MBL2_HUMAN
ID MBL2_HUMAN Reviewed; 248 AA.
AC P11226; Q4VB12; Q4VB13; Q4VB14; Q5SQS3; Q86SI4; Q96KE4; Q96TF7; Q96TF8;
AC Q96TF9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=Mannose-binding protein C {ECO:0000305};
DE Short=MBP-C;
DE AltName: Full=Collectin-1;
DE AltName: Full=MBP1;
DE AltName: Full=Mannan-binding protein;
DE AltName: Full=Mannose-binding lectin;
DE Flags: Precursor;
GN Name=MBL2 {ECO:0000312|HGNC:HGNC:6922}; Synonyms=COLEC1, MBL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2450948; DOI=10.1084/jem.167.3.1034;
RA Ezekowitz R.A.B., Day L.E., Herman G.A.;
RT "A human mannose-binding protein is an acute-phase reactant that shares
RT sequence homology with other vertebrate lectins.";
RL J. Exp. Med. 167:1034-1046(1988).
RN [2]
RP ERRATUM OF PUBMED:2450948.
RA Ezekowitz R.A.B., Day L.E., Herman G.A.;
RL J. Exp. Med. 174:753-753(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION.
RC TISSUE=Liver;
RX PubMed=2477486; DOI=10.1084/jem.170.4.1175;
RA Sastry K., Herman G.A., Day L.E., Deignan E., Bruns G., Morton C.C.,
RA Ezekowitz R.A.B.;
RT "The human mannose-binding protein gene. Exon structure reveals its
RT evolutionary relationship to a human pulmonary surfactant gene and
RT localization to chromosome 10.";
RL J. Exp. Med. 170:1175-1189(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2590164; DOI=10.1042/bj2620763;
RA Taylor M.E., Brickell P.M., Craig R.K., Summerfield J.A.;
RT "Structure and evolutionary origin of the gene encoding a human serum
RT mannose-binding protein.";
RL Biochem. J. 262:763-771(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-52; ASP-54 AND GLU-57.
RX PubMed=9743385;
RA Madsen H.O., Satz M.L., Hogh B., Svejgaard A., Garred P.;
RT "Different molecular events result in low protein levels of mannan-binding
RT lectin in populations from South-East Africa and South America.";
RL J. Immunol. 161:3169-3175(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-24.
RC TISSUE=Liver;
RA Chen Z., Zhu X., Xie P.;
RT "Cloning and sequencing of mannan-binding lectin cDNA of Chinese.";
RL Mian Yi Xue Za Zhi 15:83-86(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wu Z., Zhang S., Wang Y.;
RT "Prokaryotic expression of human mbl.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tan J., Ong R., Hibberd M.L., Seielstad M.;
RT "Genetic variation in immune response genes.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lai Q., Zuo D., Chen Z.;
RT "Cloning and sequencing of mannan-binding lectin gene from chinese Han
RT people.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-54.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59, AND VARIANT ASP-54.
RX PubMed=12175909; DOI=10.1016/s0027-5107(02)00142-2;
RA Jueliger S., Kremsner P.G., Alpers M.P., Reeder J.C., Kun J.F.J.;
RT "Restricted polymorphisms of the mannose-binding lectin gene in a
RT population of Papua New Guinea.";
RL Mutat. Res. 505:87-91(2002).
RN [13]
RP PROTEIN SEQUENCE OF 21-248, SUBCELLULAR LOCATION, AND HYDROXYLATION AT
RP PRO-47; PRO-73; PRO-79; PRO-82 AND PRO-88.
RC TISSUE=Liver, and Plasma;
RX PubMed=7982896; DOI=10.1093/oxfordjournals.jbchem.a124471;
RA Kurata H., Sannoh T., Kozutsumi Y., Yokota Y., Kawasaki T.;
RT "Structure and function of mannan-binding proteins isolated from human
RT liver and serum.";
RL J. Biochem. 115:1148-1154(1994).
RN [14]
RP INTERACTION WITH MASP1 AND MASP2.
