VM3HB_PROFL
ID VM3HB_PROFL Reviewed; 614 AA.
AC P20164; Q8JIR1;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 4.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like HR1b {ECO:0000303|PubMed:2398046};
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE AltName: Full=Trimerelysin I;
DE AltName: Full=Trimerelysin-1;
DE Contains:
DE RecName: Full=Disintegrin-like 1b;
DE Flags: Precursor;
OS Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=88087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Amami habu; TISSUE=Venom gland;
RX PubMed=12220724; DOI=10.1016/s0041-0101(02)00179-4;
RA Kishimoto M., Takahashi T.;
RT "Molecular cloning of HR1a and HR1b, high molecular hemorrhagic factors,
RT from Trimeresurus flavoviridis venom.";
RL Toxicon 40:1369-1375(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 281-292; 376-386; 397-404
RP AND 504-515, CATALYTIC ACTIVITY, AND VARIANTS OKINAWA HABU VAL-34 AND
RP CYS-313.
RC STRAIN=Okinawa habu; TISSUE=Venom;
RX PubMed=18256489; DOI=10.1271/bbb.70540;
RA Morine N., Matsuda S., Terada K., Iwasaki H., Oku H.;
RT "The occurrence of HR1b in the venom of the snake Okinawa habu
RT (Protobothrops flavoviridis).";
RL Biosci. Biotechnol. Biochem. 72:591-594(2008).
RN [3]
RP PROTEIN SEQUENCE OF 192-607, AND PYROGLUTAMATE FORMATION AT GLN-192.
RC STRAIN=Amami habu; TISSUE=Venom;
RX PubMed=2398046; DOI=10.1016/s0021-9258(17)46189-8;
RA Takeya H., Oda K., Miyata T., Omori-Satoh T., Iwanaga S.;
RT "The complete amino acid sequence of the high molecular mass hemorrhagic
RT protein HR1B isolated from the venom of Trimeresurus flavoviridis.";
RL J. Biol. Chem. 265:16068-16073(1990).
RN [4]
RP PROTEIN SEQUENCE OF 399-409.
RC TISSUE=Venom;
RX PubMed=8514736; DOI=10.1093/oxfordjournals.jbchem.a124069;
RA Takeya H., Nishida S., Nishino N., Makinose Y., Omori-Satoh T., Nikai T.,
RA Sugihara H., Iwanaga S.;
RT "Primary structures of platelet aggregation inhibitors (disintegrins)
RT autoproteolytically released from snake venom hemorrhagic
RT metalloproteinases and new fluorogenic peptide substrates for these
RT enzymes.";
RL J. Biochem. 113:473-483(1993).
CC -!- FUNCTION: [Zinc metalloproteinase-disintegrin-like HR1b]: Zinc protease
CC that induces hemorrhage. Has preference for Tyr, Leu, Arg, Met, and Phe
CC at the P1 position, in descending order (in vitro). Shows equal
CC preference for the sequences of Ala-Asp and Arg-Ile at the P3-P2
CC position with different enzyme cleavage sites across the P1 position:
CC the N-terminus side for Ala-Asp and the C-terminus side for Arg-Ile.
CC {ECO:0000269|PubMed:18256489}.
CC -!- FUNCTION: [Disintegrin-like 1b]: Inhibits platelet aggregation induced
CC by ADP, thrombin, platelet-activating factor and collagen. Acts by
CC inhibiting fibrinogen interaction with platelet receptors alpha-
CC IIb/beta-3 (ITGA2B/ITGB3). {ECO:0000250}.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIb sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: Lys-201 is present instead of the conserved Glu which binds a
CC calcium ion. {ECO:0000305}.
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DR EMBL; AB074144; BAB92014.1; -; mRNA.
DR PIR; A37877; A37877.
DR AlphaFoldDB; P20164; -.
DR SMR; P20164; -.
DR MEROPS; M12.154; -.
DR PRIDE; P20164; -.
DR KEGG; ag:BAB92014; -.
