BGBP_PENVA
ID BGBP_PENVA Reviewed; 1454 AA.
AC P81182; Q86G48;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Beta-1,3-glucan-binding protein;
DE Short=BGBP;
DE AltName: Full=Beta-1,3-glucan recognition protein;
DE Short=BetaGRP;
DE AltName: Full=BetaGBP-HDL;
DE AltName: Full=High density lipoprotein;
DE Flags: Precursor;
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 329-335; 761-772 AND
RP 827-840.
RC TISSUE=Hepatopancreas;
RX PubMed=15043941; DOI=10.1016/j.dci.2003.11.008;
RA Romo-Figueroa M.G., Vargas-Requena C., Sotelo-Mundo R.R.,
RA Vargas-Albores F., Higuera-Ciapara I., Soderhall K., Yepiz-Plascencia G.M.;
RT "Molecular cloning of a beta-glucan pattern-recognition lipoprotein from
RT the white shrimp Penaeus (Litopenaeus) vannamei: correlations between the
RT deduced amino acid sequence and the native protein structure.";
RL Dev. Comp. Immunol. 28:713-726(2004).
RN [2]
RP PROTEIN SEQUENCE OF 198-222, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=9149399; DOI=10.1016/s0305-0491(96)00268-4;
RA Vargas-Albores F., Jimenez-Vega F., Yepiz-Plascencia G.M.;
RT "Purification and comparison of beta-1,3-glucan binding protein from white
RT shrimp (Penaeus vannamei).";
RL Comp. Biochem. Physiol. 116B:453-458(1997).
CC -!- FUNCTION: Involved in the recognition of invading microorganisms. Binds
CC specifically to beta-1,3-glucan and activates the prophenoloxidase
CC cascade. {ECO:0000269|PubMed:9149399}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9149399}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9149399}.
CC -!- TISSUE SPECIFICITY: Expressed in the hepatopancreas and secreted into
CC the hemolymph. Expressed at lower levels in muscle, pleopod and gill
CC tissue. {ECO:0000269|PubMed:9149399}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR EMBL; AY249858; AAO92933.1; -; mRNA.
DR AlphaFoldDB; P81182; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0038187; F:pattern recognition receptor activity; IDA:UniProtKB.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0045088; P:regulation of innate immune response; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Immunity; Innate immunity;
KW Lipid transport; Secreted; Transport.
FT PROPEP 1..197
FT /evidence="ECO:0000269|PubMed:9149399"
FT /id="PRO_0000002825"
FT CHAIN 198..1454
FT /note="Beta-1,3-glucan-binding protein"
FT /id="PRO_0000002826"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 825
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 220..221
FT /note="ER -> VW (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="D -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1454 AA; 164013 MW; 03076021A5D6465F CRC64;
MSFDLTTPFD VIKTVSLSAR YSWTTSQKGA TLNITYNDKN FVLSSSLQLS TRASNITFQA
TTPFEGFQNS FIEIKYDIDN REELLASRVS VDDHSYSFVV GGYIEDKLAV FKWNLNSPLT
GWTDAKFVAK IDLSSENKNL EISLEKEGDL KAIAVSGKFI GSTLDFNLRT PFRGLNNFNV
FGSLNRSKRS LEMRMMNDAG QASLAGNFNS LRFNMKTPFE RAEQISWEVT KTGEGSYKAE
WRRNDNYATF TIEKDVSKQS FDLNIKSEFR GWEILALTGR LDQETKQAYL SGAINEQKIT
VTGSGSITNK IKFSMTIETP YENYRQVKAQ LNYAKRKNAI KLEASSSSSD FHLLWSRSGS
GLEAHLIVPN SRQNTEISIN LTPTQGKITI TSRFEPIRDY LQEYHVNLGQ NEITADHIIK
LNGHEVFKMD FERNAPEQKV HLEIHTHVAE RHTTIHFHRE GFSKLNFLFK REVPQYGEKH
FKVDITGSGA LPQKGALDIV VENTFREPAK TINARVEVDR TGARKKIMLE VSPRQSRVYI
FNLEYIADLE SPQHGDFTLK ITTPNNSPWQ NISGNWNVED PNDATITFTV GNVTYNAKGK
LTLRESTMIL SSTDPSAENI YLQWKFERNG DTKDYFLKLG RKSRYGMLKL TGTITDIAHV
DIEGGFKAGP FMPNEFLFTS MWGKSNGVVT GEGTFDYGNY HGSHRLVKFE RNAERKSASF
EWSATSNIPQ YNSVSVSGNY DFNHKVVIFV VINADGRESK IDINIADINP TSSRNTAMIS
IPLLGPTFKR TELTVSHDFS HPNRKSISAV AKFGRSESFI NAKWNRSDGF DTLEGNIEAK
SRFLGDFLIN VRYDMSNIAD AHAEVDYLRT TTDGDKKEFK LNWTRKSTDD HLENEMVFDS
NFETLSHARA YANADYGGIF KLLSGLDWDD KKISLTLEVR KNKISGILTT PFEGFETLEI
DLQYKLTGKD KSVKATYQRG DRKASFNMEM STKGKKGGSF KVDLTTPFEV VKNLHIDGQY
ENKVAQINYQ RNDIQMNFNG KANIKSSKAS FDISFTPPSG QNIRIAASYD VQDFIDGTGD
EEKELASLSL EFEGNSMDFS LHGFRNDDRL YVMIHGTSSF AVLKMFHLKL DSELNTEARD
GTFELTFNDF KFNVSNHFER RANNGYYFRS KIESTLTPLP ALIIGLGREG QERIITIGYG
EDKEITFSVK GKNNFLSGFS GKVDIPSIGY EGVEYDVDYS FPGDNHLQIK VEIDLNENGQ
EVEATFFLDS EGIKARLSSA VLGDHSLRVR RSVAPDGFYA EAGLDDYNLK LRGGFKNEDT
ARGVQLEGEV FGKRFLIDTL FQSEGKRYSE GKLIIHTPFH GMEKMGGLFT WSNQNKKIMA
HAELHLPSYT TPTITGEISL DLKKKINGYV TLDVAGEEFT LKCNLAGSSI SQGYTGSLEF
YTTIPCCITC CGDR
