MBL1_MOUSE
ID MBL1_MOUSE Reviewed; 239 AA.
AC P39039; Q0P6H1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Mannose-binding protein A;
DE Short=MBP-A {ECO:0000303|PubMed:1712818};
DE AltName: Full=Mannan-binding protein;
DE AltName: Full=Ra-reactive factor polysaccharide-binding component p28B;
DE Short=RaRF p28B;
DE Flags: Precursor;
GN Name=Mbl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=CBA/J; TISSUE=Liver;
RX PubMed=1712818;
RA Sastry K., Zahedi K., Lelias J.M., Whitehead A.S., Ezekowitz R.A.;
RT "Molecular characterization of the mouse mannose-binding proteins. The
RT mannose-binding protein A but not C is an acute phase reactant.";
RL J. Immunol. 147:692-697(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 19-35, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=1637828; DOI=10.1021/bi00145a012;
RA Kuge S., Ihara S., Watanabe E., Watanabe M., Takishima K., Suga T.,
RA Mamiya G., Kawakami M.;
RT "cDNAs and deduced amino acid sequences of subunits in the binding
RT component of mouse bactericidal factor, Ra-reactive factor: similarity to
RT mannose-binding proteins.";
RL Biochemistry 31:6943-6950(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=7766991; DOI=10.1007/bf00303252;
RA Sastry R., Wang J.S., Brown D.C., Ezekowitz R.A., Tauber A.I., Sastry K.N.;
RT "Characterization of murine mannose-binding protein genes Mbl1 and Mbl2
RT reveals features common to other collectin genes.";
RL Mamm. Genome 6:103-110(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND SUBUNIT.
RX PubMed=25419660; DOI=10.1371/journal.pone.0113498;
RA Risteli M., Ruotsalainen H., Bergmann U., Venkatraman Girija U., Wallis R.,
RA Myllylae R.;
RT "Lysyl hydroxylase 3 modifies lysine residues to facilitate oligomerization
RT of mannan-binding lectin.";
RL PLoS ONE 9:E113498-E113498(2014).
CC -!- FUNCTION: Calcium-dependent lectin. Plays a role in the innate immune
CC response by binding mannose, fucose and N-acetylglucosamine moieties on
CC different microorganisms and mediating activation of the lectin
CC complement pathway (By similarity). Binds to late apoptotic cells, as
CC well as to apoptotic blebs and to necrotic cells, but not to early
CC apoptotic cells, facilitating their uptake by macrophages (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P19999}.
CC -!- SUBUNIT: Homotrimer (By similarity). Forms higher oligomeric complexes
CC formed by the association of two, three or more homotrimers
CC (PubMed:25419660). Oligomerization occurs in the endoplasmic reticulum
CC (By similarity). Interacts with MASP1 and MASP2 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P19999,
CC ECO:0000269|PubMed:25419660}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1637828,
CC ECO:0000269|PubMed:25419660}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P39039-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P39039-2; Sequence=VSP_038477;
CC -!- TISSUE SPECIFICITY: Detected in liver and blood serum (at protein
CC level) (PubMed:1637828, PubMed:25419660). Detected in liver
CC (PubMed:1712818). {ECO:0000269|PubMed:1637828,
CC ECO:0000269|PubMed:1712818, ECO:0000269|PubMed:25419660}.
CC -!- DOMAIN: The helical collagen-like domains from three protein chains
CC assemble into a coiled coil and mediate trimerization.
CC {ECO:0000250|UniProtKB:P19999}.
CC -!- PTM: Hydroxylated on lysine and proline residues within the collagen-
CC like domain. {ECO:0000250|UniProtKB:P19999}.
CC -!- PTM: O-glycosylated. O-linked glycans on hydroxylysine residues consist
CC of Glc-Gal disaccharides bound to the oxygen atom of post-
CC translationally added hydroxyl groups. {ECO:0000250|UniProtKB:P19999}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to competing donor splice site.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Mannose-binding protein A;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_168";
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DR EMBL; S42292; AAB19342.1; -; mRNA.
DR EMBL; D11441; BAA02006.1; -; mRNA.
DR EMBL; U09010; AAA82009.1; -; Genomic_DNA.
DR EMBL; U09007; AAA82009.1; JOINED; Genomic_DNA.
DR EMBL; U09008; AAA82009.1; JOINED; Genomic_DNA.
