MBL1_PIG
ID MBL1_PIG Reviewed; 249 AA.
AC Q5U9S1; A0SVI9; Q9TR19; Q9TT24;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Mannose-binding protein A {ECO:0000250|UniProtKB:P19999};
DE Short=MBP-A {ECO:0000250|UniProtKB:P19999};
DE AltName: Full=28 kDa mannan-binding protein monomeric subunit {ECO:0000303|PubMed:8602463};
DE Short=pMBP-28 {ECO:0000303|PubMed:8602463};
DE AltName: Full=Mannan-binding lectin A {ECO:0000303|PubMed:17194476, ECO:0000312|EMBL:AAV40945.1};
DE Short=MBL-A {ECO:0000303|PubMed:17194476};
DE AltName: Full=Mannose-binding lectin A {ECO:0000312|EMBL:ABK78780.1};
DE Flags: Precursor;
GN Name=MBL1 {ECO:0000303|PubMed:17284229};
GN Synonyms=MBL-A {ECO:0000312|EMBL:ABZ79702.1};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAV40945.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-41; 33-39; 106-114 AND
RP 154-165, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver {ECO:0000312|EMBL:AAV40945.1}, and
RC Plasma {ECO:0000269|PubMed:16480769};
RX PubMed=16480769; DOI=10.1016/j.dci.2005.12.008;
RA Lillie B.N., Hammermueller J.D., Macinnes J.I., Jacques M., Hayes M.A.;
RT "Porcine mannan-binding lectin A binds to Actinobacillus suis and
RT Haemophilus parasuis.";
RL Dev. Comp. Immunol. 30:954-965(2006).
RN [2] {ECO:0000312|EMBL:ABZ79702.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Landrace {ECO:0000312|EMBL:ABZ79702.1};
RC TISSUE=Liver {ECO:0000312|EMBL:ABZ79702.1};
RA Yao X., Liu Y.-F., Liu H.-Y.;
RT "Genetic analysis of mannan-binding lectin A from Landrace of China.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:ABK78780.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30, AND TISSUE SPECIFICITY.
RC STRAIN=Landrace {ECO:0000269|PubMed:17194476};
RX PubMed=17194476; DOI=10.1016/j.dci.2006.11.002;
RA Lillie B.N., Keirstead N.D., Squires E.J., Hayes M.A.;
RT "Gene polymorphisms associated with reduced hepatic expression of porcine
RT mannan-binding lectin C.";
RL Dev. Comp. Immunol. 31:830-846(2007).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 21-44, FUNCTION, AND SUBUNIT.
RC TISSUE=Serum {ECO:0000269|PubMed:8602463};
RX PubMed=8602463; DOI=10.1046/j.1365-3083.1996.d01-39.x;
RA Storgaard P., Nielsen E.H., Andersen O., Skriver E., Mortensen H.,
RA Hojrup P., Leslie G., Holmskow U., Svehag S.E.;
RT "Isolation and characterization of porcine mannan-binding proteins of
RT different size and ultrastructure.";
RL Scand. J. Immunol. 43:289-296(1996).
RN [5] {ECO:0000305}
RP PROTEIN SEQUENCE OF 21-35, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Serum {ECO:0000269|PubMed:16518621};
RX PubMed=16518621; DOI=10.1007/s00251-006-0092-7;
RA Juul-Madsen H.R., Krogh-Meibom T., Henryon M., Palaniyar N., Heegaard P.M.,
RA Purup S., Willis A.C., Tornoe I., Ingvartsen K.L., Hansen S., Holmskov U.;
RT "Identification and characterization of porcine mannan-binding lectin A
RT (pMBL-A), and determination of serum concentration heritability.";
RL Immunogenetics 58:129-137(2006).
RN [6] {ECO:0000312|EMBL:AAF21018.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-84.
RX PubMed=11063327; DOI=10.2527/2000.78112992x;
RA Marklund L., Shi X., Tuggle C.K.;
RT "Mapping of the Mannose-Binding Lectin 2 (MBL2) gene to pig chromosome
RT 14.";
RL J. Anim. Sci. 78:2992-2993(2000).
RN [7] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17284229; DOI=10.1111/j.1744-313x.2007.00656.x;
RA Phatsara C., Jennen D.G., Ponsuksili S., Murani E., Tesfaye D.,
RA Schellander K., Wimmers K.;
RT "Molecular genetic analysis of porcine mannose-binding lectin genes, MBL1
RT and MBL2, and their association with complement activity.";
RL Int. J. Immunogenet. 34:55-63(2007).
RN [8] {ECO:0000305}
RP VARIANT CYS-91.
RX PubMed=17089118; DOI=10.1007/s00251-006-0160-z;
RA Lillie B.N., Keirstead N.D., Squires E.J., Hayes M.A.;
RT "Single-nucleotide polymorphisms in porcine mannan-binding lectin A.";
RL Immunogenetics 58:983-993(2006).