RX PubMed=9087411; DOI=10.1038/386506a0;
RA Thiel S., Vorup-Jensen T., Stover C.M., Schwaeble W.J., Laursen S.B.,
RA Poulsen K., Willis A.C., Eggleton P., Hansen S., Holmskov U., Reid K.B.M.,
RA Jensenius J.C.;
RT "A second serine protease associated with mannan-binding lectin that
RT activates complement.";
RL Nature 386:506-510(1997).
RN [15]
RP FUNCTION.
RX PubMed=14515269; DOI=10.1002/eji.200323888;
RA Nauta A.J., Raaschou-Jensen N., Roos A., Daha M.R., Madsen H.O.,
RA Borrias-Essers M.C., Ryder L.P., Koch C., Garred P.;
RT "Mannose-binding lectin engagement with late apoptotic and necrotic
RT cells.";
RL Eur. J. Immunol. 33:2853-2863(2003).
RN [16]
RP DNA-BINDING.
RX PubMed=15145932; DOI=10.1074/jbc.m403763200;
RA Palaniyar N., Nadesalingam J., Clark H., Shih M.J., Dodds A.W.,
RA Reid K.B.M.;
RT "Nucleic acid is a novel ligand for innate, immune pattern recognition
RT collectins surfactant proteins A and D and mannose-binding lectin.";
RL J. Biol. Chem. 279:32728-32736(2004).
RN [17]
RP INTERACTION WITH MEP1A AND MEP1B.
RX PubMed=16116208; DOI=10.4049/jimmunol.175.5.3177;
RA Hirano M., Ma B.Y., Kawasaki N., Okimura K., Baba M., Nakagawa T., Miwa K.,
RA Kawasaki N., Oka S., Kawasaki T.;
RT "Mannan-binding protein blocks the activation of metalloproteases meprin
RT alpha and beta.";
RL J. Immunol. 175:3177-3185(2005).
RN [18]
RP TISSUE SPECIFICITY.
RX PubMed=18006063; DOI=10.1016/j.molimm.2007.10.006;
RA Hummelshoej T., Fog L.M., Madsen H.O., Sim R.B., Garred P.;
RT "Comparative study of the human ficolins reveals unique features of
RT Ficolin-3 (Hakata antigen).";
RL Mol. Immunol. 45:1623-1632(2008).
RN [19]
RP INTERACTION WITH CR1.
RX PubMed=23460739; DOI=10.4049/jimmunol.1202451;
RA Jacquet M., Lacroix M., Ancelet S., Gout E., Gaboriaud C., Thielens N.M.,
RA Rossi V.;
RT "Deciphering complement receptor type 1 interactions with recognition
RT proteins of the lectin complement pathway.";
RL J. Immunol. 190:3721-3731(2013).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP INTERACTION WITH CR1.
RX PubMed=29563915; DOI=10.3389/fimmu.2018.00453;
RA Jacquet M., Cioci G., Fouet G., Bally I., Thielens N.M., Gaboriaud C.,
RA Rossi V.;
RT "C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on
RT CCP24-25 Modules.";
RL Front. Immunol. 9:453-453(2018).
RN [22]
RP INTERACTION WITH SARS-COV-2 SPIKE GLYCOPROTEIN (MICROBIAL FUNCTION),
RP FUNCTION, AND POLYMORPHISM.
RX PubMed=35102342; DOI=10.1038/s41590-021-01114-w;
RA Stravalaci M., Pagani I., Paraboschi E.M., Pedotti M., Doni A.,
RA Scavello F., Mapelli S.N., Sironi M., Perucchini C., Varani L.,
RA Matkovic M., Cavalli A., Cesana D., Gallina P., Pedemonte N., Capurro V.,
RA Clementi N., Mancini N., Invernizzi P., Bayarri-Olmos R., Garred P.,
RA Rappuoli R., Duga S., Bottazzi B., Uguccioni M., Asselta R., Vicenzi E.,
RA Mantovani A., Garlanda C.;
RT "Recognition and inhibition of SARS-CoV-2 by humoral innate immunity
RT pattern recognition molecules.";
RL Nat. Immunol. 23:275-286(2022).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 108-248, SUBUNIT, AND COILED-COIL.
