ID   MBL2_CHLAE              Reviewed;         248 AA.
AC   Q66S37;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Mannose-binding protein C;
DE            Short=MBP-C;
DE   AltName: Full=MBP1;
DE   AltName: Full=Mannan-binding protein;
DE   AltName: Full=Mannose-binding lectin;
DE   Flags: Precursor;
GN   Name=MBL2;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15483660; DOI=10.1038/sj.gene.6364140;
RA   Verga Falzacappa M.V., Segat L., Puppini B., Amoroso A., Crovella S.;
RT   "Evolution of the mannose-binding lectin gene in primates.";
RL   Genes Immun. 5:653-661(2004).
CC   -!- FUNCTION: Calcium-dependent lectin involved in innate immune defense.
CC       Binds mannose, fucose and N-acetylglucosamine on different
CC       microorganisms and activates the lectin complement pathway. Binds to
CC       late apoptotic cells, as well as to apoptotic blebs and to necrotic
CC       cells, but not to early apoptotic cells, facilitating their uptake by
CC       macrophages (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Oligomeric complex of 3 or more homotrimers. Interacts with
CC       MASP1 and MASP2 (By similarity). Interacts with MEP1A and MEP1B and may
CC       inhibit their catalytic activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DOMAIN: The coiled-coil domain mediates trimerization. {ECO:0000250}.
CC   -!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG,
CC       is most likely to be 4-hydroxy as this fits the requirement for 4-
CC       hydroxylation in vertebrates. {ECO:0000250}.
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DR   EMBL; AY707523; AAU11300.1; -; Genomic_DNA.
DR   EMBL; AY707520; AAU11300.1; JOINED; Genomic_DNA.
DR   EMBL; AY707521; AAU11300.1; JOINED; Genomic_DNA.
DR   EMBL; AY707522; AAU11300.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q66S37; -.
DR   SMR; Q66S37; -.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0001867; P:complement activation, lectin pathway; IEA:UniProtKB-KW.
DR   CDD; cd03591; CLECT_collectin_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; IPR008160; Collagen.
DR   InterPro; IPR033990; Collectin_CTLD.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR037570; Mannose-binding_protein_C.
DR   PANTHER; PTHR24024:SF34; PTHR24024:SF34; 1.
DR   Pfam; PF01391; Collagen; 1.
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   3: Inferred from homology;
KW   Calcium; Coiled coil; Collagen; Complement activation lectin pathway;
KW   Complement pathway; Disulfide bond; Hydroxylation; Immunity;
KW   Innate immunity; Lectin; Mannose-binding; Repeat; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..248
FT                   /note="Mannose-binding protein C"
FT                   /id="PRO_0000017399"
FT   DOMAIN          42..99
FT                   /note="Collagen-like"
FT   DOMAIN          134..245
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   REGION          43..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          112..130
FT                   /evidence="ECO:0000250"
FT   MOD_RES         47
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         73
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         79
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         82
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         88
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250"
FT   DISULFID        155..244
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        222..236
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   248 AA;  26238 MW;  428375505E88BCBB CRC64;
     MSLFPSLTLL LLSVVATSYS ETVTCEDSQK ICPAVIACNS PGINGFPGKD GRDGTKGEKG
     EPGQGLRGLQ GPPGKLGPPG NPGSSGSPGP KGQKGDPGES PDGDSSLAAS ERKALQTEMA
     RIKKWLTFSL GRQVGNKFFL TNGEMMSFDK VKALCAKFQA SVATPRNAAE NRAIQNLIKE
     EAFLGITDEN TEGEFVDLTG NKLTYTNWNN GEPNNAGSNE DCVLLLKNGK WNDIPCSSSH
     LALCEFPI