VM3KL_NAJAT
ID VM3KL_NAJAT Reviewed; 593 AA.
AC D3TTC1; D4AEP6;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Zinc metalloproteinase-disintegrin-like kaouthiagin-like;
DE Short=K-like;
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], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT,
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 197-593 IN COMPLEX WITH ZINC ION
RP AND CALCIUM IONS, GLYCOSYLATION AT ASN-319 AND ASN-490, AND DISULFIDE
RP BONDS.
RC STRAIN=Taiwan; 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 cleaves the membrane-
CC bound precursor of TNF-alpha (TNF) into its mature soluble form showing
CC the same digestion pattern than ADAM17. {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 inhibit cell migration (PubMed:19932752).
CC {ECO:0000305|PubMed:19932752}.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III
CC subfamily. P-IIIa sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: The protein is 98% identical to atrase B (AC D6PXE8), a
CC metalloproteinase secreted by a Chinese cobra from the Hunan Province
CC of China. Surprisingly, mature proteins released from the two similar
CC precursors are not the same size. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FJ177516; ACN50005.1; -; mRNA.
DR PDB; 3K7N; X-ray; 2.30 A; A=197-593.
DR PDBsum; 3K7N; -.
DR AlphaFoldDB; D3TTC1; -.
DR SMR; D3TTC1; -.
DR MEROPS; M12.236; -.
DR iPTMnet; D3TTC1; -.
DR PRIDE; D3TTC1; -.
DR TopDownProteomics; D3TTC1; -.
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; -; 2.
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; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
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..196
FT /id="PRO_5000578131"
FT CHAIN 197..593
FT /note="Zinc metalloproteinase-disintegrin-like kaouthiagin-
FT like"
FT /id="PRO_5000578132"
FT DOMAIN 205..400
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 408..477
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 455..457
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 457
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 460
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19932752"
FT CARBOHYD 490
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 358..363
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..462
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 449..469
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 456..488
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 481..493
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 500..550
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 515..558
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 528..538
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 545..581
FT /evidence="ECO:0000269|PubMed:19932752"
FT DISULFID 575..586
FT /evidence="ECO:0000269|PubMed:19932752"
FT CONFLICT 231
FT /note="R -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="D -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:3K7N"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:3K7N"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:3K7N"
FT HELIX 225..243
FT /evidence="ECO:0007829|PDB:3K7N"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:3K7N"
FT STRAND 248..257
FT /evidence="ECO:0007829|PDB:3K7N"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:3K7N"
FT TURN 284..288
FT /evidence="ECO:0007829|PDB:3K7N"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:3K7N"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:3K7N"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:3K7N"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:3K7N"
FT HELIX 332..346
FT /evidence="ECO:0007829|PDB:3K7N"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:3K7N"
FT HELIX 378..391
FT /evidence="ECO:0007829|PDB:3K7N"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:3K7N"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:3K7N"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:3K7N"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:3K7N"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:3K7N"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:3K7N"
FT TURN 482..485
FT /evidence="ECO:0007829|PDB:3K7N"
FT HELIX 496..504
FT /evidence="ECO:0007829|PDB:3K7N"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:3K7N"
FT HELIX 513..520
FT /evidence="ECO:0007829|PDB:3K7N"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:3K7N"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:3K7N"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:3K7N"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:3K7N"
FT STRAND 579..582
FT /evidence="ECO:0007829|PDB:3K7N"
FT STRAND 585..588
FT /evidence="ECO:0007829|PDB:3K7N"
SQ SEQUENCE 593 AA; 66292 MW; 75FE5516845A3A0B CRC64;
MIQALLVIIC LAVFPHQGSS IILESGNVND YEVVYPQKVP ALLKGGVQNP QPETKYEDTM
RYEFQVNGEP VVLHLERNKG LFSEDYTETH YAPDGREITT SPPVQDHCYY HGYIQNEADS
SAVISACDGL KGHFEHQGET YFIEPLKISN SEAHAIYKDE NVENEDETPE ICGVTETTWE
SDESIEKTSQ FTNTPEQDRY LQDKKYIEFY VIVDNRMYRY YNNDKPAIKI RVYEMINAVN
TKFRPLKIHI ALIGLEIWSN KDKFEVKPAA SVTLKSFGEW RETVLLPRKR NDNAQLLTGI
DFNGNTVGRA YIGSLCKTNE SVAIVQDYNR RISLVASTIT HELGHNLGIH HDKASCICIP
GPCIMLKKRT APAFQFSSCS IREYREYLLR DRPQCILNKP LSTDIVSPPI CGNYFVEVGE
ECDCGSPQAC QSACCNAATC QFKGAETECR VAKDDCDLPE LCTGQSAECP TDSLQRNGHP
CQNNQSYCYN GTCPTLTNQC ITLLGPHFTV SPKGCFDLNM RGDDGSFCRM EDGTKIPCAA
KDVKCGRLYC TEKNTMSCLI PPNPDGIMAE PGTKCGDGMV CSKGQCVDVQ TAY
