HEMO_MANSE
ID HEMO_MANSE Reviewed; 413 AA.
AC P31398;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Hemolin;
DE AltName: Full=Hemocyte aggregation inhibitor;
DE AltName: Full=Protein P4;
DE Flags: Precursor;
OS Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Sphingidae; Sphinginae; Sphingini; Manduca.
OX NCBI_TaxID=7130;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fat body;
RX PubMed=1790333; DOI=10.1002/arch.940180410;
RA Ladendorff N.E., Kanost M.R.;
RT "Bacteria-induced protein P4 (hemolin) from Manduca sexta: a member of the
RT immunoglobulin superfamily which can inhibit hemocyte aggregation.";
RL Arch. Insect Biochem. Physiol. 18:285-300(1991).
RN [2]
RP SEQUENCE REVISION.
RA Kanost M.R.;
RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=12706633; DOI=10.1016/s0965-1748(03)00028-6;
RA Zhu Y., Johnson T.J., Myers A.A., Kanost M.R.;
RT "Identification by subtractive suppression hybridization of bacteria-
RT induced genes expressed in Manduca sexta fat body.";
RL Insect Biochem. Mol. Biol. 33:541-559(2003).
RN [4]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=14728663; DOI=10.1111/j.1365-2583.2004.00454.x;
RA Gorman M.J., Kankanala P., Kanost M.R.;
RT "Bacterial challenge stimulates innate immune responses in extra-embryonic
RT tissues of tobacco hornworm eggs.";
RL Insect Mol. Biol. 13:19-24(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16731347; DOI=10.1016/j.ibmb.2006.04.001;
RA Eleftherianos I., Marokhazi J., Millichap P.J., Hodgkinson A.J.,
RA Sriboonlert A., ffrench-Constant R.H., Reynolds S.E.;
RT "Prior infection of Manduca sexta with non-pathogenic Escherichia coli
RT elicits immunity to pathogenic Photorhabdus luminescens: roles of immune-
RT related proteins shown by RNA interference.";
RL Insect Biochem. Mol. Biol. 36:517-525(2006).
CC -!- FUNCTION: Insect-immune protein with antimicrobial activity
CC (PubMed:16731347). Forms a protein complex at the bacterial surface.
CC Can inhibit hemocyte aggregation. {ECO:0000269|PubMed:16731347}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16731347}.
CC -!- TISSUE SPECIFICITY: Hemolymph. {ECO:0000305|PubMed:16731347}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fat body of fifth instar larvae after
CC bacterial challenge (PubMed:12706633, PubMed:16731347). Expressed in
CC naive 2 h (precellular blastoderm stage) and 24 h (predorsal closure
CC stage) eggs (PubMed:14728663). {ECO:0000269|PubMed:12706633,
CC ECO:0000269|PubMed:14728663, ECO:0000269|PubMed:16731347}.
CC -!- INDUCTION: By bacterial infection. {ECO:0000269|PubMed:12706633,
CC ECO:0000269|PubMed:14728663, ECO:0000269|PubMed:16731347}.
CC -!- DISRUPTION PHENOTYPE: Silencing by small interfering RNA (siRNA) leads
CC to reduced protective effect conferred by non-pathogenic E.coli
CC infection prior the subsequent infection by lethal and highly virulent
CC pathogen Photorhabdus luminescens TT01. Speeds the rate at which
CC insects die after the pathogen infection.
CC {ECO:0000269|PubMed:16731347}.
CC -!- SIMILARITY: Belongs to the hemolin family. {ECO:0000305}.
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DR EMBL; M64346; AAA20148.1; -; mRNA.
DR AlphaFoldDB; P31398; -.
DR SMR; P31398; -.
DR PRIDE; P31398; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0006955; P:immune response; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain;
KW Innate immunity; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..413
FT /note="Hemolin"
FT /id="PRO_0000014773"
FT DOMAIN 25..112
FT /note="Ig-like C2-type 1"
FT DOMAIN 121..215
FT /note="Ig-like C2-type 2"
FT DOMAIN 233..322
FT /note="Ig-like C2-type 3"
FT DOMAIN 327..411
FT /note="Ig-like C2-type 4"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..97
FT /evidence="ECO:0000250|UniProtKB:P25033"
FT DISULFID 141..199
FT /evidence="ECO:0000250|UniProtKB:P25033"
FT DISULFID 252..305
FT /evidence="ECO:0000250|UniProtKB:P25033"
FT DISULFID 349..395
FT /evidence="ECO:0000250|UniProtKB:P25033"
SQ SEQUENCE 413 AA; 45699 MW; 255ED95AC992D9AF CRC64;
MVSKSIVALA ACVAMCVAQP VEKMPVLKDQ PAEVLFRESQ ATVLECVTEN GDKDVKYSWQ
KDGKEFKWQE HNIAQRKDEG SLVFLKPEAK DEGQYRCFAE SAAGVATSHI ISFRRTYMVV
PTTFKTVEKK PVEGSWLKLE CSIPEGYPKP TIVWRKQLGE DESIADSILA RRITQSPEGD
LYFTSVEKED VSESYKYVCA AKSPAIDGDV PLVGYTIKSL EKNTNQKNGE LVPMYVSNDM
IAKAGDVTMI YCMYGGVPMA YPNWFKDGKD VNGKPSDRIT RHNRTSGKRL FIKETLLEDQ
GTFTCDVNNE VGKPQKHSVK LTVVSGPRFT KKPEKQVIAK QGQDFVIPCE VSALPAAPVS
WTFNAKPISG SRVVASPSGL TIKGIQKSDK GYYGCQAHNE HGDAYAETLV IVA
