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Protein

Coagulation factor X-activating enzyme heavy chain

Gene
N/A
Organism
Daboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) by cleaving the Arg-Ile bond and is also able to activate coagulation factor IX (F9) and protein S (PROS1) by specific cleavage of Arg-Ile and Arg-Val bonds.1 Publication

Catalytic activityi

Specifically activates several components of the blood clotting system, including coagulation factor X, coagulation factor IX and protein C by cleavage of Arg-|-Xaa bonds. Has no action on insulin B chain.2 Publications

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi333Zinc; catalytic1
Active sitei334PROSITE-ProRule annotation1
Metal bindingi337Zinc; catalytic1
Metal bindingi343Zinc; catalytic1
Metal bindingi403Calcium 1; via carbonyl oxygen1
Metal bindingi406Calcium 11
Metal bindingi408Calcium 1; via carbonyl oxygen1
Metal bindingi410Calcium 11
Metal bindingi413Calcium 11
Metal bindingi416Calcium 11
Metal bindingi467Calcium 21
Metal bindingi468Calcium 2; via carbonyl oxygen1
Metal bindingi470Calcium 21
Metal bindingi482Calcium 21
Metal bindingi483Calcium 2; via carbonyl oxygen1

GO - Molecular functioni

Keywordsi

Molecular functionBlood coagulation cascade activating toxin, Hemostasis impairing toxin, Hydrolase, Metalloprotease, Protease, Toxin
LigandCalcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.158.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor X-activating enzyme heavy chain (EC:3.4.24.58)
Alternative name(s):
Coagulation factor X-activating enzyme chain alpha
RVV-X heavy chain
Russellysin
Snake venom metalloproteinase
Short name:
SVMP
OrganismiDaboia siamensis (Eastern Russel's viper) (Daboia russelii siamensis)
Taxonomic identifieri343250 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeViperinaeDaboia

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000035522621 – 1882 PublicationsAdd BLAST168
ChainiPRO_0000078204189 – 619Coagulation factor X-activating enzyme heavy chainAdd BLAST431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi215 ↔ 2511 Publication
Glycosylationi216N-linked (GlcNAc...) (complex) asparagine1 Publication1
Glycosylationi257N-linked (GlcNAc...) (complex) asparagine2 Publications1
Disulfide bondi308 ↔ 3881 Publication
Disulfide bondi348 ↔ 3721 Publication
Disulfide bondi350 ↔ 3551 Publication
Glycosylationi351N-linked (GlcNAc...) (complex) asparagine1 Publication1
Glycosylationi371N-linked (GlcNAc...) (complex) asparagine2 Publications1
Disulfide bondi404 ↔ 4331 Publication
Disulfide bondi415 ↔ 4281 Publication
Disulfide bondi417 ↔ 4231 Publication
Disulfide bondi427 ↔ 4501 Publication
Disulfide bondi441 ↔ 4471 Publication
Disulfide bondi446 ↔ 4721 Publication
Disulfide bondi459 ↔ 4791 Publication
Disulfide bondi466 ↔ 4981 Publication
Disulfide bondi491 ↔ 5031 Publication
Disulfide bondi510 ↔ 5601 Publication
Disulfide bondi525 ↔ 5711 Publication
Disulfide bondi538 ↔ 5481 Publication
Disulfide bondi555 ↔ 5971 Publication
Disulfide bondi577Interchain (with C-158 in coagulation factor X-activating enzyme light chain LC2)PROSITE-ProRule annotation1 Publication
Disulfide bondi591 ↔ 6031 Publication

Post-translational modificationi

N-glycosylated; probably required for conformation. Removal of easily accessible sugars does not change its functional capacity, but removal of the core sugars with N-glycanase causes a virtually complete loss of enzyme activity, apparently as a result of major conformational changes in the molecule. Not O-glycosylated.4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

iPTMnetiQ7LZ61.