CC -!- FUNCTION: Calcium-dependent lectin. Plays a role in the innate immune
CC response by binding mannose, fucose and N-acetylglucosamine on
CC bacteria, including strains of A.suis, H.parasuis and
CC A.pleuropneumoniae, and activates the lectin complement pathway.
CC According to some authors, it only binds mannose (PubMed:8602463).
CC {ECO:0000269|PubMed:16480769, ECO:0000269|PubMed:16518621,
CC ECO:0000269|PubMed:17284229, ECO:0000269|PubMed:8602463}.
CC -!- SUBUNIT: Interacts with MASP1 and MASP2 (By similarity). Forms
CC oligomeric complexes of 3, 4, 5 or, predominantly, 6 homotrimers. The
CC homotrimers appear as globular heads that are connected to a central
CC hub by thin stalks. {ECO:0000250|UniProtKB:P19999,
CC ECO:0000269|PubMed:16518621, ECO:0000269|PubMed:8602463}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16480769,
CC ECO:0000269|PubMed:16518621}.
CC -!- TISSUE SPECIFICITY: Detected in blood serum (at protein level)
CC (PubMed:16480769, PubMed:16518621). Expressed in liver. Weakly
CC expressed in lung, testis and brain. Not detected in bone marrow and
CC heart. {ECO:0000269|PubMed:16480769, ECO:0000269|PubMed:16518621,
CC ECO:0000269|PubMed:17194476, ECO:0000269|PubMed:17284229}.
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 -!- CAUTION: Incorrectly identified as MBL2 by PubMed:11063327.
CC {ECO:0000305}.
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DR EMBL; AY771222; AAV40945.1; -; mRNA.
DR EMBL; EU421730; ABZ79702.1; -; mRNA.
DR EMBL; EF028164; ABK78780.1; -; Genomic_DNA.
DR EMBL; AF208528; AAF21018.1; -; Genomic_DNA.
DR RefSeq; NP_001007195.1; NM_001007194.3.
DR AlphaFoldDB; Q5U9S1; -.
DR SMR; Q5U9S1; -.
DR STRING; 9823.ENSSSCP00000026746; -.
DR PaxDb; Q5U9S1; -.
DR PeptideAtlas; Q5U9S1; -.
DR Ensembl; ENSSSCT00065093535; ENSSSCP00065040925; ENSSSCG00065068117.
DR Ensembl; ENSSSCT00070002202; ENSSSCP00070001845; ENSSSCG00070001162.
DR GeneID; 492276; -.
DR KEGG; ssc:492276; -.
DR CTD; 17194; -.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; Q5U9S1; -.
DR OrthoDB; 1222552at2759; -.
DR TreeFam; TF330481; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 14.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0005537; F:mannose binding; ISS:UniProtKB.
DR GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
DR GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR GO; GO:0001867; P:complement activation, lectin pathway; IEA:UniProtKB-KW.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central.
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 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..20
FT /evidence="ECO:0000269|PubMed:16480769,
FT ECO:0000269|PubMed:16518621, ECO:0000269|PubMed:8602463"
FT CHAIN 21..249
FT /note="Mannose-binding protein A"
FT /evidence="ECO:0000269|PubMed:16480769,
FT ECO:0000269|PubMed:16518621, ECO:0000269|PubMed:8602463"
FT /id="PRO_5000094188"
FT DOMAIN 64..98
FT /note="Collagen-like"
FT /evidence="ECO:0000255"
FT DOMAIN 135..246
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 41..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..221
FT /note="Calcium-dependent carbohydrate binding"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 54
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 55
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 58
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 61
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 72
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 78
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 89
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 90
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 93
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT CARBOHYD 55
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT CARBOHYD 58
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT CARBOHYD 90
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT CARBOHYD 93
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT DISULFID 156..245
FT /evidence="ECO:0000250|UniProtKB:P19999,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 223..237
FT /evidence="ECO:0000250|UniProtKB:P19999,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT VARIANT 91
FT /note="G -> C"
FT /evidence="ECO:0000269|PubMed:17089118"
FT CONFLICT 11..12
FT /note="LL -> GV (in Ref. 3; ABK78780)"
FT /evidence="ECO:0000305"
FT CONFLICT 21..23
FT /note="EIK -> SIS (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="P -> T (in Ref. 6; AAF21018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 26489 MW; 50BDB1BCF2075558 CRC64;
MLLFSSLPVL LLCVVTASYS EIKTCEDAQK TCSVITCGIP VTNGTPGRDG RDGPKGEKGE
PGPGFRGSQG PPGKMGPPGN IGETGPLGPK GQKGDPGDTS GVEAKLANLE GQIRILKSEL
DHVKKLQTFS LGKKSRKKLY VTNGEMMPFS KVKTLCAELQ ATVATPKNAE ENKAIQDMAP
DVAFLGITDE VTEGQFMYVT GGRMTYSNWK SNEPNDHGSG EDCVILQRDG LWNDISCSSS
FLAVCEFPA
