VM3H_NAJAT
ID VM3H_NAJAT Reviewed; 613 AA.
AC D3TTC2; D4AEP5;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like atragin;
DE EC=3.4.24.-;
DE AltName: Full=Snake venom metalloproteinase;
DE Short=SVMP;
DE Flags: Precursor;
OS Naja atra (Chinese cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8656;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 192-201, FUNCTION, SUBUNIT
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 192-613 IN COMPLEX WITH ZINC ION
RP AND CALCIUM IONS, GLYCOSYLATION AT ASN-436, AND DISULFIDE BONDS.
RC TISSUE=Venom, and Venom gland;
RX PubMed=19932752; DOI=10.1016/j.jsb.2009.11.009;
RA Guan H.-H., Goh K.S., Davamani F., Wu P.-L., Huang Y.W., Jeyakanthan J.,
RA Wu W.-G., Chen C.-J.;
RT "Structures of two elapid snake venom metalloproteases with distinct
RT activities highlight the disulfide patterns in the D domain of ADAMalysin
RT family proteins.";
RL J. Struct. Biol. 169:294-303(2010).
CC -!- FUNCTION: Snake venom zinc metalloproteinase that seems to inhibit cell
CC migration. This activity is dominated by the local structure of the
CC hyper-variable region. {ECO:0000269|PubMed:19932752}.
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:19932752}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- MISCELLANEOUS: Does not show autolytic activity, as encountered in
CC viperid venoms. Does not show activity on TNF-alpha (TNF)
CC (PubMed:19932752). {ECO:0000305|PubMed:19932752}.
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; FJ177517; ACN50006.1; -; mRNA.
DR PDB; 3K7L; X-ray; 2.50 A; A=192-613.
DR PDBsum; 3K7L; -.
DR AlphaFoldDB; D3TTC2; -.
DR SMR; D3TTC2; -.
DR MEROPS; M12.159; -.
DR iPTMnet; D3TTC2; -.
DR PRIDE; D3TTC2; -.
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; 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; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Secreted; Signal; Toxin; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..191
FT /evidence="ECO:0000255"
FT /id="PRO_5000578133"
FT CHAIN 192..613
FT /note="Zinc metalloproteinase-disintegrin-like atragin"
FT /id="PRO_5000578134"
FT DOMAIN 205..400
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 408..494
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT REGION 560..574
FT /note="Hypervariable region that may play important roles
FT toward cell migration"
FT MOTIF 472..474
FT /note="D/ECD-tripeptide"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 410
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 413
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 417
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 477
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 489
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 490
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 316..395
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 356..379
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 411..440
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 422..435
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 424..430
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 434..457
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 448..454
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 453..479
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 466..486
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 473..505
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 498..510
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 517..567
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 532..575
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 542..577
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 545..555
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 562..601
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 595..606
FT /evidence="ECO:0000269|PubMed:19932752"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:3K7L"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:3K7L"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:3K7L"
FT HELIX 225..243
FT /evidence="ECO:0007829|PDB:3K7L"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 248..257
FT /evidence="ECO:0007829|PDB:3K7L"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:3K7L"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:3K7L"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:3K7L"
FT HELIX 332..346
FT /evidence="ECO:0007829|PDB:3K7L"
FT HELIX 378..391
FT /evidence="ECO:0007829|PDB:3K7L"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:3K7L"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:3K7L"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:3K7L"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:3K7L"
FT TURN 499..502
FT /evidence="ECO:0007829|PDB:3K7L"
FT HELIX 513..521
FT /evidence="ECO:0007829|PDB:3K7L"
FT HELIX 530..537
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:3K7L"
FT HELIX 557..562
FT /evidence="ECO:0007829|PDB:3K7L"
FT TURN 584..587
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 599..602
FT /evidence="ECO:0007829|PDB:3K7L"
FT STRAND 605..608
FT /evidence="ECO:0007829|PDB:3K7L"
FT HELIX 609..612
FT /evidence="ECO:0007829|PDB:3K7L"
SQ SEQUENCE 613 AA; 69180 MW; 5C53CC09B60AD816 CRC64;
MIQALLVIIC LAVFPHQGSS IILESGNVND YEVVYPQKVP ALLKGGVQNP QPETKYEDTM
RYEFQVNGEP VVLHLERNKG LFSEDYTETH YAPDGREITT SPPVQDHCYY HGYIQNEADS
SAVISACDGL KGHFEHQGET YFIEPLKISN SEAHAIYKDE NVENEDETPE ICGVTETTWE
SDESIEKTSQ LTNTPEQDRY LQAKKYIEFY VVVDNIMYRH YKRDQPVIKR KVYEMINTMN
MIYRRLNFHI ALIGLEIWSN INEINVQSDV RATLNLFGEW REKKLLPRKR NDNAQLLTGI
DFNGTPVGLA YIGSICNPKT SAAVVQDYSS RTRMVAITMA HEMGHNLGMN HDRGFCTCGF
NKCVMSTRRT KPAYQFSSCS VREHQRYLLR DRPQCILNKP LSTDIVSPPI CGNYFVEVGE
ECDCGSPADC QSACCNATTC KLQHEAQCDS EECCEKCKFK GARAECRAAK DDCDLPELCT
GQSAECPTDV FQRNGLPCQN NQGYCYNGKC PIMTNQCIAL RGPGVKVSRD SCFTLNQRTR
GCGLCRMEYG RKIPCAAKDV KCGRLFCKRR NSMICNCSIS PRDPNYGMVE PGTKCGDGMV
CSNRQCVDVK TAY