RX PubMed=7634089; DOI=10.1038/nsb1194-789;
RA Sheriff S., Chang C.Y., Ezekowitz R.A.;
RT "Human mannose-binding protein carbohydrate recognition domain trimerizes
RT through a triple alpha-helical coiled-coil.";
RL Nat. Struct. Biol. 1:789-794(1994).
RN [24]
RP VARIANT ASP-54, AND ASSOCIATION WITH MANNOSE-BINDING PROTEIN DEFICIENCY AND
RP SUSCEPTIBILITY TO CHRONIC INFECTIONS.
RX PubMed=1675710; DOI=10.1016/0140-6736(91)93263-9;
RA Sumiya M., Super M., Tabona P., Levinsky R.J., Arai T., Turner M.W.,
RA Summerfield J.A.;
RT "Molecular basis of opsonic defect in immunodeficient children.";
RL Lancet 337:1569-1570(1991).
RN [25]
RP VARIANTS ASP-54 AND GLU-57, AND ASSOCIATION WITH MANNOSE-BINDING PROTEIN
RP DEFICIENCY.
RX PubMed=1304173; DOI=10.1093/hmg/1.9.709;
RA Lipscombe R.J., Sumiya M., Hill A.V.S., Lau Y.L., Levinsky R.J.,
RA Summerfield J.A., Turner M.W.;
RT "High frequencies in African and non-African populations of independent
RT mutations in the mannose binding protein gene.";
RL Hum. Mol. Genet. 1:709-715(1992).
RN [26]
RP ERRATUM OF PUBMED:1304173.
RA Lipscombe R.J., Sumiya M., Hill A.V.S., Lau Y.L., Levinsky R.J.,
RA Summerfield J.A., Turner M.W.;
RL Hum. Mol. Genet. 2:342-342(1993).
RN [27]
RP VARIANT ASP-54.
RX PubMed=1303250; DOI=10.1038/ng0992-50;
RA Super M., Gillies S.D., Foley S., Sastry K., Schweinle J.E.,
RA Silverman V.J., Ezekowitz R.A.;
RT "Distinct and overlapping functions of allelic forms of human mannose
RT binding protein.";
RL Nat. Genet. 2:50-55(1992).
RN [28]
RP VARIANTS CYS-52; ASP-54 AND GLU-57.
RX PubMed=10447262;
RX DOI=10.1002/(sici)1098-1004(1999)14:1<80::aid-humu10>3.0.co;2-j;
RA Gabolde M., Muralitharan S., Besmond C.;
RT "Genotyping of the three major allelic variants of the human mannose-
RT binding lectin gene by denaturing gradient gel electrophoresis.";
RL Hum. Mutat. 14:80-83(1999).
RN [29]
RP INVOLVEMENT IN SUSCEPTIBILITY TO HBV INFECTION, AND VARIANTS CYS-52; ASP-54
RP AND GLU-57.
RX PubMed=15994813; DOI=10.1128/jvi.79.14.9192-9196.2005;
RA Thio C.L., Mosbruger T., Astemborski J., Greer S., Kirk G.D., O'Brien S.J.,
RA Thomas D.L.;
RT "Mannose binding lectin genotypes influence recovery from hepatitis B virus
RT infection.";
RL J. Virol. 79:9192-9196(2005).
RN [30]
RP VARIANT GLU-57, AND ASSOCIATION WITH PROTECTION AGAINST TUBERCULOSIS.
RX PubMed=21695215; DOI=10.1371/journal.pone.0020908;
RA Thye T., Niemann S., Walter K., Homolka S., Intemann C.D., Chinbuah M.A.,
RA Enimil A., Gyapong J., Osei I., Owusu-Dabo E., Rusch-Gerdes S.,
RA Horstmann R.D., Ehlers S., Meyer C.G.;
RT "Variant G57E of mannose binding lectin associated with protection against
RT tuberculosis caused by Mycobacterium africanum but not by M.
RT tuberculosis.";
RL PLoS ONE 6:E20908-E20908(2011).
