MBL1_RAT
ID MBL1_RAT Reviewed; 238 AA.
AC P19999;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Mannose-binding protein A;
DE Short=MBP-A {ECO:0000303|PubMed:3009480};
DE AltName: Full=Mannan-binding protein;
DE Flags: Precursor;
GN Name=Mbl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=3009480; DOI=10.1016/s0021-9258(19)62698-0;
RA Drickamer K., Dordal M.S., Reynolds L.;
RT "Mannose-binding proteins isolated from rat liver contain carbohydrate-
RT recognition domains linked to collagenous tails. Complete primary
RT structures and homology with pulmonary surfactant apoprotein.";
RL J. Biol. Chem. 261:6878-6887(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=3029088; DOI=10.1016/s0021-9258(18)61545-5;
RA Drickamer K., McCreary V.;
RT "Exon structure of a mannose-binding protein gene reflects its evolutionary
RT relationship to the asialoglycoprotein receptor and nonfibrillar
RT collagens.";
RL J. Biol. Chem. 262:2582-2589(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [4]
RP PROTEIN SEQUENCE OF 18-42, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=3584121; DOI=10.1016/s0021-9258(18)47587-4;
RA Ikeda K., Sannoh T., Kawasaki N., Kawasaki T., Yamashina I.;
RT "Serum lectin with known structure activates complement through the
RT classical pathway.";
RL J. Biol. Chem. 262:7451-7454(1987).
RN [5]
RP INTERACTION WITH MASP1 AND MASP2.
RC TISSUE=Liver;
RX PubMed=10913141; DOI=10.1074/jbc.m004030200;
RA Wallis R., Dodd R.B.;
RT "Interaction of mannose-binding protein with associated serine proteases:
RT effects of naturally occurring mutations.";
RL J. Biol. Chem. 275:30962-30969(2000).
RN [6]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, OLIGOMERIZATION, MUTAGENESIS OF
RP ARG-40; GLY-42; LYS-44; GLY-45 AND LYS-47, AND HYDROXYLATION AT LYS-44 AND
RP LYS-47.
RX PubMed=10903744; DOI=10.4049/jimmunol.165.3.1403;
RA Heise C.T., Nicholls J.R., Leamy C.E., Wallis R.;
RT "Impaired secretion of rat mannose-binding protein resulting from mutations
RT in the collagen-like domain.";
RL J. Immunol. 165:1403-1409(2000).
RN [7]
RP SUBUNIT, SUBCELLULAR LOCATION, HYDROXYLATION AT LYS-44; LYS-47; PRO-50;
RP LYS-79 AND LYS-82, GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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).
RN [8] {ECO:0007744|PDB:1MSB}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 124-238, AND DISULFIDE BONDS.
RX PubMed=1721241; DOI=10.1126/science.1721241;
RA Weis W.I., Kahn R., Fourme R., Drickamer K., Hendrickson W.A.;
RT "Structure of the calcium-dependent lectin domain from a rat mannose-
RT binding protein determined by MAD phasing.";
RL Science 254:1608-1615(1991).
RN [9] {ECO:0007744|PDB:2MSB}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 124-238 IN COMPLEX WITH CALCIUM
RP AND CARBOHYDRATE, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=1436090; DOI=10.1038/360127a0;
RA Weis W.I., Drickamer K., Hendrickson W.A.;
RT "Structure of a C-type mannose-binding protein complexed with an
RT oligosaccharide.";
RL Nature 360:127-134(1992).
RN [10] {ECO:0007744|PDB:1RTM}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 90-238 IN COMPLEX WITH CALCIUM,
RP SUBUNIT, DOMAIN, AND DISULFIDE BONDS.
RX PubMed=7704532; DOI=10.1016/s0969-2126(94)00124-3;
RA Weis W.I., Drickamer K.;
RT "Trimeric structure of a C-type mannose-binding protein.";
RL Structure 2:1227-1240(1994).
RN [11] {ECO:0007744|PDB:1KMB, ECO:0007744|PDB:2KMB, ECO:0007744|PDB:3KMB, ECO:0007744|PDB:4KMB}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 90-238 OF MUTANT 228-LYS--LYS-230
RP IN COMPLEXES WITH CALCIUM AND CARBOHYDRATE, FUNCTION, SUBUNIT, DOMAIN,
RP DISULFIDE BONDS, AND MUTAGENESIS OF 228-ALA--HIS-230.
