Mbl1
entrez
24548
canonical
uniprot
P19999
canonical
ensembl
ENSRNOG00000011706
resolver
ensembl
ENSRNOG00055009165
resolver
ensembl
ENSRNOG00060010036
resolver
ensembl
ENSRNOG00065020393
resolver
ensp
ENSRNOP00000015723
resolver
ensp
ENSRNOP00055012421
resolver
ensp
ENSRNOP00060013245
resolver
ensp
ENSRNOP00065027602
resolver
enst
ENSRNOT00000015723
resolver
enst
ENSRNOT00055015506
resolver
enst
ENSRNOT00060016970
resolver
enst
ENSRNOT00065034454
resolver
genesymbol
Mbl1
resolver
uniprot_entry
MBL1_RAT
resolver
amino_acid_sequence
MLLLPLLVLLCVVSVSSSGSQTCEETLKTCSVIACGRDGRDGPKGEKGEPGQGLRGLQGPPGKLGPPGSVGAPGSQGPKGQKGDRGDSRAIEVKLANMEAEINTLKSKLELTNKLHAFSMGKKSGKKFFVTNHERMPFSKVKALCSELRGTVAIPRNAEENKAIQEVAKTSAFLGITDEVTEGQFMYVTGGRLTYSNWKKDEPNDHGSGEDCVTIVDNGLWNDISCQASHTAVCEFPA
uniprot
proteins
function
FUNCTION: Calcium-dependent lectin (PubMed:11850428, PubMed:1436090, PubMed:9033386). Plays a role in the innate immune response by binding mannose, fucose and N-acetylglucosamine moieties on different microorganisms and mediating activation of the lectin complement pathway (PubMed:3584121). Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages (By similarity). {ECO:0000250, ECO:0000269|PubMed:11850428, ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:3584121, ECO:0000269|PubMed:9033386}.
uniprot
proteins
mass_dalton
25308
uniprot
proteins
mutagenesis
MUTAGEN 40; /note="R->C: Prevents higher-order oligomer assembly. Slight reduction in secretion rate."; /evidence="ECO:0000269|PubMed:10903744"; MUTAGEN 42; /note="G->E: Disrupts homotrimer formation. 5-fold reduction in secretion rate. Prevents K-44 hydroxylation and glycosylation. 10-fold decrease in complement activation."; /evidence="ECO:0000269|PubMed:10903744"; MUTAGEN 44; /note="K->R: No effect on secretion rate, nor on homooligomer formation. 3-fold reduction in secretion rate; when associated with R-47. Prevents higher-order oligomer assembly; when associated with R-47. 10-fold decrease in complement activation; when associated with R-47."; /evidence="ECO:0000269|PubMed:10903744"; MUTAGEN 45; /note="G->D: Disrupts homotrimer formation. 5-fold reduction in secretion rate. Prevents K-47 hydroxylation and glycosylation."; /evidence="ECO:0000269|PubMed:10903744"; MUTAGEN 47; /note="K->R: No effect on secretion rate, nor on homooligomer formation. 3-fold reduction in secretion rate; when associated with R-44. Prevents higher-order oligomer assembly; when associated with R-44. 10-fold decrease in complement activation; when associated with R-44."; /evidence="ECO:0000269|PubMed:10903744"; MUTAGEN 228..230; /note="ASH->KKK: Changes carbohydrate binding specificity, leading to interaction with Lewis blood group antigens."; /evidence="ECO:0000269|PubMed:9033386
uniprot
proteins
post_translational_modification
PTM: Hydroxylated on lysine and proline residues within the collagen-like domain. {ECO:0000269|PubMed:10903744, ECO:0000269|PubMed:25419660}.; PTM: O-glycosylated. O-linked glycans on hydroxylysine residues consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. {ECO:0000269|PubMed:10903744, ECO:0000269|PubMed:25419660}.
uniprot
proteins
pubmed
10903744
uniprot
proteins
pubmed
10913141
uniprot
proteins
pubmed
11850428
uniprot
proteins
pubmed
1436090
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1721241
uniprot
proteins
pubmed
25419660
uniprot
proteins
pubmed
3009480
uniprot
proteins
pubmed
3029088
uniprot
proteins
pubmed
3584121
uniprot
proteins
pubmed
7704532
uniprot
proteins
pubmed
9033386
uniprot
proteins
pubmed
9922165
uniprot
proteins
sequence_length
238
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10903744, ECO:0000269|PubMed:25419660, ECO:0000269|PubMed:3584121}. Note=According to PubMed:10903744, long retention times in the endoplasmic reticulum and the Golgi apparatus that have been observed in former studies may reflect the abnormal physiology of the hepatoma cells used.
uniprot
proteins