DR EMBL; U09009; AAA82009.1; JOINED; Genomic_DNA.
DR EMBL; BC012245; AAH12245.1; -; mRNA.
DR EMBL; BC021762; AAH21762.1; -; mRNA.
DR CCDS; CCDS26961.1; -. [P39039-1]
DR PIR; A46466; LNMSMA.
DR RefSeq; NP_034905.1; NM_010775.2. [P39039-1]
DR RefSeq; XP_006518732.1; XM_006518669.3. [P39039-1]
DR RefSeq; XP_017171395.1; XM_017315906.1.
DR AlphaFoldDB; P39039; -.
DR SMR; P39039; -.
DR STRING; 10090.ENSMUSP00000048765; -.
DR GlyGen; P39039; 4 sites.
DR iPTMnet; P39039; -.
DR PhosphoSitePlus; P39039; -.
DR CPTAC; non-CPTAC-3725; -.
DR jPOST; P39039; -.
DR MaxQB; P39039; -.
DR PaxDb; P39039; -.
DR PeptideAtlas; P39039; -.
DR PRIDE; P39039; -.
DR ProteomicsDB; 295803; -. [P39039-1]
DR ProteomicsDB; 295804; -. [P39039-2]
DR DNASU; 17194; -.
DR Ensembl; ENSMUST00000225792; ENSMUSP00000153147; ENSMUSG00000037780. [P39039-1]
DR GeneID; 17194; -.
DR KEGG; mmu:17194; -.
DR UCSC; uc007tcp.1; mouse. [P39039-1]
DR CTD; 17194; -.
DR MGI; MGI:96923; Mbl1.
DR VEuPathDB; HostDB:ENSMUSG00000037780; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154368; -.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; P39039; -.
DR OMA; TCSVVAC; -.
DR OrthoDB; 1222552at2759; -.
DR PhylomeDB; P39039; -.
DR TreeFam; TF330481; -.
DR BioGRID-ORCS; 17194; 1 hit in 71 CRISPR screens.
DR PRO; PR:P39039; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P39039; protein.
DR Bgee; ENSMUSG00000037780; Expressed in left lobe of liver and 20 other tissues.
DR ExpressionAtlas; P39039; baseline and differential.
DR Genevisible; P39039; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0120153; F:calcium-dependent carbohydrate binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005537; F:mannose binding; ISS:UniProtKB.
DR GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISO:MGI.
DR GO; GO:0030247; F:polysaccharide binding; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0001867; P:complement activation, lectin pathway; IDA:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IGI:MGI.
DR GO; GO:0051873; P:killing by host of symbiont cells; IGI:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IGI:MGI.
DR GO; GO:0070207; P:protein homotrimerization; ISS:UniProtKB.
DR GO; GO:0043129; P:surfactant homeostasis; IBA:GO_Central.
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; IPR042129; Mannose-binding_protein_A.
DR PANTHER; PTHR24024:SF35; PTHR24024:SF35; 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 Alternative splicing; Calcium; Collagen;
KW Complement activation lectin pathway; Complement pathway;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydroxylation;
KW Immunity; Innate immunity; Lectin; Mannose-binding; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:1637828"
FT CHAIN 19..239
FT /note="Mannose-binding protein A"
FT /id="PRO_0000017413"
FT DOMAIN 37..89
FT /note="Collagen-like"
FT DOMAIN 144..239
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 35..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..211
FT /note="Calcium-dependent carbohydrate binding"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 44
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 45
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 48
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 51
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 62
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 68
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 74
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 79
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 80
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 83
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT CARBOHYD 45
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT CARBOHYD 48
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT CARBOHYD 80
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT CARBOHYD 83
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT DISULFID 146..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 213..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 1..98
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038477"
SQ SEQUENCE 239 AA; 25396 MW; D222F1A748D424D9 CRC64;
MLLLPLLPVL LCVVSVSSSG SQTCEDTLKT CSVIACGRDG RDGPKGEKGE PGQGLRGLQG
PPGKLGPPGS VGSPGSPGPK GQKGDHGDNR AIEEKLANME AEIRILKSKL QLTNKLHAFS
MGKKSGKKLF VTNHEKMPFS KVKSLCTELQ GTVAIPRNAE ENKAIQEVAT GIAFLGITDE
ATEGQFMYVT GGRLTYSNWK KDEPNNHGSG EDCVIILDNG LWNDISCQAS FKAVCEFPA