RX PubMed=9033386; DOI=10.1021/bi962564e;
RA Ng K.K., Weis W.I.;
RT "Structure of a selectin-like mutant of mannose-binding protein complexed
RT with sialylated and sulfated Lewis(x) oligosaccharides.";
RL Biochemistry 36:979-988(1997).
RN [12] {ECO:0007744|PDB:1BUU}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 75-238, AND DISULFIDE BONDS.
RX PubMed=9922165; DOI=10.1021/bi981972a;
RA Ng K.K.-S., Park-Snyder S., Weis W.I.;
RT "Ca2+-dependent structural changes in C-type mannose-binding proteins.";
RL Biochemistry 37:17965-17976(1998).
RN [13] {ECO:0007744|PDB:1KWT, ECO:0007744|PDB:1KWU, ECO:0007744|PDB:1KWV, ECO:0007744|PDB:1KWW, ECO:0007744|PDB:1KWX, ECO:0007744|PDB:1KWY, ECO:0007744|PDB:1KWZ, ECO:0007744|PDB:1KX0, ECO:0007744|PDB:1KX1}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 90-238 IN COMPLEXES WITH CALCIUM
RP AND CARBOHYDRATE, FUNCTION, SUBUNIT, DOMAIN, AND DISULFIDE BONDS.
RX PubMed=11850428; DOI=10.1074/jbc.m200493200;
RA Ng K.K., Kolatkar A.R., Park-Snyder S., Feinberg H., Clark D.A.,
RA Drickamer K., Weis W.I.;
RT "Orientation of bound ligands in mannose-binding proteins. Implications for
RT multivalent ligand recognition.";
RL J. Biol. Chem. 277:16088-16095(2002).
CC -!- FUNCTION: Calcium-dependent lectin (PubMed:1436090, PubMed:9033386,
CC PubMed:11850428). Plays a role in the innate immune response by binding
CC mannose, fucose and N-acetylglucosamine moieties on different
CC microorganisms and mediating activation of the lectin complement
CC pathway (PubMed:3584121). Binds to late apoptotic cells, as well as to
CC apoptotic blebs and to necrotic cells, but not to early apoptotic
CC cells, facilitating their uptake by macrophages (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:11850428, ECO:0000269|PubMed:1436090,
CC ECO:0000269|PubMed:3584121, ECO:0000269|PubMed:9033386}.
CC -!- SUBUNIT: Homotrimer (PubMed:7704532, PubMed:9033386, PubMed:11850428,
CC PubMed:25419660). Forms higher oligomeric complexes formed by the
CC association of two, three or more homotrimers (PubMed:10903744,
CC PubMed:25419660). Oligomerization occurs in the endoplasmic reticulum
CC (By similarity). Interacts with MASP1 and MASP2 (PubMed:10913141).
CC {ECO:0000250, ECO:0000269|PubMed:10903744, ECO:0000269|PubMed:10913141,
CC ECO:0000269|PubMed:11850428, ECO:0000269|PubMed:25419660,
CC ECO:0000269|PubMed:7704532, ECO:0000269|PubMed:9033386}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10903744,
CC ECO:0000269|PubMed:25419660, ECO:0000269|PubMed:3584121}.
CC Note=According to PubMed:10903744, long retention times in the
CC endoplasmic reticulum and the Golgi apparatus that have been observed
CC in former studies may reflect the abnormal physiology of the hepatoma
CC cells used.
CC -!- TISSUE SPECIFICITY: Detected in blood serum (at protein level).
CC {ECO:0000269|PubMed:3584121}.
CC -!- DOMAIN: The helical collagen-like domains from three protein chains
CC assemble into a coiled coil and mediate trimerization.
CC {ECO:0000269|PubMed:11850428, ECO:0000269|PubMed:7704532,
CC ECO:0000269|PubMed:9033386}.
CC -!- PTM: Hydroxylated on lysine and proline residues within the collagen-
CC like domain. {ECO:0000269|PubMed:10903744,
CC ECO:0000269|PubMed:25419660}.
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:0000269|PubMed:10903744,
CC ECO:0000269|PubMed:25419660}.
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_rat_Ctlect_00135";
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DR EMBL; M14105; AAA98781.1; -; Genomic_DNA.
DR EMBL; M14104; AAA98781.1; JOINED; Genomic_DNA.
