COL10_HUMAN
ID COL10_HUMAN Reviewed; 277 AA.
AC Q9Y6Z7; Q3SYH6; Q6UW19;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Collectin-10;
DE AltName: Full=Collectin liver protein 1;
DE Short=CL-L1;
DE AltName: Full=Collectin-34;
DE Short=CL-34;
DE Flags: Precursor;
GN Name=COLEC10; Synonyms=CLL1; ORFNames=UNQ366/PRO702;
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], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10224141; DOI=10.1074/jbc.274.19.13681;
RA Ohtani K., Suzuki Y., Eda S., Kawai T., Kase T., Yamazaki H., Shimada T.,
RA Keshi H., Sakai Y., Fukuoh A., Sakamoto T., Wakamiya N.;
RT "Molecular cloning of a novel human collectin from liver (CL-L1).";
RL J. Biol. Chem. 274:13681-13689(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RC TISSUE=Placenta;
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].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN 3MC3, VARIANTS 3MC3
RP 9-ARG--LYS-277 DEL AND TRP-176, AND CHARACTERIZATION OF VARIANTS 3MC3
RP 9-ARG--LYS-277 DEL AND TRP-176.
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 binds to various sugars: galactose > mannose =
CC fucose > N-acetylglucosamine > N-acetylgalactosamine (PubMed:10224141).
CC Acts as a chemoattractant, probably involved in the regulation of cell
CC migration (PubMed:28301481). {ECO:0000269|PubMed:10224141,
CC ECO:0000269|PubMed:28301481}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28301481}. Golgi
CC apparatus {ECO:0000250|UniProtKB:Q8CF98}. Cytoplasm
CC {ECO:0000269|PubMed:10224141}.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, placenta and adrenal
CC gland. Moderately expressed in small intestine, lung, stomach and
CC prostate. Weakly expressed in trachea and spleen.
CC {ECO:0000269|PubMed:10224141}.
CC -!- DISEASE: 3MC syndrome 3 (3MC3) [MIM:248340]: 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:28301481}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the COLEC10/COLEC11 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Collectin L1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_226";
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DR EMBL; AB002631; BAA81747.1; -; mRNA.
DR EMBL; AY359038; AAQ89397.1; -; mRNA.
DR EMBL; AK291791; BAF84480.1; -; mRNA.
DR EMBL; CH471060; EAW91979.1; -; Genomic_DNA.
DR EMBL; BC103815; AAI03816.1; -; mRNA.
DR EMBL; BC103816; AAI03817.1; -; mRNA.
DR CCDS; CCDS6327.1; -.
DR RefSeq; NP_001311024.1; NM_001324095.1.
DR RefSeq; NP_006429.2; NM_006438.4.
DR AlphaFoldDB; Q9Y6Z7; -.
DR SMR; Q9Y6Z7; -.
DR BioGRID; 115833; 70.
DR ComplexPortal; CPX-6181; CL-LK-MASP1 lectin-protease complex.
DR ComplexPortal; CPX-6240; CL-LK-MASP2 lectin-protease complex.
DR IntAct; Q9Y6Z7; 10.
DR MINT; Q9Y6Z7; -.
DR STRING; 9606.ENSP00000332723; -.
DR GlyGen; Q9Y6Z7; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y6Z7; -.
DR PhosphoSitePlus; Q9Y6Z7; -.
DR BioMuta; COLEC10; -.
DR DMDM; 166218411; -.
DR jPOST; Q9Y6Z7; -.
DR MassIVE; Q9Y6Z7; -.
DR MaxQB; Q9Y6Z7; -.
DR PaxDb; Q9Y6Z7; -.
DR PeptideAtlas; Q9Y6Z7; -.
DR PRIDE; Q9Y6Z7; -.
DR ProteomicsDB; 86836; -.
DR Antibodypedia; 13640; 130 antibodies from 16 providers.
DR DNASU; 10584; -.
DR Ensembl; ENST00000332843.3; ENSP00000332723.2; ENSG00000184374.3.
DR GeneID; 10584; -.