CC -!- FUNCTION: Calcium-dependent lectin involved in innate immune defense
CC (PubMed:35102342). Binds mannose, fucose and N-acetylglucosamine on
CC different microorganisms and activates the lectin complement pathway.
CC Binds to late apoptotic cells, as well as to apoptotic blebs and to
CC necrotic cells, but not to early apoptotic cells, facilitating their
CC uptake by macrophages. May bind DNA. Upon SARS coronavirus-2/SARS-CoV-2
CC infection, activates the complement lectin pathway which leads to the
CC inhibition SARS-CoV-2 infection and a reduction of the induced
CC inflammatory response (PubMed:35102342). {ECO:0000269|PubMed:14515269,
CC ECO:0000269|PubMed:35102342}.
CC -!- SUBUNIT: Oligomeric complex of 3 or more homotrimers. Interacts with
CC MASP1 and MASP2. Interacts with MEP1A and MEP1B and may inhibit their
CC catalytic activity. Interacts with CR1 (via Sushi 24 and Sushi 25
CC domains). {ECO:0000269|PubMed:16116208, ECO:0000269|PubMed:23460739,
CC ECO:0000269|PubMed:29563915, ECO:0000269|PubMed:7634089,
CC ECO:0000269|PubMed:9087411}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS coronavirus-2/SARS-
CC CoV-2 Spike glycoprotein homotrimer; the interaction is calcium-
CC dependent and modulated by Spike glycoprotein glycosylation state.
CC {ECO:0000269|PubMed:35102342}.
CC -!- INTERACTION:
CC P11226; P02743: APCS; NbExp=2; IntAct=EBI-5325353, EBI-2115799;
CC P11226; P02749: APOH; NbExp=3; IntAct=EBI-5325353, EBI-2114682;
CC P11226; P27797: CALR; NbExp=6; IntAct=EBI-5325353, EBI-1049597;
CC P11226; P17927: CR1; NbExp=8; IntAct=EBI-5325353, EBI-2807625;
CC P11226; Q9UGM3: DMBT1; NbExp=2; IntAct=EBI-5325353, EBI-1044970;
CC P11226; Q07954: LRP1; NbExp=5; IntAct=EBI-5325353, EBI-1046087;
CC P11226; P48740-1: MASP1; NbExp=9; IntAct=EBI-5325353, EBI-16138717;
CC P11226; P48740-2: MASP1; NbExp=8; IntAct=EBI-5325353, EBI-26435098;
CC P11226; P48740-3: MASP1; NbExp=7; IntAct=EBI-5325353, EBI-26435118;
CC P11226; PRO_0000027592 [P48740]: MASP1; NbExp=2; IntAct=EBI-5325353, EBI-26356151;
CC P11226; O00187: MASP2; NbExp=6; IntAct=EBI-5325353, EBI-7965040;
CC P11226; O00187-2: MASP2; NbExp=3; IntAct=EBI-5325353, EBI-26356134;
CC P11226; PRO_0000027598 [O00187]: MASP2; NbExp=2; IntAct=EBI-5325353, EBI-25426044;
CC P11226; P11226: MBL2; NbExp=6; IntAct=EBI-5325353, EBI-5325353;
CC P11226; P10124: SRGN; NbExp=4; IntAct=EBI-5325353, EBI-744915;
CC P11226; O00206: TLR4; NbExp=2; IntAct=EBI-5325353, EBI-528701;
CC P11226; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-5325353, EBI-947187;
CC P11226; PRO_0000037570 [P27958]; Xeno; NbExp=6; IntAct=EBI-5325353, EBI-6904269;
CC PRO_0000017401; PRO_0000000214 [P9WQP3]: fbpA; Xeno; NbExp=2; IntAct=EBI-25427940, EBI-26878164;
CC PRO_0000017401; P9WQP1: fbpB; Xeno; NbExp=2; IntAct=EBI-25427940, EBI-26878221;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7982896}.
CC -!- TISSUE SPECIFICITY: Plasma protein produced mainly in the liver.
CC {ECO:0000269|PubMed:18006063}.
CC -!- DOMAIN: The coiled-coil domain mediates trimerization.
