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Protein

Snake venom metalloproteinase atrolysin-D

Gene
N/A
Organism
Crotalus atrox (Western diamondback rattlesnake)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Snake venom zinc metalloproteinase that causes hemorrhage by provoking the degradation of the sub-endothelial matrix proteins (fibronectin, laminin, type IV collagen, nidogen, and gelatins).1 Publication

Catalytic activityi

Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 23-Gly-|-Phe-24 of insulin B chain. With small molecule substrates prefers hydrophobic residue at P2' and small residue such as Ala, Gly at P1.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi200 – 2001Calcium
Metal bindingi284 – 2841Calcium
Metal bindingi333 – 3331Zinc; catalytic
Active sitei334 – 3341
Metal bindingi337 – 3371Zinc; catalytic
Metal bindingi343 – 3431Zinc; catalytic
Metal bindingi388 – 3881Calcium; via carbonyl oxygen
Metal bindingi391 – 3911Calcium

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hemorrhagic toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Protease, Toxin

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.42. 1710.

Protein family/group databases

MEROPSiM12.144.

Names & Taxonomyi

Protein namesi
Recommended name:
Snake venom metalloproteinase atrolysin-D (EC:3.4.24.42)
Short name:
SVMP
Alternative name(s):
Hemorrhagic metalloproteinase atrolysin D
Hemorrhagic toxin D
Short name:
HT-D
OrganismiCrotalus atrox (Western diamondback rattlesnake)
Taxonomic identifieri8730 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCrotalus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 1901701 PublicationPRO_0000029000Add
BLAST
Chaini191 – 393203Snake venom metalloproteinase atrolysin-DPRO_0000029001Add
BLAST
Propeptidei394 – 41421PRO_0000029002Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911Pyrrolidone carboxylic acid1 Publication
Disulfide bondi308 ↔ 388PROSITE-ProRule annotation1 Publication
Disulfide bondi348 ↔ 355PROSITE-ProRule annotation1 Publication

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid, Zymogen

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

Secondary structure

1
414
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi197 – 2059Combined sources
Helixi207 – 2126Combined sources
Turni213 – 2153Combined sources
Helixi217 – 23519Combined sources
Helixi236 – 2383Combined sources
Beta strandi240 – 24910Combined sources
Helixi262 – 27514Combined sources
Helixi277 – 2804Combined sources
Beta strandi284 – 2907Combined sources
Beta strandi295 – 2973Combined sources
Turni310 – 3123Combined sources
Beta strandi313 – 3186Combined sources
Helixi324 – 33815Combined sources
Beta strandi353 – 3553Combined sources
Beta strandi358 – 3603Combined sources
Helixi371 – 38414Combined sources
Helixi388 – 3903Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ATLX-ray1.80A/B192-393[»]
1DTHX-ray2.00A/B191-393[»]
1HTDX-ray2.10A/B192-393[»]
ProteinModelPortaliP15167.
SMRiP15167. Positions 192-393.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15167.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini197 – 393197Peptidase M12BPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006978.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15167-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIEVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVT ALPKGAVQPK
60 70 80 90 100
YEDAMQYELK VNGEPVVLHL EKNKELFSKD YSETHYSPDG RKITTNPSVE
110 120 130 140 150
DHCYYRGRIE NDADSTASIS ACNGLKGHFK LQGEMYLIEP LELSDSEAHA
160 170 180 190 200
VFKLENVEKE DEAPKMCGVT QNWESYEPIK KASDLNLNPD QQNLPQRYIE
210 220 230 240 250
LVVVADHRVF MKYNSDLNTI RTRVHEIVNF INGFYRSLNI HVSLTDLEIW
260 270 280 290 300
SNEDQINIQS ASSDTLNAFA EWRETDLLNR KSHDNAQLLT AIELDEETLG
310 320 330 340 350
LAPLGTMCDP KLSIGIVQDH SPINLLMGVT MAHELGHNLG MEHDGKDCLR
360 370 380 390 400
GASLCIMRPG LTKGRSYEFS DDSMHYYERF LKQYKPQCIL NKPLRIDPVS
410
TPVSGNELLE AGEE
Length:414
Mass (Da):46,845
Last modified:October 1, 1996 - v3
Checksum:i0B41F26C9E450031
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti191 – 1911Missing in some chains.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01237 mRNA. Translation: AAA03352.1.
PIRiS41610. HYRSAC.

Genome annotation databases

KEGGiag:AAA03352.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01237 mRNA. Translation: AAA03352.1.
PIRiS41610. HYRSAC.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ATLX-ray1.80A/B192-393[»]
1DTHX-ray2.00A/B191-393[»]
1HTDX-ray2.10A/B192-393[»]
ProteinModelPortaliP15167.
SMRiP15167. Positions 192-393.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM12.144.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA03352.

Phylogenomic databases

HOVERGENiHBG006978.

Enzyme and pathway databases

BRENDAi3.4.24.42. 1710.

Miscellaneous databases

EvolutionaryTraceiP15167.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVM1AD_CROAT
AccessioniPrimary (citable) accession number: P15167
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 1, 1996
Last modified: March 16, 2016
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.