DR EMBL; BC088159; AAH88159.1; -; mRNA.
DR PIR; B24791; LNRTMA.
DR RefSeq; NP_036731.2; NM_012599.2.
DR PDB; 1AFA; X-ray; 2.00 A; 1/2/3=90-238.
DR PDB; 1AFB; X-ray; 1.90 A; 1/2/3=90-238.
DR PDB; 1AFD; X-ray; 2.00 A; 1/2/3=90-238.
DR PDB; 1BCH; X-ray; 2.00 A; 1/2/3=90-238.
DR PDB; 1BCJ; X-ray; 2.10 A; 1/2/3=90-238.
DR PDB; 1BUU; X-ray; 1.90 A; A=75-238.
DR PDB; 1FIF; X-ray; 1.95 A; A/B/C=90-238.
DR PDB; 1FIH; X-ray; 1.95 A; A/B/C=90-238.
DR PDB; 1KMB; X-ray; 2.10 A; 1/2/3=90-238.
DR PDB; 1KWT; X-ray; 1.95 A; A/B/C=90-238.
DR PDB; 1KWU; X-ray; 1.95 A; A/B/C=90-238.
DR PDB; 1KWV; X-ray; 2.00 A; A/B/C=90-238.
DR PDB; 1KWW; X-ray; 1.90 A; A/B/C=90-238.
DR PDB; 1KWX; X-ray; 2.00 A; A/B/C=90-238.
DR PDB; 1KWY; X-ray; 2.00 A; A/B/C=90-238.
DR PDB; 1KWZ; X-ray; 1.90 A; A/B/C=90-238.
DR PDB; 1KX0; X-ray; 2.00 A; A/B/C=90-238.
DR PDB; 1KX1; X-ray; 2.80 A; A/B/C/D/E/F=90-238.
DR PDB; 1MSB; X-ray; 2.30 A; A/B=124-238.
DR PDB; 1RTM; X-ray; 1.80 A; 1/2/3=90-238.
DR PDB; 1YTT; X-ray; 1.80 A; A/B=124-238.
DR PDB; 2KMB; X-ray; 2.00 A; 1/2/3=90-238.
DR PDB; 2MSB; X-ray; 1.70 A; A/B=124-238.
DR PDB; 3KMB; X-ray; 1.95 A; 1/2/3=90-238.
DR PDB; 4KMB; X-ray; 2.00 A; 1/2/3=90-238.
DR PDBsum; 1AFA; -.
DR PDBsum; 1AFB; -.
DR PDBsum; 1AFD; -.
DR PDBsum; 1BCH; -.
DR PDBsum; 1BCJ; -.
DR PDBsum; 1BUU; -.
DR PDBsum; 1FIF; -.
DR PDBsum; 1FIH; -.
DR PDBsum; 1KMB; -.
DR PDBsum; 1KWT; -.
DR PDBsum; 1KWU; -.
DR PDBsum; 1KWV; -.
DR PDBsum; 1KWW; -.
DR PDBsum; 1KWX; -.
DR PDBsum; 1KWY; -.
DR PDBsum; 1KWZ; -.
DR PDBsum; 1KX0; -.
DR PDBsum; 1KX1; -.
DR PDBsum; 1MSB; -.
DR PDBsum; 1RTM; -.
DR PDBsum; 1YTT; -.
DR PDBsum; 2KMB; -.
DR PDBsum; 2MSB; -.
DR PDBsum; 3KMB; -.
DR PDBsum; 4KMB; -.
DR AlphaFoldDB; P19999; -.
DR SMR; P19999; -.
DR STRING; 10116.ENSRNOP00000015723; -.
DR UniLectin; P19999; -.
DR GlyGen; P19999; 4 sites.
DR PaxDb; P19999; -.
DR Ensembl; ENSRNOT00000015723; ENSRNOP00000015723; ENSRNOG00000011706.
DR GeneID; 24548; -.
DR KEGG; rno:24548; -.
DR UCSC; RGD:3055; rat.
DR CTD; 17194; -.
DR RGD; 3055; Mbl1.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154368; -.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; P19999; -.
DR OMA; TCSVVAC; -.
DR OrthoDB; 1222552at2759; -.
DR PhylomeDB; P19999; -.
DR TreeFam; TF330481; -.
DR EvolutionaryTrace; P19999; -.