CC -!- POLYMORPHISM: Genetic variations in MBL2 influence susceptibility to
CC hepatitis B virus (HBV) infection [MIM:610424].
CC {ECO:0000269|PubMed:15994813}.
CC -!- POLYMORPHISM: Genetic variations in MBL2 may influence susceptibility
CC to severe COVID-19 disease caused by SARS-CoV-2 virus infection.
CC {ECO:0000269|PubMed:35102342}.
CC -!- POLYMORPHISM: Genetic variations in MBL2 are responsible for mannose-
CC binding protein deficiency [MIM:614372]. This condition is defined as
CC MBL2 protein level of less than 100 ng/ml, is present in about 5% of
CC people of European descent and in about 10% of sub-Saharan Africans.
CC Most MBL2-deficient adults appear healthy, but low levels of MBL2 are
CC associated with increased risk of infection in toddlers, in cancer
CC patients undergoing chemotherapy, and in organ-transplant patients
CC receiving immunosuppressive drugs, particularly recipients of liver
CC transplants. There is an association between low levels of MBL2 and a
CC defect of opsonization which results in susceptibility to frequent and
CC chronic infections (PubMed:1675710). Functional MBL2 deficiency may be
CC associated with protection against tuberculosis caused by Mycobacterium
CC africanum but not by Mycobacterium tuberculosis, as observed in studies
CC on Ghanaian patients with pulmonary tuberculosis (PubMed:21695215).
CC {ECO:0000269|PubMed:1675710, ECO:0000269|PubMed:21695215}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Mannose-binding protein;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_227";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X15422; CAA33462.1; -; mRNA.
DR EMBL; X15954; CAA34079.1; -; Genomic_DNA.
DR EMBL; X15955; CAA34079.1; JOINED; Genomic_DNA.
DR EMBL; X15956; CAA34079.1; JOINED; Genomic_DNA.
DR EMBL; X15957; CAA34079.1; JOINED; Genomic_DNA.
DR EMBL; AF080510; AAC31937.1; -; Genomic_DNA.
DR EMBL; AF080508; AAC31937.1; JOINED; Genomic_DNA.
DR EMBL; AF080509; AAC31937.1; JOINED; Genomic_DNA.
DR EMBL; Y16576; CAB56044.1; -; Genomic_DNA.
DR EMBL; Y16577; CAB56120.1; -; Genomic_DNA.
DR EMBL; Y16578; CAB56045.1; -; Genomic_DNA.
DR EMBL; Y16579; CAB56121.1; -; Genomic_DNA.
DR EMBL; Y16580; CAB56122.1; -; Genomic_DNA.
DR EMBL; Y16581; CAB56123.1; -; Genomic_DNA.
DR EMBL; Y16582; CAB56124.1; -; Genomic_DNA.
DR EMBL; AF360991; AAK52907.1; -; mRNA.
DR EMBL; AY826184; AAV80468.1; -; mRNA.
DR EMBL; DQ217939; ABB01009.1; -; Genomic_DNA.
DR EMBL; EU596574; ACC62880.1; -; Genomic_DNA.
DR EMBL; CH471083; EAW54148.1; -; Genomic_DNA.
DR EMBL; CH471083; EAW54149.1; -; Genomic_DNA.
DR EMBL; BC096179; AAH96179.1; -; mRNA.
DR EMBL; BC096180; AAH96180.3; -; mRNA.
DR EMBL; BC069338; AAH69338.1; -; mRNA.
DR EMBL; BC096181; AAH96181.3; -; mRNA.
DR EMBL; BC096182; AAH96182.3; -; mRNA.
DR EMBL; AF482699; AAN39274.1; -; Genomic_DNA.
DR EMBL; AF482700; AAN39275.1; -; Genomic_DNA.
DR CCDS; CCDS7247.1; -.
DR PIR; JL0115; LNHUMC.
DR RefSeq; NP_000233.1; NM_000242.2.
DR RefSeq; XP_006717924.1; XM_006717861.3.
DR RefSeq; XP_011538118.1; XM_011539816.2.
DR PDB; 1HUP; X-ray; 2.50 A; A=108-248.
DR PDBsum; 1HUP; -.
