COL11_HUMAN
ID COL11_HUMAN Reviewed; 271 AA.
AC Q9BWP8; A1IGE4; A1IGE5; A1IGE6; A7VJJ2; A7VJJ3; A7VJJ4; A7VJJ5; B2R9M5;
AC B4E1G0; J3KQY9; Q5CZ85; Q7Z6N1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Collectin-11;
DE AltName: Full=Collectin kidney protein 1;
DE Short=CL-K1;
DE Flags: Precursor;
GN Name=COLEC11; ORFNames=UNQ596/PRO1182;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), FUNCTION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=17179669; DOI=10.1111/j.1348-0421.2006.tb03868.x;
RA Keshi H., Sakamoto T., Kawai T., Ohtani K., Katoh T., Jang S.-J.,
RA Motomura W., Yoshizaki T., Fukuda M., Koyama S., Fukuzawa J., Fukuoh A.,
RA Yoshida I., Suzuki Y., Wakamiya N.;
RT "Identification and characterization of a novel human collectin CL-K1.";
RL Microbiol. Immunol. 50:1001-1013(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 10), AND VARIANT
RP ARG-219.
RC TISSUE=Lung, and Ovary;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 9).
RC TISSUE=Neuroblastoma;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-271 (ISOFORM 3).
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP FUNCTION, DNA-BINDING, SUBUNIT, INTERACTION WITH MASP1, AND TISSUE
RP SPECIFICITY.
RX PubMed=20956340; DOI=10.4049/jimmunol.1002185;
RA Hansen S., Selman L., Palaniyar N., Ziegler K., Brandt J., Kliem A.,
RA Jonasson M., Skjoedt M.O., Nielsen O., Hartshorn K., Joergensen T.J.,
RA Skjoedt K., Holmskov U.;
RT "Collectin 11 (CL-11, CL-K1) is a MASP-1/3-associated plasma collectin with
RT microbial-binding activity.";
RL J. Immunol. 185:6096-6104(2010).
RN [10]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=23954398; DOI=10.1016/j.molimm.2013.07.011;
RA Henriksen M.L., Brandt J., Iyer S.S., Thielens N.M., Hansen S.;
RT "Characterization of the interaction between collectin 11 (CL-11, CL-K1)
RT and nucleic acids.";
RL Mol. Immunol. 56:757-767(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12] {ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD}
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 116-270 OF HOMOTRIMER IN COMPLEX
RP WITH CALCIUM AND CARBOHYDRATE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP DISULFIDE BONDS, AND CHARACTERIZATION OF VARIANTS 3MC2 PRO-169; SER-204 AND
RP SER-217 DEL.
RX PubMed=25912189; DOI=10.1186/s12915-015-0136-2;
RA Venkatraman Girija U., Furze C.M., Gingras A.R., Yoshizaki T., Ohtani K.,
RA Marshall J.E., Wallis A.K., Schwaeble W.J., El-Mezgueldi M., Mitchell D.A.,
RA Moody P.C., Wakamiya N., Wallis R.;
RT "Molecular basis of sugar recognition by collectin-K1 and the effects of
RT mutations associated with 3MC syndrome.";
RL BMC Biol. 13:27-27(2015).
RN [13]
RP FUNCTION, AND VARIANTS 3MC2 PRO-169; SER-204 AND SER-217 DEL.
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).
RN [14]
RP FUNCTION, AND VARIANT 3MC2 THR-166.
RX PubMed=28301481; DOI=10.1371/journal.pgen.1006679;
RA Munye M.M., Diaz-Font A., Ocaka L., Henriksen M.L., Lees M., Brady A.,
RA Jenkins D., Morton J., Hansen S.W., Bacchelli C., Beales P.L.,
RA Hernandez-Hernandez V.;
RT "COLEC10 is mutated in 3MC patients and regulates early craniofacial
RT development.";
RL PLoS Genet. 13:E1006679-E1006679(2017).
CC -!- FUNCTION: Lectin that plays a role in innate immunity, apoptosis and
CC embryogenesis (PubMed:23954398, PubMed:25912189, PubMed:21258343).
CC Calcium-dependent lectin that binds self and non-self glycoproteins
CC presenting high mannose oligosaccharides with at least one terminal
CC alpha-1,2-linked mannose epitope (PubMed:25912189). Primarily
CC recognizes the terminal disaccharide of the glycan (PubMed:25912189).
