COL11_MOUSE
ID COL11_MOUSE Reviewed; 272 AA.
AC Q3SXB8; Q3SXB7; Q9DC75;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Collectin-11;
DE AltName: Full=Collectin kidney protein 1;
DE Short=CL-K1;
DE Flags: Precursor;
GN Name=Colec11;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Heart;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=21258343; DOI=10.1038/ng.757;
RA Rooryck C., Diaz-Font A., Osborn D.P., Chabchoub E.,
RA Hernandez-Hernandez V., Shamseldin H., Kenny J., Waters A., Jenkins D.,
RA Kaissi A.A., Leal G.F., Dallapiccola B., Carnevale F., Bitner-Glindzicz M.,
RA Lees M., Hennekam R., Stanier P., Burns A.J., Peeters H., Alkuraya F.S.,
RA Beales P.L.;
RT "Mutations in lectin complement pathway genes COLEC11 and MASP1 cause 3MC
RT syndrome.";
RL Nat. Genet. 43:197-203(2011).
CC -!- FUNCTION: Lectin that plays a role in innate immunity, apoptosis and
CC embryogenesis. Calcium-dependent lectin that binds self and non-self
CC glycoproteins presenting high mannose oligosaccharides with at least
CC one terminal alpha-1,2-linked mannose epitope. Primarily recognizes the
CC terminal disaccharide of the glycan. Also recognizes a subset of
CC fucosylated glycans and lipopolysaccharides. Plays a role in innate
CC immunity through its ability to bind non-self sugars presented by
CC microorganisms and to activate the complement through the recruitment
CC of MAPS1. Also plays a role in apoptosis through its ability to bind in
CC a calcium-independent manner the DNA present at the surface of
CC apoptotic cells and to activate the complement in response to this
CC binding. Finally, plays a role in development, probably serving as a
CC guidance cue during the migration of neural crest cells and other cell
CC types during embryogenesis. {ECO:0000250|UniProtKB:Q9BWP8}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Interacts with MASP1; probably
CC triggers the lectin pathway of complement.
CC {ECO:0000250|UniProtKB:Q9BWP8}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9BWP8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3SXB8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3SXB8-2; Sequence=VSP_030472;
CC -!- TISSUE SPECIFICITY: Highly expressed in embryonic murine craniofacial
CC cartilage, heart, bronchi, kidney and vertebral bodies.
CC {ECO:0000269|PubMed:21258343}.
CC -!- SIMILARITY: Belongs to the COLEC10/COLEC11 family. {ECO:0000305}.
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DR EMBL; AK003121; BAB22581.1; -; mRNA.
DR EMBL; BC104380; AAI04381.2; -; mRNA.
DR EMBL; BC104381; AAI04382.2; -; mRNA.
DR CCDS; CCDS36426.1; -. [Q3SXB8-1]
DR CCDS; CCDS88320.1; -. [Q3SXB8-2]
DR RefSeq; NP_082142.1; NM_027866.2.
DR AlphaFoldDB; Q3SXB8; -.
DR SMR; Q3SXB8; -.
DR STRING; 10090.ENSMUSP00000049285; -.
DR PhosphoSitePlus; Q3SXB8; -.
DR CPTAC; non-CPTAC-3379; -.
DR CPTAC; non-CPTAC-3516; -.
DR MaxQB; Q3SXB8; -.
DR PaxDb; Q3SXB8; -.
DR PeptideAtlas; Q3SXB8; -.
DR PRIDE; Q3SXB8; -.
DR ProteomicsDB; 285243; -. [Q3SXB8-1]
DR ProteomicsDB; 285244; -. [Q3SXB8-2]
DR GeneID; 71693; -.
DR KEGG; mmu:71693; -.
DR UCSC; uc007nfr.1; mouse. [Q3SXB8-1]
DR CTD; 78989; -.
DR MGI; MGI:1918943; Colec11.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; Q3SXB8; -.
DR PhylomeDB; Q3SXB8; -.
DR TreeFam; TF330481; -.
DR Reactome; R-MMU-166662; Lectin pathway of complement activation.
DR Reactome; R-MMU-166663; Initial triggering of complement.
DR Reactome; R-MMU-3000480; Scavenging by Class A Receptors.
DR BioGRID-ORCS; 71693; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q3SXB8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3SXB8; protein.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0120153; F:calcium-dependent carbohydrate binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0042806; F:fucose binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005537; F:mannose binding; ISS:UniProtKB.
DR GO; GO:0070492; F:oligosaccharide binding; ISS:UniProtKB.
DR GO; GO:0019730; P:antimicrobial humoral response; ISS:UniProtKB.
DR GO; GO:0006956; P:complement activation; ISO:MGI.
DR GO; GO:0001867; P:complement activation, lectin pathway; ISS:UniProtKB.
DR GO; GO:0032502; P:developmental process; ISS:UniProtKB.
DR GO; GO:1903028; P:positive regulation of opsonization; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
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; 2.
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 Alternative splicing; Calcium; Coiled coil; Collagen;
KW Developmental protein; Disulfide bond; Immunity; Innate immunity; Lectin;
KW Mannose-binding; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..272
FT /note="Collectin-11"
FT /id="PRO_0000315045"
FT DOMAIN 45..104
FT /note="Collagen-like"
FT DOMAIN 150..266
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 45..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..149
FT /evidence="ECO:0000255"
FT BINDING 201
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 236
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 241
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 245
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 253..255
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8"
FT DISULFID 171..265
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 243..257
FT /evidence="ECO:0000250|UniProtKB:Q9BWP8,
FT ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 142
FT /note="N -> NALPSPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030472"
FT CONFLICT 147
FT /note="L -> V (in Ref. 1; BAB22581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 272 AA; 28989 MW; DEC4715CDCDE8B8F CRC64;
MMMRDLALAG MLISLAFLSL LPSGCPQQTT EDACSVQILV PGLKGDAGEK GDKGAPGRPG
RVGPTGEKGD MGDKGQKGTV GRHGKIGPIG AKGEKGDSGD IGPPGPSGEP GIPCECSQLR
KAIGEMDNQV TQLTTELKFI KNAVAGLRET ESKIYLLVKE EKRYADAQLS CQARGGTLSM
PKDEAANGLM ASYLAQAGLA RVFIGINDLE KEGAFVYSDR SPMQTFNKWR SGEPNNAYDE
EDCVEMVASG GWNDVACHIT MYFMCEFDKE NL
