BGBP1_GALME
ID BGBP1_GALME Reviewed; 490 AA.
AC Q0E666; C0HLY9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Beta-1,3-glucan-binding protein 1 {ECO:0000305};
DE Short=BGBP1 {ECO:0000305};
DE AltName: Full=Beta-1,3-glucan recognition protein {ECO:0000303|PubMed:34443685};
DE Flags: Precursor;
GN Name=bgrp1 {ECO:0000312|EMBL:CAK22401.1};
OS Galleria mellonella (Greater wax moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea;
OC Pyralidae; Galleriinae; Galleria.
OX NCBI_TaxID=7137 {ECO:0000312|EMBL:CAK22401.1};
RN [1] {ECO:0000312|EMBL:CAK22401.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Niere M., Weise C., Wernig-Pohl U., Goetz P.;
RT "Identification of a beta-1,3-glucan recognition protein from the hemolymph
RT of Galleria mellonella larvae.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 20-39, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=34443685; DOI=10.3390/molecules26165097;
RA Staczek S., Zdybicka-Barabas A., Wojda I., Wiater A., Mak P., Suder P.,
RA Skrzypiec K., Cytrynska M.;
RT "Fungal alpha-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in
RT the Insect Model Host Galleria mellonella.";
RL Molecules 26:5097-5097(2021).
CC -!- FUNCTION: Plays a role in the recognition of invading microorganisms
CC activating the phenoloxidase cascade (By similarity). Binds
CC specifically to beta-1,3-glucan (By similarity). Binds the Aspergillus
CC niger cell wall component alpha-1,3-glucan, a fungal pathogen-
CC associated molecular pattern (PAMP) that activates the host immune
CC response (PubMed:34443685). {ECO:0000250|UniProtKB:Q9NL89,
CC ECO:0000269|PubMed:34443685}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9NL89}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34443685}.
CC Note=Secreted in the hemolymph. {ECO:0000269|PubMed:34443685}.
CC -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000269|PubMed:34443685}.
CC -!- SIMILARITY: Belongs to the insect beta-1,3-glucan binding protein
CC family. {ECO:0000305}.
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DR EMBL; AM265582; CAK22401.1; -; mRNA.
DR CAZy; CBM39; Carbohydrate-Binding Module Family 39.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR Proteomes; UP000504614; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR CDD; cd02179; GH16_beta_GRP; 1.
DR Gene3D; 2.60.40.2140; -; 1.
DR InterPro; IPR031756; BGBP_N.
DR InterPro; IPR043030; BGBP_N_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR035806; GH16_GRP_C.
DR Pfam; PF15886; CBM39; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51969; CBM39; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Immunity; Innate immunity;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..490
FT /note="Beta-1,3-glucan-binding protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5004171107"
FT DOMAIN 20..119
FT /note="CBM39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01314"
FT DOMAIN 152..490
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 490 AA; 55395 MW; 46D3A6133E56B6B3 CRC64;
MYKQTVVIFL LCFFICVSCY EVPPAKLEAI WPKGLRVSLP DDGYSLFAFH GKLNEEMEGL
EAGHWSRDIT KSKGGRWTFN DKQAKLKIGD KIYFWTYVIK EGLGYRQDNG EWTVTGYVDE
AGNPVAPTSQ PDAVVTEPPA AITPATAIVT NPPTSQNTYP CEISVSMVSV PGFVCKGQLL
FEDNFNKGID KGNIWTTENM FPGEPDYPFN VYLYDNVHVR DGKLIITPTT LESKYGEDYV
RQQLDLTQRC TGTIGTADCT RVASGPIILP PVITSKINTK NRFSFKYGRV EVRARMPTGD
WLIPEILLEP RDRIYGIHSY ASGLLRVACV KGNVEYSKTL YGGPILCDSE PYRNVNLKQK
IGFDHWNKDF HNYTLEWRPD GISLFVDGEK YGDVTPPTDG FYGDAKKENV QAASQWLKGT
SMAPLDDYFY ISIGLDVGGV HEFPDSSTKP WQNKATKAML NFWNNRDQWF PTWFKDTSSL
QVDYVRVYAL