ID G7N2G0_MACMU Unreviewed; 248 AA.
AC G7N2G0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Mannose-binding protein C {ECO:0000256|ARBA:ARBA00021805};
DE AltName: Full=MBP1 {ECO:0000256|ARBA:ARBA00029921};
DE AltName: Full=Mannan-binding protein {ECO:0000256|ARBA:ARBA00032886};
DE AltName: Full=Mannose-binding lectin {ECO:0000256|ARBA:ARBA00032099};
GN ORFNames=EGK_19851 {ECO:0000313|EMBL:EHH19187.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH19187.1};
RN [1] {ECO:0000313|EMBL:EHH19187.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH19187.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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. {ECO:0000256|ARBA:ARBA00025689}.
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. {ECO:0000256|ARBA:ARBA00026014}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; CM001261; EHH19187.1; -; Genomic_DNA.
DR AlphaFoldDB; G7N2G0; -.
DR Proteomes; UP000013456; Chromosome 9.
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 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Complement activation lectin pathway {ECO:0000256|ARBA:ARBA00023153};
KW Complement pathway {ECO:0000256|ARBA:ARBA00022875};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Immunity {ECO:0000256|ARBA:ARBA00022859};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Mannose-binding {ECO:0000256|ARBA:ARBA00023035};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..248
FT /note="Mannose-binding protein C"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003500595"
FT DOMAIN 134..245
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 43..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 248 AA; 26342 MW; 98F2F06E9BD619DD CRC64;
MSLFPSLTLL LLSVVATSYS ETVTCEDSQK ICPAVIACNS PGINGFPGKD GRDGTKGEKG
EPGQGLRGLQ GPPGKLGPPG NPGSSGSPGP KGQKGDPGES PDCESSLAAS ERKALQTEMA
RIKKWLTFSL GRQVGNQFFL TNGEMMTFDK VKALCAEFRA SVATPRNAAE NRAIQNLIKE
EAFLGITDEN TEGEFVDLTG NKLTYTNWND GEPNNAGSNE DCVLLLKNGK WNDIPCSSSH
LALCEFPI
//