CC Also recognizes a subset of fucosylated glycans and lipopolysaccharides
CC (PubMed:17179669, PubMed:25912189). Plays a role in innate immunity
CC through its ability to bind non-self sugars presented by microorganisms
CC and to activate the complement through the recruitment of MAPS1
CC (PubMed:20956340, PubMed:25912189). Also plays a role in apoptosis
CC through its ability to bind in a calcium-independent manner the DNA
CC present at the surface of apoptotic cells and to activate the
CC complement in response to this binding (Probable). Finally, plays a
CC role in development, probably serving as a guidance cue during the
CC migration of neural crest cells and other cell types during
CC embryogenesis (PubMed:21258343, PubMed:28301481).
CC {ECO:0000269|PubMed:17179669, ECO:0000269|PubMed:20956340,
CC ECO:0000269|PubMed:21258343, ECO:0000269|PubMed:23954398,
CC ECO:0000269|PubMed:25912189, ECO:0000269|PubMed:28301481,
CC ECO:0000305|PubMed:20956340, ECO:0000305|PubMed:23954398}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked (PubMed:20956340,
CC PubMed:25912189). Interacts with MASP1; probably triggers the lectin
CC pathway of complement (PubMed:20956340). {ECO:0000269|PubMed:20956340,
CC ECO:0000269|PubMed:25912189}.
CC -!- INTERACTION:
CC Q9BWP8; Q9BWP8: COLEC11; NbExp=4; IntAct=EBI-25809731, EBI-25809731;
CC Q9BWP8-1; Q9BXI9-2: C1QTNF6; NbExp=3; IntAct=EBI-27104870, EBI-27104631;
CC PRO_0000315044; P07911: UMOD; NbExp=2; IntAct=EBI-26568155, EBI-2819647;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25912189}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1; Synonyms=CL-K1-I;
CC IsoId=Q9BWP8-1; Sequence=Displayed;
CC Name=2; Synonyms=CL-K1-Ia;
CC IsoId=Q9BWP8-2; Sequence=VSP_030468;
CC Name=3; Synonyms=CL-K1-Ib;
CC IsoId=Q9BWP8-3; Sequence=VSP_030470;
CC Name=4; Synonyms=CL-K1-II;
CC IsoId=Q9BWP8-4; Sequence=VSP_030466;
CC Name=5; Synonyms=CL-K1-Ic;
CC IsoId=Q9BWP8-5; Sequence=VSP_030467;
CC Name=6; Synonyms=CL-K1-IIa;
CC IsoId=Q9BWP8-6; Sequence=VSP_030465, VSP_030469;
CC Name=7; Synonyms=CL-K1-IIb;
CC IsoId=Q9BWP8-7; Sequence=VSP_030466, VSP_030470;
CC Name=8; Synonyms=CL-K1-IIc;
CC IsoId=Q9BWP8-8; Sequence=VSP_030463, VSP_030471;
CC Name=9;
CC IsoId=Q9BWP8-9; Sequence=VSP_030464;
CC Name=10;
CC IsoId=Q9BWP8-10; Sequence=VSP_045532;
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:17179669). Detected in adrenal
CC gland, kidney, liver, ovaries and testis (at protein level)
CC (PubMed:20956340). {ECO:0000269|PubMed:17179669,
CC ECO:0000269|PubMed:20956340}.
CC -!- DISEASE: 3MC syndrome 2 (3MC2) [MIM:265050]: A form of 3MC syndrome, an
CC autosomal recessive disorder characterized by facial dysmorphism,
CC craniosynostosis, learning disability, and genital, limb and
CC vesicorenal anomalies. Facial features include hypertelorism,
CC blepharophimosis, blepharoptosis and highly arched eyebrows, cleft lip
CC and/or palate. The term 3MC syndrome includes Carnevale, Mingarelli,
CC Malpuech, and Michels syndromes. {ECO:0000269|PubMed:21258343,
CC ECO:0000269|PubMed:25912189, ECO:0000269|PubMed:28301481}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the COLEC10/COLEC11 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Collectin K1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_225";
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DR EMBL; AB119525; BAF43301.1; -; mRNA.
DR EMBL; AB119650; BAF43302.1; -; mRNA.
DR EMBL; AB119651; BAF43303.1; -; mRNA.
DR EMBL; AB119652; BAF43304.1; -; mRNA.
DR EMBL; AB119684; BAF79604.1; -; mRNA.
DR EMBL; AB119685; BAF79605.1; -; mRNA.
DR EMBL; AB119686; BAF79606.1; -; mRNA.
