ID   ML1P_MANSE              Reviewed;         151 AA.
AC   B0FHH8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=MD-2-related lipid-recognition protein {ECO:0000303|PubMed:18343500};
DE            Short=MsML-1 {ECO:0000303|PubMed:18343500};
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] {ECO:0000305, ECO:0000312|EMBL:ABY55152.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-41, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, GLYCOSYLATION, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Fat body {ECO:0000269|PubMed:18343500}, and
RC   Larval hemolymph {ECO:0000269|PubMed:18343500};
RX   PubMed=18343500; DOI=10.1016/j.molimm.2008.02.006;
RA   Ao J.Q., Ling E., Rao X.J., Yu X.Q.;
RT   "A novel ML protein from Manduca sexta may function as a key accessory
RT   protein for lipopolysaccharide signaling.";
RL   Mol. Immunol. 45:2772-2781(2008).
CC   -!- FUNCTION: Binds to lipopolysaccharide from a variety of Gram-negative
CC       bacteria and to lipid A. {ECO:0000269|PubMed:18343500}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18343500}.
CC   -!- TISSUE SPECIFICITY: Hemolymph (at protein level). Constitutively
CC       expressed mainly in fat body and also in hemocytes and secreted into
CC       hemolymph. Not detected in midgut, epidermis, or Malpighian tubule of
CC       naive larvae. {ECO:0000269|PubMed:18343500}.
CC   -!- INDUCTION: Not induced in larvae following injection with
CC       microorganisms. {ECO:0000269|PubMed:18343500}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18343500}.
CC   -!- MASS SPECTROMETRY: Mass=16113.82; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18343500};
CC   -!- SIMILARITY: Belongs to the NPC2 family. {ECO:0000255}.
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DR   EMBL; EU329722; ABY55152.1; -; mRNA.
DR   AlphaFoldDB; B0FHH8; -.
DR   SMR; B0FHH8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR003172; ML_dom.
DR   InterPro; IPR039670; NPC2-like.
DR   PANTHER; PTHR11306; PTHR11306; 1.
DR   Pfam; PF02221; E1_DerP2_DerF2; 1.
DR   SMART; SM00737; ML; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Lipid-binding;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:18343500"
FT   CHAIN           19..151
FT                   /note="MD-2-related lipid-recognition protein"
FT                   /evidence="ECO:0000269|PubMed:18343500"
FT                   /id="PRO_0000407280"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..141
FT                   /evidence="ECO:0000250|UniProtKB:P49278"
FT   DISULFID        45..51
FT                   /evidence="ECO:0000250|UniProtKB:P49278"
FT   DISULFID        95..100
FT                   /evidence="ECO:0000250|UniProtKB:P49278"
SQ   SEQUENCE   151 AA;  17102 MW;  25E56BE43F6E7242 CRC64;
     MAALHWLLLA ALLGCTLAEE QAIFYNCEEA SEAVCSVKEV RINPCNPNKK CIFKKGVNAS
     ISFDFEPNFA SSKLVTTLYG PFDVEFDEMT NVDACQYTKC PTEPGKSQVL DYTLYIGKKL
     PQGTYTFKWK LWNPEETSQL CCFKTTIKIR K