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Blood coagulation inhibitor (disintegrin) superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   Small proteins [ 56992] (90)
Fold:   Blood coagulation inhibitor (disintegrin) [ 57551]
Superfamily:   Blood coagulation inhibitor (disintegrin) [ 57552]
Families:   Blood coagulation inhibitor (disintegrin) [ 57553] (6)


Superfamily statistics
Genomes (305) Uniprot 2018_03 genome PDB chains (SCOP 1.75)
Domains 2,612 8,186 13
Proteins 2,492 7,853 13


Functional annotation
General category Processes_EC
Detailed category Blood clotting

Document:
Function annotation of SCOP domain superfamilies

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)Acting on peptide bonds (peptide hydrolases)0Least InformativeDirect
Enzyme Commission (EC)Metalloendopeptidases0InformativeDirect

Document: EC annotation of SCOP domains

Disease Ontology (DO)

(show details)
DO termFDR (all)SDDO levelAnnotation (direct or inherited)
Disease Ontology (DO)organ system cancer0.003314Least InformativeInherited
Disease Ontology (DO)artery disease0.0007385Moderately InformativeDirect
Disease Ontology (DO)atherosclerosis0.00002011InformativeDirect
Disease Ontology (DO)integumentary system cancer0.00542Highly InformativeInherited

Document: DO annotation of SCOP domains

Mouse Phenotype (MP)

(show details)
MP termFDR (all)SDMP levelAnnotation (direct or inherited)
Mammalian Phenotype (MP)cardiovascular system phenotype0.4318Least InformativeInherited
Mammalian Phenotype (MP)abnormal heart morphology0.08088Moderately InformativeInherited
Mammalian Phenotype (MP)reproductive system phenotype0.2217Moderately InformativeInherited
Mammalian Phenotype (MP)abnormal eye morphology0.3199Moderately InformativeInherited
Mammalian Phenotype (MP)abnormal heart ventricle morphology0.07145InformativeInherited
Mammalian Phenotype (MP)abnormal semilunar valve morphology0.000001343Highly InformativeDirect
Mammalian Phenotype (MP)abnormal heart ventricle outflow tract morphology0.000001343Highly InformativeDirect
Mammalian Phenotype (MP)abnormal atrioventricular valve morphology0.000002036Highly InformativeDirect
Mammalian Phenotype (MP)abnormal fertilization0.00000752Highly InformativeDirect
Mammalian Phenotype (MP)abnormal heart right ventricle morphology0.00006779Highly InformativeDirect
Mammalian Phenotype (MP)ventricular septal defect0.0002373Highly InformativeDirect
Mammalian Phenotype (MP)double outlet right ventricle0.0003109Highly InformativeDirect
Mammalian Phenotype (MP)abnormal eyelid morphology0.003006Highly InformativeInherited

Document: MP annotation of SCOP domains

Worm Phenotype (WP)

(show details)
WP termFDR (all)SDWP levelAnnotation (direct or inherited)
Worm Phenotype (WP)general pace of development variant0Least InformativeDirect
Worm Phenotype (WP)larval lethal0Least InformativeDirect
Worm Phenotype (WP)retarded heterochronic variations0Least InformativeDirect
Worm Phenotype (WP)cell development variant0Least InformativeDirect
Worm Phenotype (WP)larval development variant0Least InformativeDirect
Worm Phenotype (WP)larval growth variant0Least InformativeDirect
Worm Phenotype (WP)pericellular component development variant0Moderately InformativeDirect
Worm Phenotype (WP)sterile progeny0Moderately InformativeDirect
Worm Phenotype (WP)basement membrane remodeling variant0InformativeDirect

Document: WP annotation of SCOP domains

Xenopus Anatomy (XA)

(show details) Document: XA annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Hydrolases0Least InformativeDirect
Enzyme Commission (EC)Acting on peptide bonds (peptidases)0Moderately InformativeDirect
Enzyme Commission (EC)Metalloendopeptidases0InformativeDirect

Document: EC annotation of SCOP domains

InterPro annotation
Cross references IPR001762 SSF57552 Protein matches
Abstract

Disintegrins are a family of small proteins from viper venoms that function as potent inhibitors of both platelet aggregation and integrin-dependent cell adhesion [PubMed15578957, PubMed15974889]. Integrin receptors are involved in cell-cell and cell-extracellular matrix interactions, serving as the final common pathway leading to aggregation via formation of platelet-platelet bridges, which are essential in thrombosis and haemostasis. Disintegrins contain an RGD (Arg-Gly-Asp) or KGD (Lys-Gly-Asp) sequence motif that binds specifically to integrin IIb-IIIa receptors on the platelet surface, thereby blocking the binding of fibrinogen to the receptor-glycoprotein complex of activated platelets. Disintegrins act as receptor antagonists, inhibiting aggregation induced by ADP, thrombin, platelet-activating factor and collagen [PubMed12050803]. The role of disintegrin in preventing blood coagulation renders it of medical interest, particularly with regard to its use as an anti-coagulant [PubMed16918409].

Disintegrins from different snake species have been characterised: albolabrin, applagin, barbourin, batroxostatin, bitistatin, obtustatin [PubMed12742023], schistatin [PubMed16101289], echistatin [PubMed15535803], elegantin, eristicophin, flavoridin [PubMed14499613], halysin, kistrin, tergeminin, salmosin [PubMed14661951] and triflavin.

Disintegrin-like proteins are found in various species ranging from slime mold to humans. Some other proteins known to contain a disintegrin domain are:

  • Some snake venom zinc metalloproteinases [PubMed15962120] consist of an N-terminal catalytic domain fused to a disintegrin domain. Such is the case for trimerelysin I (HR1B), atrolysin-e (Ht-e) and trigramin. It has been suggested that these proteinases are able to cleave themselves from the disintegrin domains and that the latter may arise from such a post-translational processing.
  • The beta-subunit of guinea pig sperm surface protein PH30 [PubMed1552944]. PH30 is a protein involved in sperm-egg fusion. The beta subunit contains a disintegrin at the N-terminal extremity.
  • Mammalian epididymial apical protein 1 (EAP I) [PubMed1417724]. EAP I is associated with the sperm membrane and may play a role in sperm maturation. Structurally, EAP I consists of an N-terminal domain, followed by a zinc metalloproteinase domain, a disintegrin domain, and a large C-terminal domain that contains a transmembrane region.

InterPro database


PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Disease Ontology (DO) · Mouse Phenotype (MP) · Worm Phenotype (WP) · Xenopus Anatomy (XA) · Enzyme Commission (EC) ]

Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 9 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a Blood coagulation inhibitor (disintegrin) domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 9 hidden Markov models representing the Blood coagulation inhibitor (disintegrin) superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Disease Ontology (DO) · Mouse Phenotype (MP) · Worm Phenotype (WP) · Xenopus Anatomy (XA) · Enzyme Commission (EC) · Internal database links ]