MBL2_TRACR
ID MBL2_TRACR Reviewed; 248 AA.
AC Q66S45;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 61.
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 Trachypithecus cristatus (Silvered leaf-monkey) (Presbytis cristata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Trachypithecus.
OX NCBI_TaxID=122765;
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; AY707515; AAU11298.1; -; Genomic_DNA.
DR EMBL; AY707512; AAU11298.1; JOINED; Genomic_DNA.
DR EMBL; AY707513; AAU11298.1; JOINED; Genomic_DNA.
DR EMBL; AY707514; AAU11298.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q66S45; -.
DR SMR; Q66S45; -.
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_0000017409"
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..111
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; 26328 MW; 735FA50C0CCFAC8C CRC64;
MSLFPSLPLL LLCVVATSYS ETVNCEDSQK ICPAVIACNS PGINGFPGKD GRDGTKGEKG
EPGQGLRGLQ GPPGKLGPPG NPGPSGSPGP KGQKGDPGKS PDCDSSLAAS ERKALQTEMA
HIKKWLTFSL GRQVGNKFFL TNGEMMTFDK VKALCAKFQA SVATPSNAAE NRAIQNLIKE
EAFLGITDEN TEGQFVDLIG NRLTYTNWNN GEPNNADSDE DCVLLLKNGK WNDVPCSSSH
LALCEFPI