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; Cell adhesion impairing toxin; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemorrhagic toxin;
KW Hemostasis impairing toxin; Hydrolase; Metal-binding; Metalloprotease;
KW Platelet aggregation inhibiting toxin; Protease;
KW Pyrrolidone carboxylic acid; Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..191
FT /evidence="ECO:0000269|PubMed:2398046"
FT /id="PRO_0000029022"
FT CHAIN 192..607
FT /note="Zinc metalloproteinase-disintegrin-like HR1b"
FT /evidence="ECO:0000269|PubMed:2398046"
FT /id="PRO_0000029023"
FT PROPEP 395..398
FT /evidence="ECO:0000269|PubMed:8514736"
FT /id="PRO_0000029024"
FT CHAIN 399..490
FT /note="Disintegrin-like 1b"
FT /id="PRO_0000029025"
FT PROPEP 608..614
FT /id="PRO_0000029026"
FT DOMAIN 198..394
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 402..488
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 466..468
FT /note="D/ECD-tripeptide"
FT ACT_SITE 335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 192
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2398046"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 309..389
FT /note="In zinc metalloproteinase-disintegrin-like HR1b"
FT /evidence="ECO:0000250"
FT DISULFID 349..373
FT /note="In zinc metalloproteinase-disintegrin-like HR1b"
FT /evidence="ECO:0000250"
FT DISULFID 351..356
FT /note="In zinc metalloproteinase-disintegrin-like HR1b"
FT /evidence="ECO:0000250"
FT DISULFID 405..434
FT /note="In zinc metalloproteinase-disintegrin-like HR1b;
FT alternate"
FT /evidence="ECO:0000250"
FT DISULFID 405..424
FT /note="In disintegrin-like 1b; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 416..434
FT /note="In disintegrin-like 1b; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 416..429
FT /note="In zinc metalloproteinase-disintegrin-like HR1b;
FT alternate"
FT /evidence="ECO:0000250"
FT DISULFID 418..424
FT /note="In zinc metalloproteinase-disintegrin-like HR1b;
FT alternate"
FT /evidence="ECO:0000250"
FT DISULFID 428..451
FT /note="In zinc metalloproteinase-disintegrin-like HR1b"
FT /evidence="ECO:0000250"
FT DISULFID 442..448
FT /note="In zinc metalloproteinase-disintegrin-like HR1b"
FT /evidence="ECO:0000250"
FT DISULFID 447..473
FT /note="In zinc metalloproteinase-disintegrin-like HR1b"
FT /evidence="ECO:0000250"
FT DISULFID 460..480
FT /note="In both disintegrin-like 1b and zinc
FT metalloproteinase-disintegrin-like HR1b"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068,
FT ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 467..499
FT /note="In zinc metalloproteinase-disintegrin-like HR1b;
FT alternate"
FT /evidence="ECO:0000250"
FT DISULFID 467..492
FT /note="In disintegrin-like 1b; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 492..504
FT /note="In zinc metalloproteinase-disintegrin-like HR1b;
FT alternate"
FT /evidence="ECO:0000250"
FT DISULFID 499..504
FT /note="In disintegrin-like 1b"
FT /evidence="ECO:0000250"
FT DISULFID 511..561
FT /note="In zinc metalloproteinase-disintegrin-like HR1b;
FT alternate"
FT /evidence="ECO:0000250"
FT DISULFID 511..526
FT /note="In disintegrin-like 1b; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 526..568
FT /note="In zinc metalloproteinase-disintegrin-like HR1b;
FT alternate"
FT /evidence="ECO:0000250"
FT DISULFID 539..549
FT /note="In zinc metalloproteinase-disintegrin-like HR1b;
FT alternate"
FT /evidence="ECO:0000250"
FT DISULFID 549..556
FT /note="In disintegrin-like 1b; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 556..593
FT /note="In zinc metalloproteinase-disintegrin-like HR1b;
FT alternate"
FT /evidence="ECO:0000250"
FT DISULFID 561..568
FT /note="In disintegrin-like 1b"
FT /evidence="ECO:0000250"
FT DISULFID 587..598
FT /note="In zinc metalloproteinase-disintegrin-like HR1b;
FT alternate"
FT /evidence="ECO:0000250"
FT DISULFID 593..598
FT /note="In disintegrin-like 1b"
FT /evidence="ECO:0000250"
FT VARIANT 34
FT /note="M -> V (in Okinawa habu)"
FT /evidence="ECO:0000269|PubMed:18256489"
FT VARIANT 313
FT /note="R -> C (in Okinawa habu)"
FT /evidence="ECO:0000269|PubMed:18256489"
SQ SEQUENCE 614 AA; 69129 MW; DE31F89CEE929705 CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVND YEVMYPQKVA ALPKGAVQQK YEDTMQYEFK
VNGEPVVLHL EKNKGLFSED YSETHYSPDG REITTNPPVE DHCYYHGRIQ NDADSTASIS
ACNGLKGHFK LQGEMYLIEP LKFSDSEAHA VYKYENVEKE EEAPKMCGVT QTNWESDEPI
KKASKLVVTA EQQRFPRRYI KLAIVVDHGI VTKHHGNLKK IRKWIYQLVN TINNIYRSLN
ILVALVYLEI WSKQNKITVQ SASNVTLDLF GDWRESVLLK QRSHDCAQLL TTIDFDGPTI
GKAYTASMCD PKRSVGIVQD YSPINLVVAV IMTHEMGHNL GIPHDGNSCT CGGFPCIMSP
MISDPPSELF SNCSKAYYQT FLTDHKPQCI LNAPSKTDIV SPPVCGNELL EAGEECDCGS
PENCQYQCCD AASCKLHSWV KCESGECCDQ CRFRTAGTEC RAAESECDIP ESCTGQSADC
PTDRFHRNGQ PCLYNHGYCY NGKCPIMFYQ CYFLFGSNAT VAEDDCFNNN KKGDKYFYCR
KENEKYIPCA QEDVKCGRLF CDNKKYPCHY NYSEDLDFGM VDHGTKCADG KVCSNRQCVD
VNEAYKSTTV FSLI
