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Entry version 134 (05 Dec 2018)
Sequence version 1 (01 Apr 1993)
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Protein

Zinc metalloproteinase-disintegrin-like jararhagin

Gene
N/A
Organism
Bothrops jararaca (Jararaca) (Bothrops jajaraca)
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

Snake venom zinc metalloproteinase-disintegrin-like jararhagin: causes hemorrhage. This is the result of the degradation of sub-endothelial matrix proteins leading to the disruption of the blood vessel endothelium, with accompanying disturbances in platelet function. It is able to degrade von Willebrand factor (vWF) and it hydrolyzes the alpha-chain of fibrinogen (FGA) while leaving the beta and gamma chains unaffected. It inhibits collagen-induced platelet aggregation through the binding to alpha-2/beta-1 integrin (ITGA2/ITGB1) (collagen receptor), and it cleaves the beta-1 subunit of the same integrin, inhibiting platelet interaction and ultimately causing impairment of signal transduction. It has inability to be affected by the plasma inhibitor alpha2-macroglobulin. In fibroblasts, it functions as a collagen-mimetic substrate and, in endothelial cells, it causes apoptosis and indirectly inhibits cell proliferation by release of angiostatin-like compounds. It induces a strong pro-inflammatory response characterized by intense leukocyte accumulation and release of cytokines at the site of the injection. Although hemorrhage and edema are a response to the direct effect of this toxin, jararhagin-induced inflammation and necrosis are dependent on macrophages and key pro-inflammatory cytokines or their receptors. It also possesses anti-tumorgenic properties.
Disintegrin jararhagin-C: the monomeric form inhibits collagen- and ADP-induced platelet aggregation, but has no effect on glycoprotein Ib-IX-dependent (GP1BA/GP5/GP9) platelet agglutination. Locally activates the early events of an acute inflammatory response as leukocyte rolling and pro-inflammatory cytokine release.
Disintegrin jararhagin-C: the dimeric form jaracetin may be a dimeric form of jararhagin-C. It binds to von Willebrand factor (VWF) and induces its interaction with GPIbalpha (GP1BA) (via the vWF A1 domain), resulting in platelet aggregation. Also binds the alpha-2 subunit of the alpha-2/beta-1 (ITGA2/ITGB1) integrin. It potently induces platelet aggregation in citrated platelet-rich plasma.

Miscellaneous

The metalloproteinase domain which is released from the cleavage of jararhagin-C is apparently unstable.
A third form of jararhagin is obtained when the toxin is submitted to in vitro autolysis. The disintegrin-like/cysteine-rich domains appear to be disulfid-linked to a N-terminal portion of the metalloproteinase domain.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Cleavage of 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 bonds in insulin B chain.1 Publication EC:3.4.24.73

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by EDTA, 1,10 phenanthroline and batimastat (a peptidomimetic MMP inhibitor).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi162Calcium 1By similarity1
Metal bindingi246Calcium 1By similarity1
Metal bindingi295Zinc; catalyticCurated1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei296PROSITE-ProRule annotation1
Metal bindingi299Zinc; catalyticCurated1
Metal bindingi305Zinc; catalyticCurated1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei339Necessary, but not sufficient, for proteolytic processing1
Metal bindingi350Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi353Calcium 1By similarity1
Metal bindingi365Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi368Calcium 2By similarity1
Metal bindingi370Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi372Calcium 2By similarity1
Metal bindingi375Calcium 2By similarity1
Metal bindingi378Calcium 2By similarity1
Metal bindingi429Calcium 3By similarity1
Metal bindingi430Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi432Calcium 3By similarity1
Metal bindingi444Calcium 3By similarity1
Metal bindingi445Calcium 3; via carbonyl oxygenBy similarity1

<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 functionCell adhesion impairing toxin, Fibrinogenolytic toxin, Hemorrhagic toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Platelet aggregation activating toxin, Platelet aggregation inhibiting toxin, Protease, Toxin
Biological processApoptosis
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.24.73 911

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M12.138

<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:
Zinc metalloproteinase-disintegrin-like jararhagin (EC:3.4.24.73)
Alternative name(s):
HF2-proteinase
JG
Jararafibrase I
Short name:
JF I
Snake venom metalloproteinase
Short name:
SVMP
Cleaved into the following chain:
Alternative name(s):
Jaracetin
<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>OrganismiBothrops jararaca (Jararaca) (Bothrops jajaraca)
<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 identifieri8724 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeBothrops

<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 <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_0000029009‹1 – 150By similarityAdd BLAST›150
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000029010151 – 571Zinc metalloproteinase-disintegrin-like jararhaginAdd BLAST421
ChainiPRO_0000029011360 – 571Disintegrin-like jararhagin-CAdd BLAST212

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 residuei151Pyrrolidone carboxylic acid (Glu)By similarity1
<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 bondi270 ↔ 350In zinc metalloproteinase-disintegrin-like jararhaginBy similarity
Disulfide bondi310 ↔ 334In zinc metalloproteinase-disintegrin-like jararhaginBy similarity
Disulfide bondi312 ↔ 317In zinc metalloproteinase-disintegrin-like jararhaginBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi333N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi366 ↔ 395In zinc metalloproteinase-disintegrin-like jararhagin; alternateBy similarity
Disulfide bondi366 ↔ 385In disintegrin-like jararhagin-C; alternateBy similarity
Disulfide bondi377 ↔ 395In disintegrin-like jararhagin-C; alternateBy similarity
Disulfide bondi377 ↔ 390In zinc metalloproteinase-disintegrin-like jararhagin; alternateBy similarity
Disulfide bondi379 ↔ 385In zinc metalloproteinase-disintegrin-like jararhagin; alternateBy similarity
Disulfide bondi389 ↔ 412In zinc metalloproteinase-disintegrin-like jararhaginBy similarity
Disulfide bondi403 ↔ 409In zinc metalloproteinase-disintegrin-like jararhaginBy similarity
Disulfide bondi408 ↔ 434In zinc metalloproteinase-disintegrin-like jararhaginBy similarity
Disulfide bondi421 ↔ 441In both disintegrin-like jararhagin-C and zinc metalloproteinase-disintegrin-like jararhaginPROSITE-ProRule annotation
Disulfide bondi428 ↔ 460In zinc metalloproteinase-disintegrin-like jararhagin; alternateBy similarity
Disulfide bondi428 ↔ 453In disintegrin-like jararhagin-C; alternateBy similarity
Disulfide bondi453 ↔ 465In zinc metalloproteinase-disintegrin-like jararhagin; alternateBy similarity
Disulfide bondi460 ↔ 465In disintegrin-like jararhagin-CBy similarity
Disulfide bondi472 ↔ 522In zinc metalloproteinase-disintegrin-like jararhagin; alternateBy similarity
Disulfide bondi472 ↔ 487In disintegrin-like jararhagin-C; alternateBy similarity
Disulfide bondi487 ↔ 533In zinc metalloproteinase-disintegrin-like jararhagin; alternateBy similarity
Disulfide bondi500 ↔ 510In zinc metalloproteinase-disintegrin-like jararhagin; alternateBy similarity
Disulfide bondi510 ↔ 517In disintegrin-like jararhagin-C; alternateBy similarity
Disulfide bondi517 ↔ 559In zinc metalloproteinase-disintegrin-like jararhagin; alternateBy similarity
Disulfide bondi522 ↔ 533In disintegrin-like jararhagin-CBy similarity
Disulfide bondi553 ↔ 564In zinc metalloproteinase-disintegrin-like jararhagin; alternateBy similarity
Disulfide bondi559 ↔ 564In disintegrin-like jararhagin-CBy similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The N-terminus of Jararhagin is blocked.

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid, Zymogen

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (Jararhagin and Jararhagin-C) and dimer (Jaracetin).1 Publication

<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

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C9Gmodel-A152-355[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P30431

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

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SMRi
P30431

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini159 – 355Peptidase M12BPROSITE-ProRule annotationAdd BLAST197
Domaini363 – 449DisintegrinPROSITE-ProRule annotationAdd BLAST87

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi427 – 429D/ECD-tripeptide3

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 biasi450 – 571Cys-richAdd BLAST122

<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

Phylogenomic databases

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG006978

KEGG Orthology (KO)

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KOi
K20139

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04269 ZnMc_adamalysin_II_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.390.10, 1 hit
4.10.70.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR006586 ADAM_Cys-rich
IPR018358 Disintegrin_CS
IPR001762 Disintegrin_dom
IPR036436 Disintegrin_dom_sf
IPR024079 MetalloPept_cat_dom_sf
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
IPR034027 Reprolysin_adamalysin

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF08516 ADAM_CR, 1 hit
PF00200 Disintegrin, 1 hit
PF01562 Pep_M12B_propep, 1 hit
PF01421 Reprolysin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00289 DISINTEGRIN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00608 ACR, 1 hit
SM00050 DISIN, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF57552 SSF57552, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS00427 DISINTEGRIN_1, 1 hit
PS50214 DISINTEGRIN_2, 1 hit
PS00142 ZINC_PROTEASE, 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: Fragment.

