Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi330 – 3301Zinc; catalyticCurated
Active sitei331 – 3311PROSITE-ProRule annotation
Metal bindingi334 – 3341Zinc; catalyticCurated
Metal bindingi340 – 3401Zinc; catalyticCurated

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Propeptidei21 – 1881681 PublicationPRO_0000028956Add
BLAST
Chaini189 – 391203Snake venom metalloproteinase rhodostoxinPRO_0000028957Add
BLAST
Propeptidei392 – 40716PRO_0000028958Add
BLAST
Chaini408 – 47568Disintegrin rhodostominPRO_0000028959Add
BLAST
Propeptidei476 – 4783PRO_0000028960

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi207 ↔ 248
Glycosylationi279 – 2791N-linked (GlcNAc...) (complex)1 Publication
Disulfide bondi305 ↔ 386
Disulfide bondi345 ↔ 370Curated
Disulfide bondi347 ↔ 353Curated
Glycosylationi369 – 3691N-linked (GlcNAc...) (complex)1 Publication
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

1
478
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi408 – 4103Combined sources
Beta strandi412 – 4143Combined sources
Beta strandi419 – 4213Combined sources
Turni423 – 4253Combined sources
Beta strandi426 – 4283Combined sources
Beta strandi429 – 4313Combined sources
Beta strandi435 – 4373Combined sources
Beta strandi438 – 4414Combined sources
Beta strandi451 – 4533Combined sources
Beta strandi456 – 4583Combined sources
Beta strandi461 – 4633Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 193-475.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30403.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini194 – 391198Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini397 – 47882DisintegrinPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi456 – 4583Cell attachment site

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2871M → T AA sequence (PubMed:8561498).Curated

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
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. Positions 193-475.
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...

Publicationsi

  1. "Nucleotide sequence of a full-length cDNA encoding a common precursor of platelet aggregation inhibitor and hemorrhagic protein from Calloselasma rhodostoma venom."
    Au L.-C.
    Biochim. Biophys. Acta 1173:243-245(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  2. "A common precursor for a putative hemorrhagic protein and rhodostomin, a platelet aggregation inhibitor of the venom of Calloselasma rhodostoma: molecular cloning and sequence analysis."
    Au L.-C., Huang Y.-B., Huang T.-F., Teh G.-W., Lin H.-H., Choo K.-B.
    Biochem. Biophys. Res. Commun. 181:585-593(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 77-478.
    Tissue: Venom gland.
  3. "Rhodostomin, an RGD-containing peptide expressed from a synthetic gene in Escherichia coli, facilitates the attachment of human hepatoma cells."
    Chang H.H., Hu S.T., Huang T.-F., Chen S.H., Lee Y.H., Lo S.J.
    Biochem. Biophys. Res. Commun. 190:242-249(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 408-475.
    Tissue: Venom gland.
  4. "Structural studies of a major hemorrhagin (rhodostoxin) from the venom of Calloselasma rhodostoma (Malayan pit viper)."
    Chung M.C., Ponnudurai G., Kataoka M., Shimizu S., Tan N.H.
    Arch. Biochem. Biophys. 325:199-208(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 189-391, DISULFIDE BONDS, GLYCOSYLATION AT ASN-279 AND ASN-369, GLYCAN STRUCTURE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Venom.
  5. Cited for: PROTEIN SEQUENCE OF 408-475.
    Tissue: Venom.
  6. "Platelet glycoprotein IIb-IIIa protein antagonists from snake venoms: evidence for a family of platelet-aggregation inhibitors."
    Dennis M.S., Henzel W.J., Pitti R.M., Lipari M.T., Napier M.A., Deisher T.A., Bunting S., Lazarus R.A.
    Proc. Natl. Acad. Sci. U.S.A. 87:2471-2475(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 408-475.
    Tissue: Venom.
  7. "Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical analysis, and structure calculations."
    Adler M., Carter P., Lazarus R.A., Wagner G.
    Biochemistry 32:282-289(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 408-475, DISULFIDE BONDS.
  8. "Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist."
    Adler M., Lazarus R.A., Dennis M.S., Wagner G.
    Science 253:445-448(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 408-475.
  9. "Sequential 1H NMR assignments of kistrin, a potent platelet aggregation inhibitor and glycoprotein IIb-IIIa antagonist."
    Adler M., Wagner G.
    Biochemistry 31:1031-1039(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 408-475.

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: February 17, 2016
This is version 125 of the entry and version 2 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.