ID   LECA_SARPE              Reviewed;         283 AA.
AC   P05047;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Lectin subunit alpha;
DE   Flags: Precursor;
OS   Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Sarcophagidae; Sarcophaga; Boettcherisca.
OX   NCBI_TaxID=7386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2413021; DOI=10.1016/s0021-9258(17)39014-2;
RA   Takahashi H., Komano H., Kawaguchi N., Kitamura N., Nakanishi S.,
RA   Natori S.;
RT   "Cloning and sequencing of cDNA of Sarcophaga peregrina humoral lectin
RT   induced on injury of the body wall.";
RL   J. Biol. Chem. 260:12228-12233(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8307011; DOI=10.1111/j.1432-1033.1994.tb19958.x;
RA   Matsui M., Kobayashi A., Kubo T., Natori S.;
RT   "Purification and characterization of ATBP, a novel protein that binds to
RT   A/T stretches in three segments of the Sarcophaga lectin gene.";
RL   Eur. J. Biochem. 219:449-454(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
RX   PubMed=2480809; DOI=10.1016/0167-4781(89)90109-7;
RA   Kobayashi A., Hirai H., Kubo T., Veno K., Nakanishi Y., Natori S.;
RT   "Cloning and in vitro transcription of the Sarcophaga lectin gene.";
RL   Biochim. Biophys. Acta 1009:244-250(1989).
CC   -!- FUNCTION: Role in the defense system of the organism against
CC       microorganisms. This lectin binds galactose.
CC   -!- INDUCTION: By injury of the body wall.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; M11673; AAA29983.1; -; mRNA.
DR   EMBL; D14870; BAA03586.1; -; Genomic_DNA.
DR   EMBL; X16659; CAA34645.1; -; Genomic_DNA.
DR   PIR; S07759; LNFHLS.
DR   AlphaFoldDB; P05047; -.
DR   SMR; P05047; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Lectin; Signal.
FT   SIGNAL          1..23
FT   CHAIN           24..283
FT                   /note="Lectin subunit alpha"
FT                   /id="PRO_0000017393"
FT   DOMAIN          51..159
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        53..157
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        132..149
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   283 AA;  32991 MW;  F324BF1A1140B3AC CRC64;
     MSLTMKNVEG FVIFLVIFTS TAAVPQLQKA LDGREYLIET ELKYNWHQAW HECARHDQQL
     VTIESADKNN AIIDLVKRVV GKSHNLWLGG NDEYSSSRDY GRPFFWSPTG QAFSFAYWSE
     NNPDNYKHQE HCVHIWDTKP LYQWNDNDCN VKMGYICEPN HFRETYDQAL KQKCEAIKIT
     NSKISTEFDQ LHAKQSLEFD SITQNVAKVN EDWKIEIQKL QNATQIAIQQ IMENHEKKIR
     DLSDNLLKQL QDSNEQLKQS TDHMNASFGE KLKGQQAENN EIC