<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.

P30431-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
ATRPKGAVQP KYEDAMQYEF KVNGEPVVLH LEKNKGLFSK DYSEIHYSPD
60 70 80 90 100
GREITTYPPV EDHCYYHGRI ENDADSTASI SACNGLKGYF KLQRETYFIE
110 120 130 140 150
PLKLPDSEAH AVFKYENVEK EDEAPKMCGV TQNWKSYEPI KKASQLAFTA
160 170 180 190 200
EQQRYDPYKY IEFFVVVDQG TVTKNNGDLD KIKARMYELA NIVNEIFRYL
210 220 230 240 250
YMHVALVGLE IWSNGDKITV KPDVDYTLNS FAEWRKTDLL TRKKHDNAQL
260 270 280 290 300
LTAIDFNGPT IGYAYIGSMC HPKRSVGIVQ DYSPINLVVA VIMAHEMGHN
310 320 330 340 350
LGIHHDTGSC SCGDYPCIMG PTISNEPSKF FSNCSYIQCW DFIMNHNPEC
360 370 380 390 400
IINEPLGTDI ISPPVCGNEL LEVGEECDCG TPENCQNECC DAATCKLKSG
410 420 430 440 450
SQCGHGDCCE QCKFSKSGTE CRASMSECDP AEHCTGQSSE CPADVFHKNG
460 470 480 490 500
QPCLDNYGYC YNGNCPIMYH QCYALFGADV YEAEDSCFKD NQKGNYYGYC
510 520 530 540 550
RKENGKKIPC APEDVKCGRL YCKDNSPGQN NPCKMFYSND DEHKGMVLPG
560 570
TKCADGKVCS NGHCVDVATA Y
Length:571
Mass (Da):63,983
Last modified:April 1, 1993 - v1
<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:iF5E549F8BF61177B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section is used for sequence fragments to indicate that the residue at the extremity of the sequence is not the actual terminal residue in the complete protein sequence.<p><a href='/help/non_ter' target='_top'>More...</a></p>Non-terminal residuei11

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X68251 Genomic DNA Translation: CAA48323.1

Protein sequence database of the Protein Information Resource

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PIRi
S24789

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:CAA48323

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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
X68251 Genomic DNA Translation: CAA48323.1
PIRiS24789

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C9Gmodel-A152-355[»]
ProteinModelPortaliP30431
SMRiP30431
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM12.138

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA48323

Phylogenomic databases

HOVERGENiHBG006978
KOiK20139

Enzyme and pathway databases

BRENDAi3.4.24.73 911

Family and domain databases

CDDicd04269 ZnMc_adamalysin_II_like, 1 hit
Gene3Di3.40.390.10, 1 hit
4.10.70.10, 1 hit
InterProiView protein in InterPro
IPR006586 ADAM_Cys-rich
IPR018358 Disintegrin_CS
IPR001762 Disintegrin_dom
IPR036436 Disintegrin_dom_sf
IPR024079 MetalloPept_cat_dom_sf
IPR001590 Peptidase_M12B
IPR002870 Peptidase_M12B_N
IPR034027 Reprolysin_adamalysin
PfamiView protein in Pfam
PF08516 ADAM_CR, 1 hit
PF00200 Disintegrin, 1 hit
PF01562 Pep_M12B_propep, 1 hit
PF01421 Reprolysin, 1 hit
PRINTSiPR00289 DISINTEGRIN
SMARTiView protein in SMART
SM00608 ACR, 1 hit
SM00050 DISIN, 1 hit
SUPFAMiSSF57552 SSF57552, 1 hit
PROSITEiView protein in PROSITE
PS50215 ADAM_MEPRO, 1 hit
PS00427 DISINTEGRIN_1, 1 hit
PS50214 DISINTEGRIN_2, 1 hit
PS00142 ZINC_PROTEASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiVM3JA_BOTJA
<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: P30431
<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: April 1, 1993
Last sequence update: April 1, 1993
Last modified: December 5, 2018
This is version 134 of the entry and version 1 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

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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