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Protein

Zinc metalloproteinase/disintegrin

Gene
N/A
Organism
Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Snake venom metalloproteinase rhodostoxin: impairs hemostasis in the envenomed animal.By similarity
Disintegrin rhodostomin: inhibit platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors alpha-IIb/beta-3 (ITGA2B/ITGB3).

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi330Zinc; catalyticCurated1
Active sitei331PROSITE-ProRule annotation1
Metal bindingi334Zinc; catalyticCurated1
Metal bindingi340Zinc; catalyticCurated1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.161.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc metalloproteinase/disintegrin
Cleaved into the following 2 chains:
Alternative name(s):
Hemorrhagic protein
Disintegrin rhodostomin
Short name:
RHO
Short name:
RHOD
Alternative name(s):
Disintegrin kistrin
Platelet aggregation activation inhibitor
OrganismiCalloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
Taxonomic identifieri8717 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCalloselasma

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_000002895621 – 1881 PublicationAdd BLAST168
ChainiPRO_0000028957189 – 391Snake venom metalloproteinase rhodostoxinAdd BLAST203
PropeptideiPRO_0000028958392 – 407Add BLAST16
ChainiPRO_0000028959408 – 475Disintegrin rhodostominAdd BLAST68
PropeptideiPRO_0000028960476 – 4783

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi207 ↔ 248
Glycosylationi279N-linked (GlcNAc...) (complex)1 Publication1
Disulfide bondi305 ↔ 386
Disulfide bondi345 ↔ 370Curated
Disulfide bondi347 ↔ 353Curated
Glycosylationi369N-linked (GlcNAc...) (complex)1 Publication1
Disulfide bondi411 ↔ 426
Disulfide bondi413 ↔ 421
Disulfide bondi420 ↔ 443
Disulfide bondi434 ↔ 440
Disulfide bondi439 ↔ 464
Disulfide bondi452 ↔ 471

Post-translational modificationi

Glycans are composed of 4 GlcNAc, 3 Man, 2 Gal, 2 NeuAC and 1 Fuc residue.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Monomeric (disintegrin).By similarity

Structurei

Secondary structure

1478
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi408 – 410Combined sources3
Beta strandi412 – 414Combined sources3
Beta strandi419 – 421Combined sources3
Turni423 – 425Combined sources3
Beta strandi426 – 428Combined sources3
Beta strandi429 – 431Combined sources3
Beta strandi435 – 437Combined sources3
Beta strandi438 – 441Combined sources4
Beta strandi451 – 453Combined sources3
Beta strandi456 – 458Combined sources3
Beta strandi461 – 463Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N4YNMR-A408-475[»]
1Q7INMR-A408-475[»]
1Q7JNMR-A408-475[»]
2LJVNMR-A408-475[»]
2M75NMR-A408-475[»]
2M7FNMR-A408-478[»]
2M7HNMR-A408-478[»]
2PJFNMR-A408-475[»]
2PJGNMR-A408-475[»]
2PJINMR-A408-475[»]
3UCIX-ray1.35A408-475[»]
4M4CX-ray1.80A/B/C/D408-475[»]
4R5RX-ray0.96A/B408-475[»]
4R5UX-ray1.81A/B408-475[»]
4RQGX-ray1.66A/B408-475[»]
ProteinModelPortaliP30403.
SMRiP30403.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30403.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini194 – 391Peptidase M12BPROSITE-ProRule annotationAdd BLAST198
Domaini397 – 478DisintegrinPROSITE-ProRule annotationAdd BLAST82

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi456 – 458Cell 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.

P30403-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQVLLVTIC LAAFPYQGSS IILESGNVND YEVVYPRKVI ALSEGAAQQK
60 70 80 90 100
YEDTMQYEFK VNGEPVVLHL EKNKGLFAKD YSETHYSPDG TRITTYPSVE
110 120 130 140 150
DHCYYQGRIH NDADSTASIS ACNGLKGHFK LQGETYFIEP MKLPDSEAHA
160 170 180 190 200
VFKYENIEKE DESPKMCGVT ETNWESDEPI KKVSQLNLNH EIKRHVDIVV
210 220 230 240 250
VVDSRFCTKH SNDLEVIRKF VHEVVNAIIE SYKYMHFGIS LVNLETWCNG
260 270 280 290 300
DLINVQEDSY ETLKAFGKWR ESDLIKHVNH SNAQFLMDMK FIKNIIGKAY
310 320 330 340 350
LDSICDPERS VGIVQNYHGI TLNVAAIMAH EMGHNLGVRH DGEYCTCYGS
360 370 380 390 400
SECIMSSHIS DPPSKYFSNC SYYQFWKYIE NQNPQCILNK PLRTVSIPVS
410 420 430 440 450
GNEHLEAGKE CDCSSPENPC CDAATCKLRP GAQCGEGLCC EQCKFSRAGK
460 470
ICRIPRGDMP DDRCTGQSAD CPRYHSHA
Length:478
Mass (Da):54,006
Last modified:February 1, 1994 - v2
Checksum:i6490A2B171D3A830
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti287M → T AA sequence (PubMed:8561498).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08780 mRNA. Translation: AAA49196.1.
PIRiS33792. JQ1301.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08780 mRNA. Translation: AAA49196.1.
PIRiS33792. JQ1301.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N4YNMR-A408-475[»]
1Q7INMR-A408-475[»]
1Q7JNMR-A408-475[»]
2LJVNMR-A408-475[»]
2M75NMR-A408-475[»]
2M7FNMR-A408-478[»]
2M7HNMR-A408-478[»]
2PJFNMR-A408-475[»]
2PJGNMR-A408-475[»]
2PJINMR-A408-475[»]
3UCIX-ray1.35A408-475[»]
4M4CX-ray1.80A/B/C/D408-475[»]
4R5RX-ray0.96A/B408-475[»]
4R5UX-ray1.81A/B408-475[»]
4RQGX-ray1.66A/B408-475[»]
ProteinModelPortaliP30403.
SMRiP30403.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM12.161.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006978.

Miscellaneous databases

EvolutionaryTraceiP30403.

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 nameiVM2RH_CALRH
AccessioniPrimary (citable) accession number: P30403
Secondary accession number(s): P17494
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1994
Last modified: November 2, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin 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.