HEMO_HYACE
ID HEMO_HYACE Reviewed; 413 AA.
AC P25033;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Hemolin;
DE AltName: Full=Hemocyte aggregation inhibitor;
DE AltName: Full=Protein P4;
DE Flags: Precursor;
OS Hyalophora cecropia (Cecropia moth) (Samia cecropia).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Saturniidae; Saturniinae; Attacini; Hyalophora.
OX NCBI_TaxID=7123;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2270488; DOI=10.1126/science.2270488;
RA Sun S.-C., Lindstroem I., Boman H.G., Faye I., Schmidt O.;
RT "Hemolin: an insect-immune protein belonging to the immunoglobulin
RT superfamily.";
RL Science 250:1729-1732(1990).
RN [2]
RP PROTEIN SEQUENCE OF 20-42.
RA Andersson K., Steiner H.;
RT "Structure and properties of protein P4, the major bacteria-inducible
RT protein in pupae of Hyalophora cecropia.";
RL Insect Biochem. 17:133-133(1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), SEQUENCE REVISION TO 173-177, AND
RP DISULFIDE BOND.
RX PubMed=9703515; DOI=10.1126/science.281.5379.991;
RA Su X.-D., Gastinel L.N., Vaughn D.E., Faye I., Poon P., Bjorkman P.J.;
RT "Crystal structure of hemolin: a horseshoe shape with implications for
RT homophilic adhesion.";
RL Science 281:991-995(1998).
CC -!- FUNCTION: Insect-immune protein. Forms a protein complex at the
CC bacterial surface. Can inhibit hemocyte aggregation.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Hemolymph.
CC -!- INDUCTION: By bacterial infection, wounding, or bacterial cell wall
CC components injection.
CC -!- SIMILARITY: Belongs to the hemolin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M63398; AAA29188.1; -; mRNA.
DR PIR; A37778; A37778.
DR PDB; 1BIH; X-ray; 3.10 A; A/B=19-413.
DR PDBsum; 1BIH; -.
DR AlphaFoldDB; P25033; -.
DR SMR; P25033; -.
DR EvolutionaryTrace; P25033; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunity; Immunoglobulin domain; Innate immunity; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 20..413
FT /note="Hemolin"
FT /id="PRO_0000014772"
FT DOMAIN 25..112
FT /note="Ig-like C2-type 1"
FT DOMAIN 122..211
FT /note="Ig-like C2-type 2"
FT DOMAIN 233..322
FT /note="Ig-like C2-type 3"
FT DOMAIN 327..413
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:0000269|PubMed:9703515,
FT ECO:0007744|PDB:1BIH"
FT DISULFID 140..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:9703515, ECO:0007744|PDB:1BIH"
FT DISULFID 252..305
FT /evidence="ECO:0000269|PubMed:9703515,
FT ECO:0007744|PDB:1BIH"
FT DISULFID 349..395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:9703515, ECO:0007744|PDB:1BIH"
FT CONFLICT 173..177
FT /note="ITAGP -> NHSWT (in Ref. 1; AAA29188)"
FT /evidence="ECO:0000305"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:1BIH"
FT TURN 68..72
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:1BIH"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:1BIH"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:1BIH"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 193..202
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:1BIH"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 315..331
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:1BIH"
FT STRAND 402..412
FT /evidence="ECO:0007829|PDB:1BIH"
SQ SEQUENCE 413 AA; 45649 MW; 1008C7B9A2532057 CRC64;
MAFKSIAVLS ACIIVGSALP VDKYPVLKDQ PAEVLFRENN PTVLECIIEG NDQGVKYSWK
KDGKSYNWQE HNAALRKDEG SLVFLRPQAS DEGHYQCFAE TPAGVASSRV ISFRKTYLIA
SPAKTHEKTP IEGRPFQLDC VLPNAYPKPL ITWKKRLSGA DPNADVTDFD RRITAGPDGN
LYFTIVTKED VSDIYKYVCT AKNAAVDEEV VLVEYEIKGV TKDNSGYKGE PVPQYVSKDM
MAKAGDVTMI YCMYGSNPMG YPNYFKNGKD VNGNPEDRIT RHNRTSGKRL LFKTTLPEDE
GVYTCEVDNG VGKPQKHSLK LTVVSAPKYE QKPEKVIVVK QGQDVTIPCK VTGLPAPNVV
WSHNAKPLSG GRATVTDSGL VIKGVKNGDK GYYGCRATNE HGDKYFETLV QVN
