MBL2_PIG
ID MBL2_PIG Reviewed; 240 AA.
AC Q9XSW3; A0SVI8; Q9TR20;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Mannose-binding protein C {ECO:0000250|UniProtKB:P11226};
DE Short=MBP-C {ECO:0000250|UniProtKB:P11226};
DE AltName: Full=27 kDa mannan-binding protein monomeric subunit {ECO:0000303|PubMed:8602463};
DE Short=pMBP-27 {ECO:0000303|PubMed:8602463};
DE AltName: Full=Mannose-binding lectin {ECO:0000303|PubMed:11298833, ECO:0000312|EMBL:AAD45377.1};
DE Short=MBL {ECO:0000303|PubMed:11298833};
DE Flags: Precursor;
GN Name=MBL2 {ECO:0000303|PubMed:17194476, ECO:0000303|PubMed:17284229};
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:AAD45377.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 94-161 AND 195-219,
RP FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver {ECO:0000312|EMBL:AAD45377.1}, and
RC Serum {ECO:0000269|PubMed:11298833};
RX PubMed=11298833; DOI=10.1046/j.1365-2567.2001.01191.x;
RA Agah A., Montalto M.C., Young K., Stahl G.L.;
RT "Isolation, cloning and functional characterization of porcine mannose-
RT binding lectin.";
RL Immunology 102:338-343(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABK78779.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28, 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 [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 19-44, 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 [4] {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).
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. According to some authors, it only binds mannose
CC (PubMed:8602463). {ECO:0000269|PubMed:11298833,
CC ECO:0000269|PubMed:17284229, ECO:0000269|PubMed:8602463}.
CC -!- SUBUNIT: Interacts with MASP1 and MASP2. Interacts with MEP1A and MEP1B
CC and may inhibit their catalytic activity (By similarity). Forms
CC oligomeric complexes of 2 or 3 homotrimers.
CC {ECO:0000250|UniProtKB:P11226, ECO:0000269|PubMed:8602463}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11226}.
CC -!- TISSUE SPECIFICITY: Expressed in liver. Weakly expressed in kidney and
CC testis. {ECO:0000269|PubMed:11298833, ECO:0000269|PubMed:17194476,
CC ECO:0000269|PubMed:17284229}.
CC -!- DOMAIN: The coiled-coil domain mediates trimerization. {ECO:0000250}.
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DR EMBL; AF164576; AAD45377.1; -; mRNA.
DR EMBL; EF028163; ABK78779.1; -; Genomic_DNA.
DR RefSeq; NP_999290.1; NM_214125.1.
DR AlphaFoldDB; Q9XSW3; -.
DR SMR; Q9XSW3; -.
DR PeptideAtlas; Q9XSW3; -.
DR GeneID; 397230; -.
DR KEGG; ssc:397230; -.
DR CTD; 4153; -.
DR InParanoid; Q9XSW3; -.
DR OrthoDB; 1222552at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
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:0005537; F:mannose binding; IEA:UniProtKB-KW.
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:0043129; P:surfactant homeostasis; IBA:GO_Central.
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; Direct protein sequencing; Disulfide bond;
KW Hydroxylation; Immunity; Innate immunity; Lectin; Mannose-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:8602463"
FT CHAIN 19..240
FT /note="Mannose-binding protein C"
FT /evidence="ECO:0000269|PubMed:8602463"
FT /id="PRO_0000397216"
FT DOMAIN 39..61
FT /note="Collagen-like 1"
FT /evidence="ECO:0000255"
FT DOMAIN 67..97
FT /note="Collagen-like 2"
FT /evidence="ECO:0000255"
FT DOMAIN 126..237
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 48..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 104..122
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11226"
FT MOD_RES 72
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11226"
FT MOD_RES 81
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11226"
FT MOD_RES 87
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11226"
FT DISULFID 147..236
FT /evidence="ECO:0000250|UniProtKB:P11226,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 214..228
FT /evidence="ECO:0000250|UniProtKB:P11226,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 19
FT /note="H -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="I -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="S -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 25523 MW; 52BD865A21D3D563 CRC64;
MSLFPSLHLL LLIVMTASHT ETENCEDIQN TCLVISCDSP GINGLPGKDG LDGAKGEKGE
PGQGLIGLQG LPGMVGPQGS PGIPGLPGLK GQKGDSGIDP GNSLANLRSE LDNIKKWLIF
AQGKQVGKKL YLTNGKKMSF NGVKALCAQF QASVATPTNS RENQAIQELA GTEAFLGITD
EYTEGQFVDL TGKRVRYQNW NDGEPNNADS AEHCVEILKD GKWNDIFCSS QLSAVCEFPA
