA Translation: CAP17273.1
AM902490 mRNA Translation: CAP17272.1
AM902489 mRNA Translation: CAP17271.1

3D structure databases

SMRiA8YPR6
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiA8YPR6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG073115

Family and domain databases

InterProiView protein in InterPro
IPR000663 Natr_peptide
IPR030480 Natr_peptide_CS
IPR002408 Natriuretic_peptide_brain
PfamiView protein in Pfam
PF00212 ANP, 1 hit
PRINTSiPR00712 BNATPEPTIDE
PR00710 NATPEPTIDES
SMARTiView protein in SMART
SM00183 NAT_PEP, 1 hit
PROSITEiView protein in PROSITE
PS00263 NATRIURETIC_PEPTIDE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSVMI_ECHOC
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A8YPR6
Secondary accession number(s): A8YPR7, A8YPR8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: November 22, 2017
This is version 35 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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