MBL2_MOUSE
ID MBL2_MOUSE Reviewed; 244 AA.
AC P41317;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Mannose-binding protein C;
DE Short=MBP-C;
DE AltName: Full=Mannan-binding protein;
DE AltName: Full=RA-reactive factor P28A subunit;
DE Short=RARF/P28A;
DE Flags: Precursor;
GN Name=Mbl2;
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.
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.
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 [3]
RP NUCLEOTIDE SEQUENCE.
RA Kuge S., Ihara S., Watanabe E., Watanabe M., Takishima K., Suga T.,
RA Mamaiya G., Kawakami M.;
RL Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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=Brown adipose tissue, Heart, Liver, Lung, and Testis;
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).
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}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Mannose-binding protein C;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_169";
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DR EMBL; S42294; AAB19343.1; -; mRNA.
DR EMBL; U09016; AAA82010.1; -; Genomic_DNA.
DR EMBL; U09013; AAA82010.1; JOINED; Genomic_DNA.
DR EMBL; U09014; AAA82010.1; JOINED; Genomic_DNA.
DR EMBL; U09015; AAA82010.1; JOINED; Genomic_DNA.
DR EMBL; D11440; BAA02005.1; -; mRNA.
DR EMBL; BC010760; AAH10760.1; -; mRNA.
DR CCDS; CCDS29742.1; -.
DR PIR; I48651; LNMSMC.
DR RefSeq; NP_034906.1; NM_010776.1.
DR RefSeq; XP_006526793.1; XM_006526730.1.
DR AlphaFoldDB; P41317; -.
DR SMR; P41317; -.
DR BioGRID; 201335; 2.
DR STRING; 10090.ENSMUSP00000025797; -.
DR GlyGen; P41317; 1 site.
DR iPTMnet; P41317; -.
DR PhosphoSitePlus; P41317; -.
DR CPTAC; non-CPTAC-3840; -.
DR jPOST; P41317; -.
DR PaxDb; P41317; -.
DR PeptideAtlas; P41317; -.
DR PRIDE; P41317; -.
DR ProteomicsDB; 292274; -.
DR Antibodypedia; 693; 759 antibodies from 40 providers.
DR DNASU; 17195; -.
DR Ensembl; ENSMUST00000025797; ENSMUSP00000025797; ENSMUSG00000024863.
DR GeneID; 17195; -.
DR KEGG; mmu:17195; -.
DR UCSC; uc008hel.1; mouse.
DR CTD; 4153; -.
DR MGI; MGI:96924; Mbl2.
DR VEuPathDB; HostDB:ENSMUSG00000024863; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154368; -.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; P41317; -.
DR OMA; CAKFQAS; -.
DR OrthoDB; 1222552at2759; -.
DR PhylomeDB; P41317; -.
DR TreeFam; TF330481; -.
DR BioGRID-ORCS; 17195; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Mbl2; mouse.
DR PRO; PR:P41317; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P41317; protein.
DR Bgee; ENSMUSG00000024863; Expressed in left lobe of liver and 41 other tissues.
DR ExpressionAtlas; P41317; baseline and differential.
DR Genevisible; P41317; MM.
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:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:1905370; C:serine-type endopeptidase complex; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0140374; P:antiviral innate immune response; ISO:MGI.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; 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:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0051873; P:killing by host of symbiont cells; IGI:MGI.
DR GO; GO:0048525; P:negative regulation of viral process; ISO:MGI.
DR GO; GO:1903028; P:positive regulation of opsonization; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IGI:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
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; 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 Calcium; Coiled coil; Collagen; Complement activation lectin pathway;
KW Complement pathway; Disulfide bond; Glycoprotein; Hydroxylation; Immunity;
KW Innate immunity; Lectin; Mannose-binding; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..244
FT /note="Mannose-binding protein C"
FT /id="PRO_0000017405"
FT DOMAIN 38..96
FT /note="Collagen-like"
FT DOMAIN 129..241
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 40..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 108..126
FT /evidence="ECO:0000250"
FT MOD_RES 43
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 58
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 69
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 78
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 81
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 34
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 151..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 218..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 3
FT /note="I -> L (in Ref. 1; AAB19343)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="V -> A (in Ref. 1; AAB19343)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 25957 MW; 49AE84E2290DEB0A CRC64;
MSIFTSFLLL CVVTVVYAET LTEGVQNSCP VVTCSSPGLN GFPGKDGRDG AKGEKGEPGQ
GLRGLQGPPG KVGPTGPPGN PGLKGAVGPK GDRGDRAEFD TSEIDSEIAA LRSELRALRN
WVLFSLSEKV GKKYFVSSVK KMSLDRVKAL CSEFQGSVAT PRNAEENSAI QKVAKDIAYL
GITDVRVEGS FEDLTGNRVR YTNWNDGEPN NTGDGEDCVV ILGNGKWNDV PCSDSFLAIC
EFSD
