EMBP2_CAVPO
ID EMBP2_CAVPO Reviewed; 234 AA.
AC P35709;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Eosinophil granule major basic protein 2;
DE Short=MBP-2;
DE Flags: Precursor;
GN Name=MBP2;
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 PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Eosinophil;
RX PubMed=2026266; DOI=10.1016/0014-5793(91)80443-7;
RA Aoki I., Shindoh Y., Nishida T., Nakai S., Hong Y.-M., Mio M., Saito T.,
RA Tasaka K.;
RT "Comparison of the amino acid and nucleotide sequences between human and
RT two guinea pig major basic proteins.";
RL FEBS Lett. 282:56-60(1991).
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; D00817; BAA00697.1; -; mRNA.
DR PIR; S15102; S15102.
DR RefSeq; NP_001166350.1; NM_001172879.1.
DR AlphaFoldDB; P35709; -.
DR SMR; P35709; -.
DR STRING; 10141.ENSCPOP00000015284; -.
DR MEROPS; I63.001; -.
DR GeneID; 100379574; -.
DR KEGG; cpoc:100379574; -.
DR CTD; 100379574; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P35709; -.
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 Glycoprotein; Immunity; Lectin; Nitration; Proteoglycan;
KW Reference proteome; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..115
FT /note="Acidic"
FT /id="PRO_0000017381"
FT CHAIN 116..234
FT /note="Eosinophil granule major basic protein 2"
FT /id="PRO_0000017382"
FT DOMAIN 133..234
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 26..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..86
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 69
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000250"
FT DISULFID 135..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 209..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 234 AA; 26140 MW; 7D926A942BF5116F CRC64;
MKLLLLLALL VGAVSTRHLN VDTSSLQSLQ GEESLAQDGE TAEGATREAA SGVLMPLREE
VKEEMEGGSG SEDDPEEEEE EKEMESSSEL DMGPEDVQCP KEEDIVKFEG SPGCKICRYV
VLSVPKTFKQ AQSVCQRCFR GNLASIHSYN INLQVQRSSR ILNVAQVWIG GQLRGKGHHK
HFHWVDGTLW NFWYWAAGQP WRGNNSGRCV TLCARGGHWR RSHCGVRRAF SCSY