DR PRO; PR:P19999; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000011706; Expressed in liver and 5 other tissues.
DR Genevisible; P19999; RN.
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:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0120153; F:calcium-dependent carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR GO; GO:0070492; F:oligosaccharide binding; IDA:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:RGD.
DR GO; GO:0030247; F:polysaccharide binding; IDA:RGD.
DR GO; GO:0002020; F:protease binding; IDA:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0001867; P:complement activation, lectin pathway; IDA:RGD.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:RGD.
DR GO; GO:0051873; P:killing by host of symbiont cells; ISO:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:RGD.
DR GO; GO:0070207; P:protein homotrimerization; IDA: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; 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 3D-structure; Calcium; Collagen; Complement activation lectin pathway;
KW Complement pathway; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydroxylation; Immunity; Innate immunity; Lectin;
KW Mannose-binding; Metal-binding; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:3584121"
FT CHAIN 18..238
FT /note="Mannose-binding protein A"
FT /id="PRO_0000017414"
FT DOMAIN 39..88
FT /note="Collagen-like"
FT DOMAIN 143..238
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 38..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..210
FT /note="Calcium-dependent carbohydrate binding"
FT /evidence="ECO:0000269|PubMed:11850428,
FT ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:9033386"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11850428,
FT ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:7704532,
FT ECO:0000269|PubMed:9033386, ECO:0007744|PDB:1AFA,
FT ECO:0007744|PDB:1AFB, ECO:0007744|PDB:1AFD,
FT ECO:0007744|PDB:1BCH, ECO:0007744|PDB:1BCJ,
FT ECO:0007744|PDB:1FIF, ECO:0007744|PDB:1FIH,
FT ECO:0007744|PDB:1KMB, ECO:0007744|PDB:1KWT,
FT ECO:0007744|PDB:1KWU, ECO:0007744|PDB:1KWV,
FT ECO:0007744|PDB:1KWW, ECO:0007744|PDB:1KWX,
FT ECO:0007744|PDB:1KWY, ECO:0007744|PDB:1KWZ,
FT ECO:0007744|PDB:1KX0, ECO:0007744|PDB:1KX1,
FT ECO:0007744|PDB:1RTM, ECO:0007744|PDB:2KMB,
FT ECO:0007744|PDB:2MSB, ECO:0007744|PDB:3KMB,
FT ECO:0007744|PDB:4KMB"
FT BINDING 182
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11850428,
FT ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:7704532,
FT ECO:0000269|PubMed:9033386, ECO:0007744|PDB:1AFA,
FT ECO:0007744|PDB:1AFB, ECO:0007744|PDB:1AFD,
FT ECO:0007744|PDB:1BCH, ECO:0007744|PDB:1BCJ,
FT ECO:0007744|PDB:1FIF, ECO:0007744|PDB:1FIH,
FT ECO:0007744|PDB:1KMB, ECO:0007744|PDB:1KWT,
FT ECO:0007744|PDB:1KWU, ECO:0007744|PDB:1KWV,
FT ECO:0007744|PDB:1KWW, ECO:0007744|PDB:1KWX,
FT ECO:0007744|PDB:1KWY, ECO:0007744|PDB:1KWZ,
FT ECO:0007744|PDB:1KX0, ECO:0007744|PDB:1KX1,
FT ECO:0007744|PDB:1RTM, ECO:0007744|PDB:2KMB,
FT ECO:0007744|PDB:2MSB, ECO:0007744|PDB:3KMB,
FT ECO:0007744|PDB:4KMB"
FT BINDING 202
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11850428,
FT ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:7704532,
