ID   EMBP1_CAVPO             Reviewed;         233 AA.
AC   P22032;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Eosinophil granule major basic protein 1;
DE            Short=MBP-1;
DE   Flags: Precursor;
GN   Name=MBP1;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 115-162.
RC   TISSUE=Eosinophil;
RX   PubMed=1705901; DOI=10.1016/0014-5793(91)80181-2;
RA   Aoki I., Shindoh Y., Nishida T., Nakai S., Hong Y.-M., Mio M., Saito T.,
RA   Tasaka K.;
RT   "Sequencing and cloning of the cDNA of guinea pig eosinophil major basic
RT   protein.";
RL   FEBS Lett. 279:330-334(1991).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8268206; DOI=10.1016/0167-4838(93)90089-a;
RA   Hashimoto Y., Nagaoka I., Yamashita T.;
RT   "Purification of the antibacterial fragments of guinea-pig major basic
RT   protein.";
RL   Biochim. Biophys. Acta 1203:236-242(1993).
CC   -!- FUNCTION: MBP may play some important roles in the allergic reactions
CC       and inflammations, since MBP is capable of releasing histamine from
CC       mast cells and damaging the epithelial cells of bronchial tubes.
CC       Antiparasitic and antibiotic.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule. Note=Matrix of eosinophil's
CC       large specific granule (crystalloid core).
CC   -!- PTM: Nitrated. {ECO:0000250}.
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DR   EMBL; D90251; BAA14291.1; -; mRNA.
DR   PIR; S13625; S13625.
DR   RefSeq; NP_001166538.1; NM_001173067.1.
DR   AlphaFoldDB; P22032; -.
DR   SMR; P22032; -.
DR   STRING; 10141.ENSCPOP00000017638; -.
DR   MEROPS; I63.001; -.
DR   GeneID; 100286788; -.
DR   KEGG; cpoc:100286788; -.
DR   CTD; 100286788; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   InParanoid; P22032; -.
DR   OrthoDB; 1328472at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   CDD; cd03598; CLECT_EMBP_like; 1.
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   InterPro; IPR033816; EMBP_CTLD.
DR   InterPro; IPR002352; Eosinophil_major_basic.
DR   Pfam; PF00059; Lectin_C; 1.
DR   PRINTS; PR00770; EMAJORBASICP.
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   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Immunity; Lectin; Nitration; Reference proteome; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   PROPEP          16..114
FT                   /note="Acidic"
FT                   /evidence="ECO:0000269|PubMed:1705901"
FT                   /id="PRO_0000017379"
FT   CHAIN           115..233
FT                   /note="Eosinophil granule major basic protein 1"
FT                   /id="PRO_0000017380"
FT   DOMAIN          132..233
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   REGION          24..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..89
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        134..231
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        208..223
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   233 AA;  26268 MW;  C8D5E96D927C56C8 CRC64;
     MKLLLLLALL LGAVSTRHLK VDTSSLQSLR GEESLAQDGE TAEGATREAT AGALMPLPEE
     EEMEGASGSE DDPEEEEEEE EEVEFSSELD VSPEDIQCPK EEDTVKFFSR PGYKTRGYVM
     VGSARTFNEA QWVCQRCYRG NLASIHSFAF NYQVQCTSAG LNVAQVWIGG QLRGKGRCRR
     FVWVDRTVWN FAYWARGQPW GGRQRGRCVT LCARGGHWRR SHCGKRRPFV CTY