ID   Q58SN0_DROME            Unreviewed;       522 AA.
AC   Q58SN0;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Hemomucin {ECO:0000313|EMBL:AAX37998.1};
DE   Flags: Fragment;
GN   Name=Hmu {ECO:0000313|EMBL:AAX37998.1,
GN   ECO:0000313|FlyBase:FBgn0015737};
GN   ORFNames=CG3373 {ECO:0000313|FlyBase:FBgn0015737};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AAX37998.1};
RN   [1] {ECO:0000313|EMBL:AAX37998.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mel6 {ECO:0000313|EMBL:AAX37998.1};
RA   Schlenke T.A., Begun D.J.;
RT   "Linkage disequilibrium and recent selection at three potential immunity
RT   receptor loci in Drosophila simulans.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the strictosidine synthase family.
CC       {ECO:0000256|ARBA:ARBA00009191}.
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DR   EMBL; AY864360; AAX37998.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q58SN0; -.
DR   PeptideAtlas; Q58SN0; -.
DR   AGR; FB:FBgn0015737; -.
DR   FlyBase; FBgn0015737; Hmu.
DR   VEuPathDB; VectorBase:FBgn0015737; -.
DR   HOGENOM; CLU_023267_1_0_1; -.
DR   ChiTaRS; Hmu; fly.
DR   ExpressionAtlas; Q58SN0; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:FlyBase.
DR   GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR   GO; GO:0016844; F:strictosidine synthase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR018119; Strictosidine_synth_cons-reg.
DR   PANTHER; PTHR10426:SF106; ADIPOCYTE PLASMA MEMBRANE-ASSOCIATED PROTEIN HEMOMUCIN-RELATED; 1.
DR   PANTHER; PTHR10426; STRICTOSIDINE SYNTHASE-RELATED; 1.
DR   Pfam; PF20067; SSL_N; 1.
DR   Pfam; PF03088; Str_synth; 1.
DR   PRINTS; PR01217; PRICHEXTENSN.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE   3: Inferred from homology;
FT   DOMAIN          134..219
FT                   /note="Strictosidine synthase conserved region"
FT                   /evidence="ECO:0000259|Pfam:PF03088"
FT   REGION          388..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..522
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAX37998.1"
FT   NON_TER         522
FT                   /evidence="ECO:0000313|EMBL:AAX37998.1"
SQ   SEQUENCE   522 AA;  56884 MW;  929961CE01266E4C CRC64;
     VTPPKDLKGA LESNFHLEGA ERLLEWRVYG PECLIARNNE IYTGIHGGEV IKLTSNHVTH
     VTKIGQPCED IYEESRCGRP LGLAFDTQGN NLIIADAYYG LWQVDLGTNK KTLLVSLAQE
     LAGKSINRPA KIFNGVTVSK EGDVYWTDSS SDFTIEDLVF ASFANPSGRL FKYNRSKNVS
     EVLLDELAFA NGLALSPNED FIVVAETGAM RLTKYHLKGA KAGQSEVFVD GLPGLPDNLT
     PDAEGIWVPL VQSADSEHPN GFTLFTRFPS VRLFLARMLA LFELPFRYLN SVYPNKFSQR
     FIHFVGHMES ITVLAPKRTT VVRVDWNGNI VGSLHGFDKS AATISHVLEF QDFLFLGSPT
     NQYLARVKSP KAKQPTLKVR NVRVEGEGLE ASIGVPPSKA TPKPKAAPST TTPKPTTTTT
     TTTPKPTTKT TTTTTTPKPT TTTTTKKPTT TTTTTTTTPK PTTTKPPTAK PSTTTTTTTT
     PKPTTTTTPT TPTTPTPEPS KPKVKRTVPE KPAPVEEEIP SD
//