DR AlphaFoldDB; P11226; -.
DR SMR; P11226; -.
DR BioGRID; 110323; 33.
DR ComplexPortal; CPX-6170; MBL2-MASP1 lectin-protease complex.
DR ComplexPortal; CPX-6203; MBL2-MASP2 lectin-protease complex.
DR DIP; DIP-61381N; -.
DR IntAct; P11226; 26.
DR MINT; P11226; -.
DR STRING; 9606.ENSP00000363079; -.
DR ChEMBL; CHEMBL1795113; -.
DR DrugBank; DB02837; 4-(Hydrogen sulfate)-beta-D-galactopyranose.
DR DrugBank; DB03879; alpha-L-methyl-fucose.
DR DrugBank; DB04426; Alpha-Methyl-N-Acetyl-D-Glucosamine.
DR DrugBank; DB01979; Methyl alpha-D-mannoside.
DR DrugBank; DB03194; Methyl beta-L-fucopyranoside.
DR DrugBank; DB03721; N-acetyl-alpha-neuraminic acid.
DR DrugBank; DB01818; O3-Sulfonylgalactose.
DR UniLectin; P11226; -.
DR iPTMnet; P11226; -.
DR PhosphoSitePlus; P11226; -.
DR BioMuta; MBL2; -.
DR DMDM; 126676; -.
DR CPTAC; non-CPTAC-2684; -.
DR jPOST; P11226; -.
DR MassIVE; P11226; -.
DR PaxDb; P11226; -.
DR PeptideAtlas; P11226; -.
DR PRIDE; P11226; -.
DR ProteomicsDB; 52723; -.
DR TopDownProteomics; P11226; -.
DR Antibodypedia; 693; 759 antibodies from 40 providers.
DR DNASU; 4153; -.
DR Ensembl; ENST00000373968.3; ENSP00000363079.3; ENSG00000165471.7.
DR Ensembl; ENST00000674931.1; ENSP00000502789.1; ENSG00000165471.7.
DR Ensembl; ENST00000675947.1; ENSP00000502615.1; ENSG00000165471.7.
DR GeneID; 4153; -.
DR KEGG; hsa:4153; -.
DR MANE-Select; ENST00000674931.1; ENSP00000502789.1; NM_001378373.1; NP_001365302.1.
DR UCSC; uc001jjt.3; human.
DR CTD; 4153; -.
DR DisGeNET; 4153; -.
DR GeneCards; MBL2; -.
DR HGNC; HGNC:6922; MBL2.
DR HPA; ENSG00000165471; Tissue enriched (liver).
DR MalaCards; MBL2; -.
DR MIM; 154545; gene.
DR MIM; 610424; phenotype.
DR MIM; 614372; phenotype.
DR neXtProt; NX_P11226; -.
DR OpenTargets; ENSG00000165471; -.
DR Orphanet; 449306; Antibiotic therapy dose selection.
DR PharmGKB; PA30665; -.
DR VEuPathDB; HostDB:ENSG00000165471; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154368; -.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; P11226; -.
DR OMA; CAKFQAS; -.
DR OrthoDB; 1222552at2759; -.
DR PhylomeDB; P11226; -.
DR TreeFam; TF330481; -.
DR PathwayCommons; P11226; -.
DR Reactome; R-HSA-166662; Lectin pathway of complement activation.
DR Reactome; R-HSA-166663; Initial triggering of complement.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; P11226; -.
DR SIGNOR; P11226; -.
DR BioGRID-ORCS; 4153; 8 hits in 1070 CRISPR screens.
DR EvolutionaryTrace; P11226; -.
DR GeneWiki; Mannan-binding_lectin; -.
DR GenomeRNAi; 4153; -.
DR Pharos; P11226; Tbio.
DR PRO; PR:P11226; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P11226; protein.
DR Bgee; ENSG00000165471; Expressed in right lobe of liver and 15 other tissues.
DR Genevisible; P11226; HS.
DR GO; GO:0009986; C:cell surface; TAS:BHF-UCL.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IPI:ComplexPortal.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005537; F:mannose binding; IDA:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0006953; P:acute-phase response; TAS:BHF-UCL.
