SLA_ECHML
ID SLA_ECHML Reviewed; 157 AA.
AC Q7T2Q1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Snaclec EMS16 subunit alpha;
DE Short=EMS16A;
DE Flags: Precursor;
OS Echis multisquamatus (Central Asian sand viper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Echis.
OX NCBI_TaxID=93050;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-44.
RX PubMed=12944366; DOI=10.1093/jb/mvg108;
RA Okuda D., Horii K., Mizuno H., Morita T.;
RT "Characterization and preliminary crystallographic studies of EMS16, an
RT antagonist of collagen receptor (GPIa/IIa) from the venom of Echis
RT multisquamatus.";
RL J. Biochem. 134:19-23(2003).
RN [2]
RP PROTEIN SEQUENCE OF 24-82.
RX PubMed=10933804; DOI=10.1021/bi000428a;
RA Marcinkiewicz C., Lobb R.R., Marcinkiewicz M.M., Daniel J.L., Smith J.B.,
RA Dangelmaier C., Weinreb P.H., Beacham D.A., Niewiarowski S.;
RT "Isolation and characterization of EMS16, a C-lectin type protein from
RT Echis multisquamatus venom, a potent and selective inhibitor of the
RT alpha2beta1 integrin.";
RL Biochemistry 39:9859-9867(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-157 IN COMPLEX WITH EMS16B, AND
RP DISULFIDE BONDS.
RX PubMed=14580195; DOI=10.1021/bi034890h;
RA Horii K., Okuda D., Morita T., Mizuno H.;
RT "Structural characterization of EMS16, an antagonist of collagen receptor
RT (GPIa/IIa) from the venom of Echis multisquamatus.";
RL Biochemistry 42:12497-12502(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-157 IN COMPLEX WITH EMS16B AND
RP ITGA2, AND SITES.
RX PubMed=15276841; DOI=10.1016/j.jmb.2004.06.036;
RA Horii K., Okuda D., Morita T., Mizuno H.;
RT "Crystal structure of EMS16 in complex with the integrin alpha2-I domain.";
RL J. Mol. Biol. 341:519-527(2004).
CC -!- FUNCTION: EMS16 is a potent and selective inhibitor of alpha-2/beta-1
CC (ITGA2/ITGB1) integrin and acts as a potent antagonist of platelet
CC aggregation and cell migration. Binds specifically to the I domain of
CC the alpha-2 subunit, in a metal ion-independent fashion.
CC -!- SUBUNIT: Heterodimer of subunits A and B; disulfide-linked.
CC {ECO:0000269|PubMed:14580195, ECO:0000269|PubMed:15276841}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- SIMILARITY: Belongs to the snaclec family. {ECO:0000305}.
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DR EMBL; AB098253; BAC77706.1; -; mRNA.
DR PDB; 1UKM; X-ray; 1.90 A; A=24-157.
DR PDB; 1V7P; X-ray; 1.90 A; A=24-157.
DR PDBsum; 1UKM; -.
DR PDBsum; 1V7P; -.
DR AlphaFoldDB; Q7T2Q1; -.
DR SMR; Q7T2Q1; -.
DR IntAct; Q7T2Q1; 1.
DR EvolutionaryTrace; Q7T2Q1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Hemostasis impairing toxin; Platelet aggregation inhibiting toxin;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:10933804,
FT ECO:0000269|PubMed:12944366"
FT CHAIN 24..157
FT /note="Snaclec EMS16 subunit alpha"
FT /id="PRO_0000318802"
FT DOMAIN 34..153
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT SITE 84
FT /note="Key residue for binding with integrin"
FT SITE 90
FT /note="Key residue for binding with integrin"
FT SITE 133
FT /note="Key residue for binding with integrin"
FT DISULFID 27..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:14580195"
FT DISULFID 55..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:14580195"
FT DISULFID 104
FT /note="Interchain (with C-100 in subunit B)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:14580195"
FT DISULFID 127..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:14580195"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1UKM"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:1UKM"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:1UKM"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:1UKM"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:1UKM"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1UKM"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1UKM"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1UKM"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1UKM"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1UKM"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:1UKM"
SQ SEQUENCE 157 AA; 18214 MW; F0D9638C6D622AB3 CRC64;
MGRFISVSFG LLVVFLSLSG TGADFDCPSD WTAYDQHCYL AIGEPQNWYE AERFCTEQAK
DGHLVSIQSR EEGNFVAQLV SGFMHRSEIY VWIGLRDRRE EQQCNPEWND GSKIIYVNWK
EGESKMCQGL TKWTNFHDWN NINCEDLYPF VCKFSAV
