ID MBL2_HYLLA Reviewed; 248 AA.
AC Q66S54;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, 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 Hylobates lar (Lar gibbon) (White-handed gibbon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Hylobates.
OX NCBI_TaxID=9580;
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; AY707507; AAU11296.1; -; Genomic_DNA.
DR EMBL; AY707504; AAU11296.1; JOINED; Genomic_DNA.
DR EMBL; AY707505; AAU11296.1; JOINED; Genomic_DNA.
DR EMBL; AY707506; AAU11296.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q66S54; -.
DR SMR; Q66S54; -.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IEA:UniProt.
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; Mannose-Binding Protein A, subunit A; 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 PANTHER; PTHR24024:SF34; MANNOSE-BINDING PROTEIN C; 1.
DR PANTHER; PTHR24024; PULMONARY SURFACTANT-ASSOCIATED PROTEIN A; 1.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57944; Triple coiled coil domain of C-type lectins; 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_0000017403"
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..107
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; 26298 MW; 4B2E2F04461E8ABF CRC64;
MSLIPSLSLL LMSMVAASYS ETVTCEDAQK TCPAVIACSS PGINGFPGKD GRDGTKGEKG
EPGQGLRGLQ GPPGKLGPPG NPGPSGSPGP KGQKGDPGKS PDCDSSLAVS ERKALQTEMA
RIKKWLTFSL GKQVGNKFFL TNGEMMTFEK VKALCVKFQA SVATPRNAAE NRAIQNLIKE
EAFMGITDEK TEGQFVDLTG NRLTYTNWNE GEPNNAGSDE DCVLLLKNGL WNDVPCSSSH
LAVCEFPI
//
