P30403

PR
Gene name
Protein name
Zinc metalloproteinase/disintegrin
Names
Species
Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
KEGG Pathway
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

10-83 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

19 structures for P30403

Entry ID Method Resolution Chain Position Source
1N4Y NMR - A 408-475 PDB
1Q7I NMR - A 408-475 PDB
1Q7J NMR - A 408-475 PDB
2LJV NMR - A 408-475 PDB
2M75 NMR - A 408-475 PDB
2M7F NMR - A 408-478 PDB
2M7H NMR - A 408-478 PDB
2PJF NMR - A 408-475 PDB
2PJG NMR - A 408-475 PDB
2PJI NMR - A 408-475 PDB
3UCI X-ray 135 A A 408-475 PDB
4M4C X-ray 180 A A/B/C/D 408-475 PDB
4R5R X-ray 096 A A/B 408-475 PDB
4R5U X-ray 181 A A/B 408-475 PDB
4RQG X-ray 166 A A/B 408-475 PDB
7X4S X-ray 180 A A/B 408-475 PDB
7X4V X-ray 138 A A/B 408-475 PDB
7X4Z X-ray 148 A A/B 408-475 PDB
AF-P30403-F1 Predicted AlphaFoldDB

No variants for P30403

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P30403

No associated diseases with P30403

5 regional properties for P30403

Type Name Position InterPro Accession
domain Peptidase M12B, ADAM/reprolysin 194 - 391 IPR001590
domain Disintegrin domain 397 - 478 IPR001762
domain Peptidase M12B, propeptide 46 - 149 IPR002870
conserved_site Disintegrin, conserved site 434 - 453 IPR018358
domain Reprolysin domain, adamalysin-type 194 - 389 IPR034027

Functions

Description
EC Number
Subcellular Localization
  • [Snake venom metalloproteinase rhodostoxin]: Secreted
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.

3 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
metalloendopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
toxin activity Interacting selectively with one or more biological molecules in another (target) organism, initiating pathogenesis (leading to an abnormal, generally detrimental state) in the target organism. The activity should refer to an evolved function of the active gene product, i.e. one that was selected for. Examples include the activity of botulinum toxin, and snake venom.

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIQVLLVTIC LAAFPYQGSS IILESGNVND YEVVYPRKVI ALSEGAAQQK YEDTMQYEFK
70 80 90 100 110 120
VNGEPVVLHL EKNKGLFAKD YSETHYSPDG TRITTYPSVE DHCYYQGRIH NDADSTASIS
130 140 150 160 170 180
ACNGLKGHFK LQGETYFIEP MKLPDSEAHA VFKYENIEKE DESPKMCGVT ETNWESDEPI
190 200 210 220 230 240
KKVSQLNLNH EIKRHVDIVV VVDSRFCTKH SNDLEVIRKF VHEVVNAIIE SYKYMHFGIS
250 260 270 280 290 300
LVNLETWCNG DLINVQEDSY ETLKAFGKWR ESDLIKHVNH SNAQFLMDMK FIKNIIGKAY
310 320 330 340 350 360
LDSICDPERS VGIVQNYHGI TLNVAAIMAH EMGHNLGVRH DGEYCTCYGS SECIMSSHIS
370 380 390 400 410 420
DPPSKYFSNC SYYQFWKYIE NQNPQCILNK PLRTVSIPVS GNEHLEAGKE CDCSSPENPC
430 440 450 460 470
CDAATCKLRP GAQCGEGLCC EQCKFSRAGK ICRIPRGDMP DDRCTGQSAD CPRYHSHA