FT ECO:0000269|PubMed:9033386, ECO:0007744|PDB:1KMB,
FT ECO:0007744|PDB:1KWT, ECO:0007744|PDB:1KWU,
FT ECO:0007744|PDB:1KWV, ECO:0007744|PDB:1KWW,
FT ECO:0007744|PDB:1KWX, ECO:0007744|PDB:1KWY,
FT ECO:0007744|PDB:1KWZ, ECO:0007744|PDB:1KX0,
FT ECO:0007744|PDB:1KX1, ECO:0007744|PDB:1RTM,
FT ECO:0007744|PDB:2KMB, ECO:0007744|PDB:2MSB,
FT ECO:0007744|PDB:3KMB, ECO:0007744|PDB:4KMB"
FT BINDING 204
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11850428,
FT ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:7704532,
FT ECO:0000269|PubMed:9033386, ECO:0007744|PDB:1KMB,
FT ECO:0007744|PDB:1KWT, ECO:0007744|PDB:1KWU,
FT ECO:0007744|PDB:1KWV, ECO:0007744|PDB:1KWW,
FT ECO:0007744|PDB:1KWX, ECO:0007744|PDB:1KWY,
FT ECO:0007744|PDB:1KWZ, ECO:0007744|PDB:1KX0,
FT ECO:0007744|PDB:1KX1, ECO:0007744|PDB:1RTM,
FT ECO:0007744|PDB:2KMB, ECO:0007744|PDB:2MSB,
FT ECO:0007744|PDB:3KMB, ECO:0007744|PDB:4KMB"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11850428,
FT ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:7704532,
FT ECO:0000269|PubMed:9033386, ECO:0007744|PDB:1AFA,
FT ECO:0007744|PDB:1AFB, ECO:0007744|PDB:1AFD,
FT ECO:0007744|PDB:1BCH, ECO:0007744|PDB:1BCJ,
FT ECO:0007744|PDB:1FIF, ECO:0007744|PDB:1FIH,
FT ECO:0007744|PDB:1KMB, ECO:0007744|PDB:1KWT,
FT ECO:0007744|PDB:1KWU, ECO:0007744|PDB:1KWV,
FT ECO:0007744|PDB:1KWW, ECO:0007744|PDB:1KWX,
FT ECO:0007744|PDB:1KWY, ECO:0007744|PDB:1KWZ,
FT ECO:0007744|PDB:1KX0, ECO:0007744|PDB:1KX1,
FT ECO:0007744|PDB:1RTM, ECO:0007744|PDB:2KMB,
FT ECO:0007744|PDB:2MSB, ECO:0007744|PDB:3KMB,
FT ECO:0007744|PDB:4KMB"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11850428,
FT ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:7704532,
FT ECO:0000269|PubMed:9033386, ECO:0007744|PDB:1AFA,
FT ECO:0007744|PDB:1AFB, ECO:0007744|PDB:1AFD,
FT ECO:0007744|PDB:1BCH, ECO:0007744|PDB:1BCJ,
FT ECO:0007744|PDB:1FIF, ECO:0007744|PDB:1FIH,
FT ECO:0007744|PDB:1KMB, ECO:0007744|PDB:1KWT,
FT ECO:0007744|PDB:1KWU, ECO:0007744|PDB:1KWV,
FT ECO:0007744|PDB:1KWW, ECO:0007744|PDB:1KWX,
FT ECO:0007744|PDB:1KWY, ECO:0007744|PDB:1KWZ,
FT ECO:0007744|PDB:1KX0, ECO:0007744|PDB:1KX1,
FT ECO:0007744|PDB:1RTM, ECO:0007744|PDB:2KMB,
FT ECO:0007744|PDB:2MSB, ECO:0007744|PDB:3KMB,
FT ECO:0007744|PDB:4KMB"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11850428,
FT ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:7704532,
FT ECO:0000269|PubMed:9033386, ECO:0007744|PDB:1KMB,
FT ECO:0007744|PDB:1KWT, ECO:0007744|PDB:1KWU,
FT ECO:0007744|PDB:1KWV, ECO:0007744|PDB:1KWW,
FT ECO:0007744|PDB:1KWX, ECO:0007744|PDB:1KWY,
FT ECO:0007744|PDB:1KWZ, ECO:0007744|PDB:1KX0,
FT ECO:0007744|PDB:1KX1, ECO:0007744|PDB:1RTM,
FT ECO:0007744|PDB:2KMB, ECO:0007744|PDB:2MSB,
FT ECO:0007744|PDB:3KMB, ECO:0007744|PDB:4KMB"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11850428,
FT ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:7704532,
FT ECO:0000269|PubMed:9033386, ECO:0007744|PDB:1AFA,
FT ECO:0007744|PDB:1AFB, ECO:0007744|PDB:1AFD,
FT ECO:0007744|PDB:1BCH, ECO:0007744|PDB:1BCJ,
FT ECO:0007744|PDB:1FIF, ECO:0007744|PDB:1FIH,
FT ECO:0007744|PDB:1KMB, ECO:0007744|PDB:1KWT,
FT ECO:0007744|PDB:1KWU, ECO:0007744|PDB:1KWV,
FT ECO:0007744|PDB:1KWW, ECO:0007744|PDB:1KWX,
FT ECO:0007744|PDB:1KWY, ECO:0007744|PDB:1KWZ,