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterotrimer; disulfide-linked. The heterotrimer consists of 1 heavy chain and 2 light chains (lectins): LC1 and LC2.2 Publications

Structurei

Secondary structure

1619
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi199 – 207Combined sources9
Turni209 – 214Combined sources6
Helixi219 – 235Combined sources17
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 – 337Combined sources14
Turni338 – 340Combined sources3
Helixi371 – 384Combined sources14
Helixi395 – 397Combined sources3
Turni430 – 432Combined sources3
Beta strandi442 – 444Combined sources3
Beta strandi458 – 460Combined sources3
Turni492 – 495Combined sources4
Helixi506 – 514Combined sources9
Helixi523 – 530Combined sources8
Beta strandi534 – 536Combined sources3
Helixi553 – 555Combined sources3
Beta strandi570 – 573Combined sources4
Beta strandi590 – 592Combined sources3
Beta strandi595 – 597Combined sources3
Beta strandi603 – 605Combined sources3
Helixi606 – 609Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2E3XX-ray2.91A189-615[»]
ProteinModelPortaliQ7LZ61.
SMRiQ7LZ61.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7LZ61.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini199 – 393Peptidase M12BPROSITE-ProRule annotationAdd BLAST195
Domaini401 – 487DisintegrinPROSITE-ProRule annotationAdd BLAST87

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi465 – 467D/ECD-tripeptide3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi488 – 615Cys-richAdd BLAST128

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006978.
KOiK20748.

Family and domain databases

CDDicd04269. ZnMc_adamalysin_II_like. 1 hit.
Gene3Di3.40.390.10. 1 hit.
4.10.70.10. 1 hit.
InterProiView protein in InterPro
IPR006586. ADAM_Cys-rich.
IPR018358. Disintegrin_CS.
IPR001762. Disintegrin_dom.
IPR036436. Disintegrin_dom_sf.
IPR024079. MetalloPept_cat_dom_sf.
IPR001590. Peptidase_M12B.
IPR002870. Peptidase_M12B_N.
IPR034027. Reprolysin_adamalysin.
PfamiView protein in Pfam
PF08516. ADAM_CR. 1 hit.
PF00200. Disintegrin. 1 hit.
PF01562. Pep_M12B_propep. 1 hit.
PF01421. Reprolysin. 1 hit.
PRINTSiPR00289. DISINTEGRIN.
SMARTiView protein in SMART
SM00608. ACR. 1 hit.
SM00050. DISIN. 1 hit.
SUPFAMiSSF57552. SSF57552. 1 hit.
PROSITEiView protein in PROSITE
PS50215. ADAM_MEPRO. 1 hit.
PS00427. DISINTEGRIN_1. 1 hit.
PS50214. DISINTEGRIN_2. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7LZ61-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMQVLLVTIS LAVFPYQGSS IILESGNVND YEVVYPQKVT ALPKGAVQQP
60 70 80 90 100
EQKYEDTMQY EFEVNGEPVV LHLEKNKILF SEDYSETHYY PDGREITTNP
110 120 130 140 150
PVEDHCYYHG RIQNDAHSSA SISACNGLKG HFKLRGEMYF IEPLKLSNSE
160 170 180 190 200
AHAVYKYENI EKEDEIPKMC GVTQTNWESD KPIKKASQLV STSAQFNKIF
210 220 230 240 250
IELVIIVDHS MAKKCNSTAT NTKIYEIVNS ANEIFNPLNI HVTLIGVEFW
260 270 280 290 300
CDRDLINVTS SADETLNSFG EWRASDLMTR KSHDNALLFT DMRFDLNTLG
310 320 330 340 350
ITFLAGMCQA YRSVEIVQEQ GNRNFKTAVI MAHELSHNLG MYHDGKNCIC
360 370 380 390 400
NDSSCVMSPV LSDQPSKLFS NCSIHDYQRY LTRYKPKCIF NPPLRKDIVS
410 420 430 440 450
PPVCGNEIWE EGEECDCGSP ANCQNPCCDA ATCKLKPGAE CGNGLCCYQC
460 470 480 490 500
KIKTAGTVCR RARDECDVPE HCTGQSAECP RDQLQQNGKP CQNNRGYCYN
510 520 530 540 550
GDCPIMRNQC ISLFGSRANV AKDSCFQENL KGSYYGYCRK ENGRKIPCAP
560 570 580 590 600
QDVKCGRLFC LNNSPRNKNP CNMHYSCMDQ HKGMVDPGTK CEDGKVCNNK
610
RQCVDVNTAY QSTTGFSQI
Length:619
Mass (Da):69,648
Last modified:November 25, 2008 - v2
Checksum:i71084A3B46338797
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti191S → A AA sequence (PubMed:8144654).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ137799 mRNA. Translation: AAZ39881.1.
PIRiA42972.

Genome annotation databases

KEGGiag:AAZ39881.

Similar proteinsi

Entry informationi

Entry nameiVM3CX_DABSI
AccessioniPrimary (citable) accession number: Q7LZ61
Secondary accession number(s): B4UT23
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: November 25, 2008
Last modified: November 22, 2017
This is version 83 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families