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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)DescriptionActionsGraphical viewLength
Metal bindingi200Calcium1
Metal bindingi284Calcium1
Metal bindingi333Zinc; catalytic1
Active sitei3341
Metal bindingi337Zinc; catalytic1
Metal bindingi343Zinc; catalytic1
Metal bindingi388Calcium; via carbonyl oxygen1
Metal bindingi391Calcium1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000002900021 – 1901 PublicationAdd BLAST170
ChainiPRO_0000029001191 – 393Snake venom metalloproteinase atrolysin-DAdd BLAST203
PropeptideiPRO_0000029002394 – 414Add BLAST21

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei191Pyrrolidone carboxylic acid1 Publication1
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

1414
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi197 – 205Combined sources9
Helixi207 – 212Combined sources6
Turni213 – 215Combined sources3
Helixi217 – 235Combined sources19
Helixi236 – 238Combined sources3
Beta strandi240 – 249Combined sources10
Helixi262 – 275Combined sources14
Helixi277 – 280Combined sources4
Beta strandi284 – 290Combined sources7
Beta strandi295 – 297Combined sources3
Turni310 – 312Combined sources3
Beta strandi313 – 318Combined sources6
Helixi324 – 338Combined sources15
Beta strandi353 – 355Combined sources3
Beta strandi358 – 360Combined sources3
Helixi371 – 384Combined sources14
Helixi388 – 390Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP15167.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini197 – 393Peptidase M12BPROSITE-ProRule annotationAdd BLAST197

Sequence similaritiesi

Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006978.
KOiK20746.

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)DescriptionActionsGraphical viewLength
Natural varianti191Missing in some chains. 1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ATLX-ray1.80A/B192-393[»]
1DTHX-ray2.00A/B191-393[»]
1HTDX-ray2.10A/B192-393[»]
ProteinModelPortaliP15167.
SMRiP15167.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM12.144.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA03352.

Phylogenomic databases

HOVERGENiHBG006978.
KOiK20746.

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: November 2, 2016
This is version 115 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.