DR EMBL; AB119687; BAF79607.1; -; mRNA.
DR EMBL; AY358439; AAQ88805.1; -; mRNA.
DR EMBL; AK303824; BAG64772.1; -; mRNA.
DR EMBL; AK313840; BAG36572.1; -; mRNA.
DR EMBL; AC010907; AAY24235.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01053.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01054.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX01055.1; -; Genomic_DNA.
DR EMBL; BC000078; AAH00078.1; -; mRNA.
DR EMBL; BC009951; AAH09951.1; -; mRNA.
DR EMBL; CR936641; CAI56781.1; -; mRNA.
DR CCDS; CCDS1649.1; -. [Q9BWP8-1]
DR CCDS; CCDS1650.1; -. [Q9BWP8-9]
DR CCDS; CCDS58689.1; -. [Q9BWP8-10]
DR CCDS; CCDS58690.1; -. [Q9BWP8-3]
DR CCDS; CCDS58691.1; -. [Q9BWP8-4]
DR CCDS; CCDS58692.1; -. [Q9BWP8-7]
DR CCDS; CCDS58693.1; -. [Q9BWP8-6]
DR CCDS; CCDS58694.1; -. [Q9BWP8-8]
DR RefSeq; NP_001242911.1; NM_001255982.1. [Q9BWP8-2]
DR RefSeq; NP_001242912.1; NM_001255983.1. [Q9BWP8-3]
DR RefSeq; NP_001242913.1; NM_001255984.1. [Q9BWP8-5]
DR RefSeq; NP_001242914.1; NM_001255985.1. [Q9BWP8-10]
DR RefSeq; NP_001242915.1; NM_001255986.1. [Q9BWP8-4]
DR RefSeq; NP_001242916.1; NM_001255987.1. [Q9BWP8-6]
DR RefSeq; NP_001242917.1; NM_001255988.1. [Q9BWP8-7]
DR RefSeq; NP_001242918.1; NM_001255989.1. [Q9BWP8-8]
DR RefSeq; NP_076932.1; NM_024027.4. [Q9BWP8-1]
DR RefSeq; NP_954705.1; NM_199235.2. [Q9BWP8-9]
DR PDB; 4YLI; X-ray; 2.45 A; A/B/C/D/E/F=116-270.
DR PDB; 4YMD; X-ray; 2.87 A; A/B/C/D/E/F=116-270.
DR PDBsum; 4YLI; -.
DR PDBsum; 4YMD; -.
DR AlphaFoldDB; Q9BWP8; -.
DR SMR; Q9BWP8; -.
DR BioGRID; 122460; 23.
DR ComplexPortal; CPX-6181; CL-LK-MASP1 lectin-protease complex.
DR ComplexPortal; CPX-6240; CL-LK-MASP2 lectin-protease complex.
DR IntAct; Q9BWP8; 14.
DR STRING; 9606.ENSP00000411770; -.
DR UniLectin; Q9BWP8; -.
DR iPTMnet; Q9BWP8; -.
DR PhosphoSitePlus; Q9BWP8; -.
DR BioMuta; COLEC11; -.
DR DMDM; 74733453; -.
DR MassIVE; Q9BWP8; -.
DR PaxDb; Q9BWP8; -.
DR PeptideAtlas; Q9BWP8; -.
DR PRIDE; Q9BWP8; -.
DR ProteomicsDB; 79295; -. [Q9BWP8-1]
DR ProteomicsDB; 79296; -. [Q9BWP8-2]
DR ProteomicsDB; 79297; -. [Q9BWP8-3]
DR ProteomicsDB; 79298; -. [Q9BWP8-4]
DR ProteomicsDB; 79299; -. [Q9BWP8-5]
DR ProteomicsDB; 79300; -. [Q9BWP8-6]
DR ProteomicsDB; 79301; -. [Q9BWP8-7]
DR ProteomicsDB; 79302; -. [Q9BWP8-8]
DR ProteomicsDB; 79303; -. [Q9BWP8-9]
DR Antibodypedia; 26364; 198 antibodies from 28 providers.
DR DNASU; 78989; -.
