TLLP_PHONI
ID TLLP_PHONI Reviewed; 225 AA.
AC P85031;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Techylectin-like protein;
DE Flags: Fragments;
OS Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Entelegynae; Lycosoidea; Ctenidae; Phoneutria.
OX NCBI_TaxID=6918;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Venom {ECO:0000269|Ref.1};
RA Richardson M., Resende F.F., Souza I.A., Goncalves J.M., Borges M.H.,
RA Cordeiro M.N.;
RT "Techylectin-like protein from venom of spider Phoneutria nigriventer has
RT sequence similarities to fibrinogen and ficolins.";
RL Submitted (OCT-2006) to UniProtKB.
CC -!- FUNCTION: Lectin involved in innate immunity.
CC {ECO:0000250|UniProtKB:Q9U8W8}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000269|Ref.1}.
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DR AlphaFoldDB; P85031; -.
DR SMR; P85031; -.
DR ArachnoServer; AS000012; Techylectin-1-Phoneutria nigriventer.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; -; 1.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; SSF56496; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Lectin; Metal-binding;
KW Secreted.
FT CHAIN 1..>225
FT /note="Techylectin-like protein"
FT /id="PRO_0000260047"
FT DOMAIN 32..225
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT MOTIF 75..77
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9U8W8"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q9U8W8"
FT SITE 176
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250|UniProtKB:Q9U8W8"
FT SITE 186
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250|UniProtKB:Q9U8W8"
FT SITE 198
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250|UniProtKB:Q9U8W8"
FT SITE 199
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250|UniProtKB:Q9U8W8"
FT SITE 210
FT /note="Implicated in ligand binding"
FT /evidence="ECO:0000250|UniProtKB:Q9U8W8"
FT DISULFID 41..60
FT /evidence="ECO:0000250|UniProtKB:Q9U8W8,
FT ECO:0000255|PROSITE-ProRule:PRU00739"
FT DISULFID 172..185
FT /evidence="ECO:0000250|UniProtKB:Q9U8W8,
FT ECO:0000255|PROSITE-ProRule:PRU00739"
FT NON_CONS 47..48
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 117..118
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 196..197
FT /evidence="ECO:0000303|Ref.1"
FT NON_TER 225
FT /evidence="ECO:0000303|Ref.1"
SQ SEQUENCE 225 AA; 25783 MW; F23E841D0E520434 CRC64;
LSTTCEGKDK GICNLNLALQ LITDVRDNFP VCPSPPLPID CEEVLQRDFK AIPNPIDVYC
DMVTDGGGWT VIQRRGDFHG PIDYFYKDWQ SYKKGFGDIE KEFWLGNENI FGLSNQRYAL
YDTFANDDED HKYMLHISGY KGDAGDSMIG VHNEQKFSTK DKNDNFPGAT SCAQLYKGGW
WYNQCHVSNL NGQYLKSYAD GVIWRSWKGY HESLGWTEIK IKDVK