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Protein

Zinc metalloproteinase/disintegrin

Gene
N/A
Organism
Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Snake venom metalloproteinase TM-3: fibrin(ogen)olytic protease which cleaves the Aalpha chain of fibrinogen (FGA) first followed by the Bbeta chain (FGB) and shows relatively low activity on the gamma chain (FGG).
Disintegrin trimucrin: inhibits platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3).

Cofactori

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

Enzyme regulationi

Inhibited by EDTA and 1,10-phenanthroline.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi333Zinc; catalytic1
Active sitei3341
Metal bindingi337Zinc; catalytic1
Metal bindingi343Zinc; catalytic1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Cell adhesion impairing toxin, Fibrinogenolytic toxin, Fibrinolytic toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Platelet aggregation inhibiting toxin, Protease, Toxin

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.157.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc metalloproteinase/disintegrin
Cleaved into the following 2 chains:
Alternative name(s):
Fibrinlysin
Trimutase
OrganismiProtobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus)
Taxonomic identifieri103944 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeProtobothrops

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_000032261221 – 189Add BLAST169
ChainiPRO_5000053304190 – 392Snake venom metalloproteinase TM-3Add BLAST203
PropeptideiPRO_0000322613393 – 408By similarityAdd BLAST16
ChainiPRO_0000322614409 – 481Disintegrin trimucrinBy similarityAdd BLAST73

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi308 ↔ 387
Disulfide bondi349 ↔ 371
Disulfide bondi351 ↔ 354
Disulfide bondi414 ↔ 429By similarity
Disulfide bondi416 ↔ 424By similarity
Disulfide bondi423 ↔ 446By similarity
Disulfide bondi437 ↔ 443By similarity
Disulfide bondi442 ↔ 467By similarity
Disulfide bondi455 ↔ 474By similarity

Keywords - PTMi

Disulfide bond, Zymogen

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1481
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
Helixi295 – 297Combined sources3
Beta strandi300 – 302Combined sources3
Turni310 – 312Combined sources3
Beta strandi313 – 318Combined sources6
Helixi324 – 338Combined sources15
Turni346 – 348Combined sources3
Beta strandi352 – 354Combined sources3
Helixi370 – 382Combined sources13
Helixi386 – 389Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KUFX-ray1.35A190-392[»]
1KUGX-ray1.37A190-392[»]
1KUIX-ray1.50A190-392[»]
1KUKX-ray1.45A190-392[»]
ProteinModelPortaliO57413.
SMRiO57413.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO57413.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini197 – 392Peptidase M12BPROSITE-ProRule annotationAdd BLAST196
Domaini400 – 481DisintegrinPROSITE-ProRule annotationAdd BLAST82

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi459 – 461Cell attachment site3

Sequence similaritiesi

Contains 1 disintegrin domain.PROSITE-ProRule annotation
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006978.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 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.

O57413-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIEVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPRKVS ALPKGAVQPK
60 70 80 90 100
YEDAMQYEFK VNGEAVVLHL EKNKGLFSED YSETHYSPDG REITTYPSVE
110 120 130 140 150
DHCYYHGRIH NDADSTASIS ACDGLKGYFK LQGETYPIEP LELSDSEAHA
160 170 180 190 200
VFKYENVEKE DEAPKMCGVT QNWESDESIK KASQLYLTPE QQRFPQRYIK
210 220 230 240 250
LAIVVDHGMY TKYSSNFKKI RKRVHQMVSN INEMCRPLNI AITLALLDVW
260 270 280 290 300
SEKDFITVQA DAPTTAGLFG DWRERVLLKK KNHDHAQLLT DTNFARNTIG
310 320 330 340 350
WAYVGRMCDE KYSVAVVKDH SSKVFMVAVT MTHELGHNLG MEHDDKDKCK
360 370 380 390 400
CDTCIMSAVI SDKQSKLFSD CSKDYYQTFL TNDNPQCILN APLRTDTVST
410 420 430 440 450
PVSGNEFLEA GEECDCGSPE NPCCDAATCK LRPGAQCAEG LCCDQCRFKK
460 470 480
KRTICRRARG DNPDDRCTGQ SADCPRNGLY G
Length:481
Mass (Da):54,178
Last modified:June 1, 1998 - v1
Checksum:iC38714924F6091DF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3E → Q in CAA54364 (PubMed:8068721).Curated1
Sequence conflicti7V → M in CAA54364 (PubMed:8068721).Curated1
Sequence conflicti29N → D in CAA54364 (PubMed:8068721).Curated1
Sequence conflicti37R → A in CAA54364 (PubMed:8068721).Curated1
Sequence conflicti40S → T in CAA54364 (PubMed:8068721).Curated1
Sequence conflicti200K → E (PubMed:12077431).Curated1
Sequence conflicti200K → E (PubMed:12071970).Curated1
Sequence conflicti368F → S in CAA54364 (PubMed:8068721).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF011909 mRNA. Translation: AAB94016.1.
X77089 mRNA. Translation: CAA54364.1.
AF519177 mRNA. Translation: AAP80728.1.
PIRiS47570. S43125.
RefSeqiNP_001310177.1. NM_001323248.1.

Genome annotation databases

GeneIDi107298299.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF011909 mRNA. Translation: AAB94016.1.
X77089 mRNA. Translation: CAA54364.1.
AF519177 mRNA. Translation: AAP80728.1.
PIRiS47570. S43125.
RefSeqiNP_001310177.1. NM_001323248.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KUFX-ray1.35A190-392[»]
1KUGX-ray1.37A190-392[»]
1KUIX-ray1.50A190-392[»]
1KUKX-ray1.45A190-392[»]
ProteinModelPortaliO57413.
SMRiO57413.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM12.157.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi107298299.

Phylogenomic databases

HOVERGENiHBG006978.

Miscellaneous databases

EvolutionaryTraceiO57413.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiIPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
[Graphical view]
PfamiPF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
[Graphical view]
PRINTSiPR00289. DISINTEGRIN.
SMARTiSM00050. DISIN. 1 hit.
[Graphical view]
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVM2T3_PROMU
AccessioniPrimary (citable) accession number: O57413
Secondary accession number(s): Q7T1S1, Q91505
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 1, 1998
Last modified: November 2, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This disintegrin is 100% identical to the disintegrin of AC E9NW27, another disintegrin of the P-II subfamily of Protobothrops mucrosquamatus.
The disintegrin belongs to the medium disintegrin subfamily.

Keywords - Technical termi

3D-structure

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.