DR Ensembl; ENST00000236693.11; ENSP00000236693.7; ENSG00000118004.18. [Q9BWP8-9]
DR Ensembl; ENST00000349077.9; ENSP00000339168.4; ENSG00000118004.18. [Q9BWP8-1]
DR Ensembl; ENST00000382062.6; ENSP00000371494.2; ENSG00000118004.18. [Q9BWP8-3]
DR Ensembl; ENST00000402794.4; ENSP00000384882.1; ENSG00000118004.18. [Q9BWP8-6]
DR Ensembl; ENST00000402922.2; ENSP00000385653.1; ENSG00000118004.18. [Q9BWP8-7]
DR Ensembl; ENST00000403096.7; ENSP00000385130.3; ENSG00000118004.18. [Q9BWP8-4]
DR Ensembl; ENST00000404205.5; ENSP00000385827.1; ENSG00000118004.18. [Q9BWP8-8]
DR Ensembl; ENST00000418971.6; ENSP00000411770.2; ENSG00000118004.18. [Q9BWP8-10]
DR GeneID; 78989; -.
DR KEGG; hsa:78989; -.
DR MANE-Select; ENST00000349077.9; ENSP00000339168.4; NM_024027.5; NP_076932.1.
DR UCSC; uc002qxz.5; human. [Q9BWP8-1]
DR CTD; 78989; -.
DR DisGeNET; 78989; -.
DR GeneCards; COLEC11; -.
DR HGNC; HGNC:17213; COLEC11.
DR HPA; ENSG00000118004; Tissue enhanced (gallbladder, liver).
DR MalaCards; COLEC11; -.
DR MIM; 265050; phenotype.
DR MIM; 612502; gene.
DR neXtProt; NX_Q9BWP8; -.
DR OpenTargets; ENSG00000118004; -.
DR Orphanet; 293843; 3MC syndrome.
DR PharmGKB; PA26737; -.
DR VEuPathDB; HostDB:ENSG00000118004; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000159468; -.
DR HOGENOM; CLU_049894_3_2_1; -.
DR InParanoid; Q9BWP8; -.
DR OMA; HITMYFL; -.
DR OrthoDB; 1105722at2759; -.
DR PhylomeDB; Q9BWP8; -.
DR TreeFam; TF330481; -.
DR PathwayCommons; Q9BWP8; -.
DR Reactome; R-HSA-166662; Lectin pathway of complement activation.
DR Reactome; R-HSA-166663; Initial triggering of complement.
DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
DR SignaLink; Q9BWP8; -.
DR SIGNOR; Q9BWP8; -.
DR BioGRID-ORCS; 78989; 15 hits in 1065 CRISPR screens.
DR ChiTaRS; COLEC11; human.
DR GenomeRNAi; 78989; -.
DR Pharos; Q9BWP8; Tbio.
DR PRO; PR:Q9BWP8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9BWP8; protein.
DR Bgee; ENSG00000118004; Expressed in right lobe of liver and 108 other tissues.
DR ExpressionAtlas; Q9BWP8; baseline and differential.
DR Genevisible; Q9BWP8; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0009897; C:external side of plasma membrane; IC:ComplexPortal.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IC:ComplexPortal.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0120153; F:calcium-dependent carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0042806; F:fucose binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
DR GO; GO:0070492; F:oligosaccharide binding; IDA:UniProtKB.
DR GO; GO:0019730; P:antimicrobial humoral response; IDA:UniProtKB.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0006956; P:complement activation; IDA:UniProtKB.
DR GO; GO:0001867; P:complement activation, lectin pathway; IDA:ComplexPortal.
DR GO; GO:0032502; P:developmental process; ISS:UniProtKB.
DR GO; GO:0097194; P:execution phase of apoptosis; IC:UniProtKB.
DR GO; GO:1903028; P:positive regulation of opsonization; IDA:ComplexPortal.
