MBL_CHICK
ID MBL_CHICK Reviewed; 254 AA.
AC Q98TA4; F1NKG3;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Mannose-binding protein {ECO:0000305};
DE Short=MBP {ECO:0000305};
DE AltName: Full=Mannan-binding protein {ECO:0000305};
DE Flags: Precursor;
GN Name=MBL {ECO:0000305};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|EMBL:AAK30298.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11003389; DOI=10.1007/s002510000232;
RA Vitved L., Holmskov U., Koch C., Teisner B., Hansen S., Skjodt K.;
RT "The homologue of mannose-binding lectin in the carp family Cyprinidae is
RT expressed at high level in spleen, and the deduced primary structure
RT predicts affinity for galactose.";
RL Immunogenetics 51:955-964(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Mamu G., Brah G.S., Deka D., Mukhopadhyay C.S.;
RT "Molecular characterization of mannose binding lectin protein in divergent
RT breeds of chickens.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [5]
RP LACK OF PARALOG.
RX PubMed=25721364; DOI=10.1016/j.molimm.2015.01.027;
RA Hamzic E., Pinard-van der Laan M.H., Bed'Hom B., Juul-Madsen H.R.;
RT "Annotation and genetic diversity of the chicken collagenous lectins.";
RL Mol. Immunol. 65:277-286(2015).
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.
CC {ECO:0000250|UniProtKB:Q5U9S1}.
CC -!- SUBUNIT: Oligomeric complex of 3 or more homotrimers.
CC {ECO:0000250|UniProtKB:P19999}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P19999}.
CC -!- MISCELLANEOUS: In contrast to mammals, which contain two copies of MBL
CC (MBL1 and MBL2), chicken genome only contains one copy of MBL.
CC {ECO:0000269|PubMed:25721364}.
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DR EMBL; AF231714; AAK30298.1; -; mRNA.
DR EMBL; KU378614; ANH22044.1; -; mRNA.
DR EMBL; KU378615; ANH22045.1; -; mRNA.
DR EMBL; KF469209; AHA14647.1; -; mRNA.
DR EMBL; AADN03005176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_989680.2; NM_204349.2.
DR AlphaFoldDB; Q98TA4; -.
DR SMR; Q98TA4; -.
DR STRING; 9031.ENSGALP00000040351; -.
DR Ensembl; ENSGALT00000041145; ENSGALP00000040351; ENSGALG00000002507.
DR GeneID; 374267; -.
DR KEGG; gga:374267; -.
DR CTD; 4153; -.
DR VEuPathDB; HostDB:geneid_374267; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000154368; -.
DR OMA; CAKFQAS; -.
DR OrthoDB; 1222552at2759; -.
DR PhylomeDB; Q98TA4; -.
DR TreeFam; TF330481; -.
DR Reactome; R-GGA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-GGA-2132263; Creation of classical C3 convertase.
DR Reactome; R-GGA-2132270; Lectin-mediated initiation of complement cascade.
DR Reactome; R-GGA-391160; Signal regulatory protein family interactions.
DR Reactome; R-GGA-5683826; Surfactant metabolism.
DR Reactome; R-GGA-5686938; Regulation of TLR by endogenous ligand.
DR PRO; PR:Q98TA4; -.
DR Proteomes; UP000000539; Chromosome 6.
DR Bgee; ENSGALG00000002507; Expressed in liver and 5 other tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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 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 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 2: Evidence at transcript level;
KW Calcium; 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..254
FT /note="Mannose-binding protein"
FT /id="PRO_5005942485"
FT DOMAIN 140..250
FT /note="C-type lectin"
FT /evidence="ECO:0000255"
FT REGION 46..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 58
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 61
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 75
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000255"
FT MOD_RES 93
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT MOD_RES 96
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT CARBOHYD 58
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT CARBOHYD 61
FT /note="O-linked (Gal...) hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT DISULFID 161..252
FT /evidence="ECO:0000250|UniProtKB:P19999"
FT DISULFID 229..243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 102
FT /note="A -> V (in Ref. 1; AAK30298 and 2; AHA14647)"
FT CONFLICT 137
FT /note="F -> V (in Ref. 1; AAK30298 and 2; AHA14647)"
SQ SEQUENCE 254 AA; 27396 MW; CFA5DDF724487D47 CRC64;
MTLLQPFSAL LLCLSLMMAT SLLTTDKPEE KMYSCPIIQC SAPAVNGLPG RDGRDGPKGE
KGDPGEGLRG LQGLPGKAGP QGLKGEVGPQ GEKGQKGERG IAVTDDLHRQ ITDLEAKIRV
LEDDLSRYKK ALSLKDFVNV GKKMFVSTGK KYNFEKGKSL CAKAGSVLAS PRNEAENTAL
KDLIDPSSQA YIGISDAQTE GRFMYLSGGP LTYSNWKPGE PNNHKNEDCA VIEDSGKWND
LDCSNSNIFI ICEL
