VM2AL_TRIAB
ID VM2AL_TRIAB Reviewed; 484 AA.
AC P0C6B6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Zinc metalloproteinase homolog-disintegrin albolatin;
DE Flags: Precursor;
OS Trimeresurus albolabris (White-lipped pit viper) (Cryptelytrops
OS albolabris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Trimeresurus.
OX NCBI_TaxID=8765;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND SUBUNIT.
RC TISSUE=Venom gland;
RX PubMed=17870140; DOI=10.1016/j.toxicon.2007.08.002;
RA Singhamatr P., Rojnuckarin P.;
RT "Molecular cloning of albolatin, a novel snake venom metalloprotease from
RT green pit viper (Trimeresurus albolabris), and expression of its
RT disintegrin domain.";
RL Toxicon 50:1192-1200(2007).
CC -!- FUNCTION: The function of this complete protein has not been studied,
CC but it may be similar to the function of the disintegrin domain. A
CC recombinant protein of this domain (409-484) inhibits collagen-induced
CC human platelet aggregation, without having effect on ADP-induced
CC aggregation. It may act either by blocking the binding of fibrinogen to
CC the platelet receptor GPIIb/GPIIIa (ITGA2B/ITGB3) or by blocking the
CC binding of collagen to the integrin alpha-2/beta-1 complex
CC (ITGA2/ITGB1). {ECO:0000269|PubMed:17870140}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (disintegrin).
CC {ECO:0000269|PubMed:17870140}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:17870140}.
CC -!- MISCELLANEOUS: The disintegrin belongs to the dimeric disintegrin
CC subfamily.
CC -!- SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II
CC subfamily. P-IIb sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: The metalloproteinase domain lacks the active site.
CC {ECO:0000305}.
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DR AlphaFoldDB; P0C6B6; -.
DR SMR; P0C6B6; -.
DR MEROPS; M12.313; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:InterPro.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
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; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
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.
PE 1: Evidence at protein level;
KW Cell adhesion impairing toxin; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Platelet aggregation inhibiting toxin;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..191
FT /evidence="ECO:0000250"
FT /id="PRO_0000319491"
FT CHAIN 192..484
FT /note="Zinc metalloproteinase homolog-disintegrin
FT albolatin"
FT /id="PRO_0000319492"
FT DOMAIN 194..392
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 400..484
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT MOTIF 462..464
FT /note="Cell attachment site; atypical (KGD)"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 305..387
FT /evidence="ECO:0000250"
FT DISULFID 345..369
FT /evidence="ECO:0000250"
FT DISULFID 347..352
FT /evidence="ECO:0000250"
FT DISULFID 403..422
FT /evidence="ECO:0000255"
FT DISULFID 414..432
FT /evidence="ECO:0000250"
FT DISULFID 416..427
FT /evidence="ECO:0000250"
FT DISULFID 426..449
FT /evidence="ECO:0000250"
FT DISULFID 440..446
FT /evidence="ECO:0000250"
FT DISULFID 445..470
FT /evidence="ECO:0000250"
FT DISULFID 458..477
FT /evidence="ECO:0000250"
SQ SEQUENCE 484 AA; 54264 MW; DFB19FBAD9E06382 CRC64;
MIQVLLVTIC LAVFPYQGSS IILESGNVND YEVVYPEKVT ALPKGAVQQK YEDAMQYEFK
VNGEPVVLYL EKNKELFSEN YSETHYSLDG REITTYPSVE DHCYYHGRIQ NDADSTASIS
ACNGLKGHFK LRGKTYLIEP LKLPNSEAHA VFKYENVEKE DEAPQMCGVT ETNWESDLPI
KKTSQLNLPL LEKRCIELVM VADHRMYTKY DGDKTEISSK IYEIANNLNV DYRPMKIRVA
LIGTEIWSTG NLSKVTLSAD ETLDSFGEWR ERDLLKRKSH DNVQLLTGMI FNEKIEGRAY
NKSMCDPKRS VGIVRDHRTR PHLVANRMAH GLGHNLGIHH DGDSCSCGAN SCIMSATVSN
EPSSRFSDCS LNQYSNDIIY NPWTSYCLYN EPSKTDIVSP PVCGNYYLEV GEDCDCGPPA
NCQNPCCDAT TCKLTPGSQC AEGLCCAQCK FIEEGTVCRV AKGDWNDDHC TGQSGDCPWI
GYYG