DR GO; GO:0006508; P:proteolysis; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Coiled coil; Collagen;
KW Developmental protein; Disease variant; Disulfide bond; Immunity;
KW Innate immunity; Lectin; Mannose-binding; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..271
FT /note="Collectin-11"
FT /id="PRO_0000315044"
FT DOMAIN 65..112
FT /note="Collagen-like"
FT DOMAIN 149..265
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 44..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 114..148
FT /evidence="ECO:0000255"
FT BINDING 200
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YMD"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YLI"
FT BINDING 240
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YMD"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"
FT BINDING 244
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YMD"
FT BINDING 252..254
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YMD"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25912189,
FT ECO:0007744|PDB:4YLI, ECO:0007744|PDB:4YMD"
FT DISULFID 170..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI,
FT ECO:0007744|PDB:4YMD"
FT DISULFID 242..256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:25912189, ECO:0007744|PDB:4YLI,
FT ECO:0007744|PDB:4YMD"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:17179669"
FT /id="VSP_030463"
FT VAR_SEQ 1..67
FT /note="MRGNLALVGVLISLAFLSLLPSGHPQPAGDDACSVQILVPGLKGDAGEKGDK
FT GAPGRPGRVGPTGEK -> MTPALCRSSSLASKGMRERRETKAPPDGLEESAPREKKQS
FT QPVVTASDISKRKCTSSFVEMGSQ (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030464"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:17179669"
FT /id="VSP_030465"
FT VAR_SEQ 1..43
FT /note="MRGNLALVGVLISLAFLSLLPSGHPQPAGDDACSVQILVPGLK -> MWWVP
FT PSPYGCLPCALP (in isoform 4 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:17179669"
FT /id="VSP_030466"
FT VAR_SEQ 1
FT /note="M -> MKKQRGVGVLPALRM (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045532"
FT VAR_SEQ 43..90
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17179669"
FT /id="VSP_030467"
FT VAR_SEQ 43..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17179669"
FT /id="VSP_030468"
FT VAR_SEQ 51..67
FT /note="DKGAPGRPGRVGPTGEK -> MWWVPPSPYGCLPCALP (in isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:17179669"
FT /id="VSP_030469"
FT VAR_SEQ 67..90
FT /note="Missing (in isoform 3 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:17179669,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_030470"
FT VAR_SEQ 75..91
FT /note="QKGSVGRHGKIGPIGSK -> MWWVPPSPYGCLPCALP (in isoform
FT 8)"
FT /evidence="ECO:0000303|PubMed:17179669"
FT /id="VSP_030471"
FT VARIANT 166
FT /note="A -> T (in 3MC2; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:28301481"
FT /id="VAR_078813"
FT VARIANT 169
FT /note="S -> P (in 3MC2; no effect on homotrimerization;
FT loss of calcium-binding; loss of carbohydrate-binding
FT probably due to the inability to bind calcium; not secreted
FT probably due to degradation early after biosynthesis;
FT dbSNP:rs387907075)"
FT /evidence="ECO:0000269|PubMed:21258343,
FT ECO:0000269|PubMed:25912189"
FT /id="VAR_065901"
FT VARIANT 204
FT /note="G -> S (in 3MC2; no effect on homotrimerization;
FT loss of calcium-binding; loss of carbohydrate-binding
FT probably due to the inability to bind calcium; not secreted
FT probably due to degradation early after biosynthesis;
FT dbSNP:rs387907076)"
FT /evidence="ECO:0000269|PubMed:21258343,
FT ECO:0000269|PubMed:25912189"
FT /id="VAR_065902"
FT VARIANT 217
FT /note="Missing (in 3MC2; no effect on homotrimerization;
FT loss of calcium-binding; loss of carbohydrate-binding
FT probably due to the inability to bind calcium; not secreted
FT probably due to degradation early after biosynthesis)"
FT /evidence="ECO:0000269|PubMed:21258343,
FT ECO:0000269|PubMed:25912189"
FT /id="VAR_065903"
FT VARIANT 219
FT /note="H -> R (in dbSNP:rs7567833)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_038143"
FT CONFLICT 178
FT /note="S -> T (in Ref. 7; CAI56781)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="G -> D (in Ref. 3; BAG64772)"
FT /evidence="ECO:0000305"
FT HELIX 117..141
FT /evidence="ECO:0007829|PDB:4YLI"
FT STRAND 150..161
FT /evidence="ECO:0007829|PDB:4YLI"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:4YLI"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:4YLI"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:4YLI"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:4YLI"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:4YLI"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4YLI"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:4YLI"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:4YLI"
SQ SEQUENCE 271 AA; 28665 MW; A14A248CE41DB340 CRC64;
MRGNLALVGV LISLAFLSLL PSGHPQPAGD DACSVQILVP GLKGDAGEKG DKGAPGRPGR
VGPTGEKGDM GDKGQKGSVG RHGKIGPIGS KGEKGDSGDI GPPGPNGEPG LPCECSQLRK
AIGEMDNQVS QLTSELKFIK NAVAGVRETE SKIYLLVKEE KRYADAQLSC QGRGGTLSMP
KDEAANGLMA AYLAQAGLAR VFIGINDLEK EGAFVYSDHS PMRTFNKWRS GEPNNAYDEE
DCVEMVASGG WNDVACHTTM YFMCEFDKEN M