FT ECO:0007744|PDB:1KX0, ECO:0007744|PDB:1KX1,
FT ECO:0007744|PDB:1RTM, ECO:0007744|PDB:2KMB,
FT ECO:0007744|PDB:2MSB, ECO:0007744|PDB:3KMB,
FT ECO:0007744|PDB:4KMB"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11850428,
FT ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:7704532,
FT ECO:0000269|PubMed:9033386, ECO:0007744|PDB:1KMB,
FT ECO:0007744|PDB:1KWT, ECO:0007744|PDB:1KWU,
FT ECO:0007744|PDB:1KWV, ECO:0007744|PDB:1KWW,
FT ECO:0007744|PDB:1KWX, ECO:0007744|PDB:1KWY,
FT ECO:0007744|PDB:1KWZ, ECO:0007744|PDB:1KX0,
FT ECO:0007744|PDB:1KX1, ECO:0007744|PDB:1RTM,
FT ECO:0007744|PDB:2KMB, ECO:0007744|PDB:2MSB,
FT ECO:0007744|PDB:3KMB, ECO:0007744|PDB:4KMB"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11850428,
FT ECO:0000269|PubMed:1436090, ECO:0000269|PubMed:7704532,
FT ECO:0000269|PubMed:9033386, ECO:0007744|PDB:1KMB,
FT ECO:0007744|PDB:1KWT, ECO:0007744|PDB:1KWU,
FT ECO:0007744|PDB:1KWV, ECO:0007744|PDB:1KWW,
FT ECO:0007744|PDB:1KWX, ECO:0007744|PDB:1KWY,
FT ECO:0007744|PDB:1KWZ, ECO:0007744|PDB:1KX0,
FT ECO:0007744|PDB:1KX1, ECO:0007744|PDB:1RTM,
FT ECO:0007744|PDB:2KMB, ECO:0007744|PDB:2MSB,
FT ECO:0007744|PDB:3KMB, ECO:0007744|PDB:4KMB"
FT MOD_RES 43
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 44
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:10903744,
FT ECO:0000269|PubMed:25419660"
FT MOD_RES 47
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:10903744,
FT ECO:0000269|PubMed:25419660"
FT MOD_RES 50
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25419660"
FT MOD_RES 61
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 67
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 73
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 78
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 79
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:25419660"
FT MOD_RES 82
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:25419660"
FT CARBOHYD 44
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000269|PubMed:10903744,
FT ECO:0000269|PubMed:25419660"
FT CARBOHYD 47
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000269|PubMed:10903744,
FT ECO:0000269|PubMed:25419660"
FT CARBOHYD 79
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000269|PubMed:25419660"
FT CARBOHYD 82
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000269|PubMed:25419660"
FT DISULFID 145..234
FT /evidence="ECO:0000269|PubMed:1436090,
FT ECO:0000269|PubMed:1721241, ECO:0000269|PubMed:7704532,
FT ECO:0000269|PubMed:9922165, ECO:0007744|PDB:1AFA,
FT ECO:0007744|PDB:1AFB, ECO:0007744|PDB:1AFD,
FT ECO:0007744|PDB:1BCH, ECO:0007744|PDB:1BCJ,
FT ECO:0007744|PDB:1BUU, ECO:0007744|PDB:1FIF,
FT ECO:0007744|PDB:1FIH, ECO:0007744|PDB:1KMB,
FT ECO:0007744|PDB:1KWT, ECO:0007744|PDB:1KWU,
FT ECO:0007744|PDB:1KWV, ECO:0007744|PDB:1KWW,
FT ECO:0007744|PDB:1KWX, ECO:0007744|PDB:1KWY,
FT ECO:0007744|PDB:1KWZ, ECO:0007744|PDB:1KX0,
FT ECO:0007744|PDB:1KX1, ECO:0007744|PDB:1MSB,
FT ECO:0007744|PDB:1RTM, ECO:0007744|PDB:1YTT,
FT ECO:0007744|PDB:2KMB, ECO:0007744|PDB:2MSB,
FT ECO:0007744|PDB:3KMB, ECO:0007744|PDB:4KMB"
FT DISULFID 212..226
FT /evidence="ECO:0000269|PubMed:1436090,
FT ECO:0000269|PubMed:1721241, ECO:0000269|PubMed:7704532,
