VM3H3_BOTJA
ID VM3H3_BOTJA Reviewed; 606 AA.
AC Q98UF9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like HF3 {ECO:0000303|PubMed:15336556};
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Bothrops jararaca (Jararaca) (Bothrops jajaraca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX NCBI_TaxID=8724;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 248-253; 257-268; 273-276;
RP 296-303 AND 395-420, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=15336556; DOI=10.1016/j.bbrc.2004.08.012;
RA Silva C.A., Zuliani J.P., Assakura M.T., Mentele R., Camargo A.C.M.,
RA Teixeira C.F.P., Serrano S.M.T.;
RT "Activation of alpha(M)beta(2)-mediated phagocytosis by HF3, a P-III class
RT metalloproteinase isolated from the venom of Bothrops jararaca.";
RL Biochem. Biophys. Res. Commun. 322:950-956(2004).
RN [2]
RP FUNCTION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=3136558; DOI=10.1016/0041-0101(88)90006-2;
RA Mandelbaum F.R., Assakura M.T.;
RT "Antigenic relationship of hemorrhagic factors and proteases isolated from
RT the venoms of three species of Bothrops snakes.";
RL Toxicon 26:379-385(1988).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Venom;
RX PubMed=20146532; DOI=10.1021/pr901027r;
RA Zelanis A., Tashima A.K., Rocha M.M., Furtado M.F., Camargo A.C., Ho P.L.,
RA Serrano S.M.;
RT "Analysis of the ontogenetic variation in the venom proteome/peptidome of
RT Bothrops jararaca reveals different strategies to deal with prey.";
RL J. Proteome Res. 9:2278-2291(2010).
RN [4]
RP FUNCTION.
RX PubMed=27020778; DOI=10.1007/s00726-016-2218-z;
RA Bertholim L., Zelanis A., Oliveira A.K., Serrano S.M.;
RT "Proteome-derived peptide library for the elucidation of the cleavage
RT specificity of HF3, a snake venom metalloproteinase.";
RL Amino Acids 48:1331-1335(2016).
CC -!- FUNCTION: The metalloproteinase-disintegrin-like HF3 is a potent
CC hemorrhagic toxin that activates macrophages for phagocytosis through
CC integrin alpha-M/beta-2 (ITGAM/ITGB2). It inhibits collagen-induced
CC platelet aggregation. This protein shows cleavage specificity for
CC substrate for leucine at P1' position, followed by hydrophobic residues
CC in P2' (PubMed:27020778). {ECO:0000269|PubMed:15336556,
CC ECO:0000269|PubMed:27020778, ECO:0000269|PubMed:3136558}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:3136558}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15336556}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:15336556}.
CC -!- DEVELOPMENTAL STAGE: This protein seems to be found in both adult and
CC newborn B.jararaca venoms. {ECO:0000269|PubMed:20146532}.
CC -!- MISCELLANEOUS: The disintegrin domain belongs to the long disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
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DR EMBL; AF149788; AAG48931.5; -; mRNA.
DR AlphaFoldDB; Q98UF9; -.
DR SMR; Q98UF9; -.
DR MEROPS; M12.320; -.
DR BRENDA; 3.4.24.49; 911.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemorrhagic toxin; Hemostasis impairing toxin; Hydrolase; Metal-binding;
KW Metalloprotease; Platelet aggregation inhibiting toxin; Protease; Secreted;
KW Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..190
FT /evidence="ECO:0000250"
FT /id="PRO_0000326421"
FT CHAIN 191..606
FT /note="Zinc metalloproteinase-disintegrin-like HF3"
FT /evidence="ECO:0000305|PubMed:15336556"
FT /id="PRO_0000326422"
FT DOMAIN 199..395
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 403..489
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 467..469
FT /note="D/ECD-tripeptide"
FT ACT_SITE 336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 390
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 405
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 418
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT BINDING 484
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 310..390
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 350..374
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 352..357
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 406..435
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 417..430
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 419..425
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 429..452
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 443..449
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 448..474
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 461..481
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 468..500
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 493..505
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 512..562
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 527..569
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 540..550
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 557..594
FT /evidence="ECO:0000250|UniProtKB:O93523"
FT DISULFID 588..599
FT /evidence="ECO:0000250|UniProtKB:O93523"
SQ SEQUENCE 606 AA; 67695 MW; 59C6EB6F3E4037C3 CRC64;
MIQVLLVTIC LAAFPYQGSS IILESGNVND YEVVYARKVT ALPKGAVQPK YEDTMQYELK
VNGEPVVLHL EKNKQLFSKD YSETHYSPDG REITTYPPVE DHCYYHGRIE NDADSTASIS
ACNGLKGHFK LQGETYFIEP LKLPNSEAHA VFKYENVEKE DEVPKMCGVT QTNWESDEPI
KKASQLVVTA EQQRYNHYKY IELVILADYR MVTKNNGDLG KIRTKIYEIV NILNEIFRYL
YIRIALVGIE IWSNADLSNV TLSADDTLAS FGTWRGTVLL KRKSHDNAQL LTAIDFDGQT
IGIANIASMC NQNKSVGVVM DYSPINLVVA VIMAHEMGHN LGINHDTGSC SCGGYSCIMA
PEISDQPSKL FSNCSKQAYQ RYINYYKPQC ILNEPLRTDI VSPPVCGNEL LEMGEECDCG
SPRNCRDPCC DAATCKLHSW VECESGECCD QCRFKGAGTE CRAARSECDI AESCTGQSAD
CPTDDFKRNG QPCLHNYGYC YNGNCPIMYH QCYALFGSNA TVAEDGCFEF NENGDKYFYC
RKQSGVNIPC AQEDVKCGRL FCHTKKHPCD YKYSEDPDYG MVDNGTKCAD GKVCSNGHCV
DVATAY