DR GO; GO:0140374; P:antiviral innate immune response; IDA:UniProtKB.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IDA:ComplexPortal.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0001867; P:complement activation, lectin pathway; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; TAS:BHF-UCL.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:MGI.
DR GO; GO:0045087; P:innate immune response; IDA:BHF-UCL.
DR GO; GO:0051873; P:killing by host of symbiont cells; IEA:Ensembl.
DR GO; GO:0048525; P:negative regulation of viral process; IDA:BHF-UCL.
DR GO; GO:0008228; P:opsonization; TAS:BHF-UCL.
DR GO; GO:1903028; P:positive regulation of opsonization; IDA:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
DR GO; GO:0006979; P:response to oxidative stress; NAS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Coiled coil; Collagen;
KW Complement activation lectin pathway; Complement pathway;
KW Direct protein sequencing; Disulfide bond; Hydroxylation; Immunity;
KW Innate immunity; Lectin; Mannose-binding; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:7982896"
FT CHAIN 21..248
FT /note="Mannose-binding protein C"
FT /id="PRO_0000017401"
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:0000269|PubMed:7634089"
FT MOD_RES 47
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7982896"
FT MOD_RES 73
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7982896"
FT MOD_RES 79
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7982896"
FT MOD_RES 82
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7982896"
FT MOD_RES 88
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:7982896"
FT DISULFID 155..244
FT DISULFID 222..236
FT VARIANT 24
FT /note="T -> A (in Chinese)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_013294"
FT VARIANT 52
FT /note="R -> C (in 0.05% of European and African
FT populations; dbSNP:rs5030737)"
FT /evidence="ECO:0000269|PubMed:10447262,
FT ECO:0000269|PubMed:15994813, ECO:0000269|PubMed:9743385"
FT /id="VAR_008543"
FT VARIANT 54
FT /note="G -> D (associated with low serum mannose-binding
FT protein (MBP) concentrations and recurrent infections;
FT dbSNP:rs1800450)"
FT /evidence="ECO:0000269|PubMed:10447262,
FT ECO:0000269|PubMed:12175909, ECO:0000269|PubMed:1303250,
FT ECO:0000269|PubMed:1304173, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15994813, ECO:0000269|PubMed:1675710,
FT ECO:0000269|PubMed:9743385"
FT /id="VAR_004182"
FT VARIANT 57
FT /note="G -> E (associated with low serum mannose-binding
FT protein (MBP) concentrations; associated with protection
FT against tuberculosis caused by Mycobacterium africanum;
FT dbSNP:rs1800451)"
FT /evidence="ECO:0000269|PubMed:10447262,
FT ECO:0000269|PubMed:1304173, ECO:0000269|PubMed:15994813,
FT ECO:0000269|PubMed:21695215, ECO:0000269|PubMed:9743385"
FT /id="VAR_004183"
FT VARIANT 214
FT /note="N -> Y (in dbSNP:rs12260094)"
FT /id="VAR_050119"
FT HELIX 110..129
FT /evidence="ECO:0007829|PDB:1HUP"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:1HUP"
FT STRAND 137..147
FT /evidence="ECO:0007829|PDB:1HUP"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:1HUP"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:1HUP"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:1HUP"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1HUP"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1HUP"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1HUP"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:1HUP"
FT STRAND 238..247
FT /evidence="ECO:0007829|PDB:1HUP"
SQ SEQUENCE 248 AA; 26144 MW; C1F2AAED46D0F774 CRC64;
MSLFPSLPLL LLSMVAASYS ETVTCEDAQK TCPAVIACSS PGINGFPGKD GRDGTKGEKG
EPGQGLRGLQ GPPGKLGPPG NPGPSGSPGP KGQKGDPGKS PDGDSSLAAS ERKALQTEMA
RIKKWLTFSL GKQVGNKFFL TNGEIMTFEK VKALCVKFQA SVATPRNAAE NGAIQNLIKE
EAFLGITDEK TEGQFVDLTG NRLTYTNWNE GEPNNAGSDE DCVLLLKNGQ WNDVPCSTSH
LAVCEFPI