FT ECO:0000269|PubMed:9922165, ECO:0007744|PDB:1AFA,
FT ECO:0007744|PDB:1AFB, ECO:0007744|PDB:1AFD,
FT ECO:0007744|PDB:1BCH, ECO:0007744|PDB:1BCJ,
FT ECO:0007744|PDB:1BUU, ECO:0007744|PDB:1FIF,
FT ECO:0007744|PDB:1FIH, ECO:0007744|PDB:1KMB,
FT ECO:0007744|PDB:1KWT, ECO:0007744|PDB:1KWU,
FT ECO:0007744|PDB:1KWV, ECO:0007744|PDB:1KWW,
FT ECO:0007744|PDB:1KWX, ECO:0007744|PDB:1KWY,
FT ECO:0007744|PDB:1KWZ, ECO:0007744|PDB:1KX0,
FT ECO:0007744|PDB:1KX1, ECO:0007744|PDB:1MSB,
FT ECO:0007744|PDB:1RTM, ECO:0007744|PDB:1YTT,
FT ECO:0007744|PDB:2KMB, ECO:0007744|PDB:2MSB,
FT ECO:0007744|PDB:3KMB, ECO:0007744|PDB:4KMB"
FT MUTAGEN 40
FT /note="R->C: Prevents higher-order oligomer assembly.
FT Slight reduction in secretion rate."
FT /evidence="ECO:0000269|PubMed:10903744"
FT MUTAGEN 42
FT /note="G->E: Disrupts homotrimer formation. 5-fold
FT reduction in secretion rate. Prevents K-44 hydroxylation
FT and glycosylation. 10-fold decrease in complement
FT activation."
FT /evidence="ECO:0000269|PubMed:10903744"
FT MUTAGEN 44
FT /note="K->R: No effect on secretion rate, nor on
FT homooligomer formation. 3-fold reduction in secretion rate;
FT when associated eith R-47. Prevents higher-order oligomer
FT assembly; when associated eith R-47. 10-fold decrease in
FT complement activation; when associated eith R-47."
FT /evidence="ECO:0000269|PubMed:10903744"
FT MUTAGEN 45
FT /note="G->D: Disrupts homotrimer formation. 5-fold
FT reduction in secretion rate. Prevents K-47 hydroxylation
FT and glycosylation."
FT /evidence="ECO:0000269|PubMed:10903744"
FT MUTAGEN 47
FT /note="K->R: No effect on secretion rate, nor on
FT homooligomer formation. 3-fold reduction in secretion rate;
FT when associated eith R-44. Prevents higher-order oligomer
FT assembly; when associated eith R-44. 10-fold decrease in
FT complement activation; when associated eith R-44."
FT /evidence="ECO:0000269|PubMed:10903744"
FT MUTAGEN 228..230
FT /note="ASH->KKK: Changes carbohydrate binding specificity,
FT leading to interaction with Lewis blood group antigens."
FT /evidence="ECO:0000269|PubMed:9033386"
FT CONFLICT 156
FT /note="R -> K (in Ref. 2; AAA98781)"
FT /evidence="ECO:0000305"
FT HELIX 91..119
FT /evidence="ECO:0007829|PDB:1RTM"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:2MSB"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:2MSB"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1BUU"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:2MSB"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:2MSB"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:2MSB"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:2MSB"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:1BUU"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:2MSB"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1RTM"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:2MSB"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:2MSB"
SQ SEQUENCE 238 AA; 25308 MW; 1A927482B8A8CB3D CRC64;
MLLLPLLVLL CVVSVSSSGS QTCEETLKTC SVIACGRDGR DGPKGEKGEP GQGLRGLQGP
PGKLGPPGSV GAPGSQGPKG QKGDRGDSRA IEVKLANMEA EINTLKSKLE LTNKLHAFSM
GKKSGKKFFV TNHERMPFSK VKALCSELRG TVAIPRNAEE NKAIQEVAKT SAFLGITDEV
TEGQFMYVTG GRLTYSNWKK DEPNDHGSGE DCVTIVDNGL WNDISCQASH TAVCEFPA