DR KEGG; hsa:10584; -.
DR MANE-Select; ENST00000332843.3; ENSP00000332723.2; NM_006438.5; NP_006429.2.
DR UCSC; uc003yoo.4; human.
DR CTD; 10584; -.
DR DisGeNET; 10584; -.
DR GeneCards; COLEC10; -.
DR HGNC; HGNC:2220; COLEC10.
DR HPA; ENSG00000184374; Tissue enriched (liver).
DR MalaCards; COLEC10; -.
DR MIM; 248340; phenotype.
DR MIM; 607620; gene.
DR neXtProt; NX_Q9Y6Z7; -.
DR OpenTargets; ENSG00000184374; -.
DR Orphanet; 293843; 3MC syndrome.
DR PharmGKB; PA26736; -.
DR VEuPathDB; HostDB:ENSG00000184374; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000159374; -.
DR HOGENOM; CLU_049894_3_2_1; -.
DR InParanoid; Q9Y6Z7; -.
DR OMA; VCATHAI; -.
DR OrthoDB; 1105722at2759; -.
DR PhylomeDB; Q9Y6Z7; -.
DR TreeFam; TF330481; -.
DR PathwayCommons; Q9Y6Z7; -.
DR Reactome; R-HSA-166662; Lectin pathway of complement activation.
DR Reactome; R-HSA-166663; Initial triggering of complement.
DR SignaLink; Q9Y6Z7; -.
DR BioGRID-ORCS; 10584; 10 hits in 1062 CRISPR screens.
DR ChiTaRS; COLEC10; human.
DR GenomeRNAi; 10584; -.
DR Pharos; Q9Y6Z7; Tbio.
DR PRO; PR:Q9Y6Z7; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9Y6Z7; protein.
DR Bgee; ENSG00000184374; Expressed in right lobe of liver and 58 other tissues.
DR ExpressionAtlas; Q9Y6Z7; baseline and differential.
DR Genevisible; Q9Y6Z7; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:1905370; C:serine-type endopeptidase complex; IC:ComplexPortal.
DR GO; GO:0042056; F:chemoattractant activity; IDA:UniProtKB.
DR GO; GO:0005537; F:mannose binding; TAS:ProtInc.
DR GO; GO:0002752; P:cell surface pattern recognition receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0001867; P:complement activation, lectin pathway; IDA:ComplexPortal.
DR GO; GO:1904888; P:cranial skeletal system development; IMP: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 Calcium; Collagen; Cytoplasm; Disease variant; Disulfide bond;
KW Glycoprotein; Golgi apparatus; Lectin; Mannose-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..277
FT /note="Collectin-10"
FT /id="PRO_0000314233"
FT DOMAIN 53..112
FT /note="Collagen-like"
FT DOMAIN 155..271
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 40..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 176..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 248..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VARIANT 9..277
FT /note="Missing (in 3MC3; results in lack of protein)"
FT /evidence="ECO:0000269|PubMed:28301481"
FT /id="VAR_078811"
FT VARIANT 176
FT /note="C -> W (in 3MC3; severely decreased secretion;
FT dbSNP:rs773764995)"
FT /evidence="ECO:0000269|PubMed:28301481"
FT /id="VAR_078812"
FT CONFLICT 85
FT /note="Q -> R (in Ref. 1; BAA81747)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="F -> S (in Ref. 2; AAQ89397)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 30705 MW; 392B570025C18C27 CRC64;
MNGFASLLRR NQFILLVLFL LQIQSLGLDI DSRPTAEVCA THTISPGPKG DDGEKGDPGE
EGKHGKVGRM GPKGIKGELG DMGDQGNIGK TGPIGKKGDK GEKGLLGIPG EKGKAGTVCD
CGRYRKFVGQ LDISIARLKT SMKFVKNVIA GIRETEEKFY YIVQEEKNYR ESLTHCRIRG
GMLAMPKDEA ANTLIADYVA KSGFFRVFIG VNDLEREGQY MFTDNTPLQN YSNWNEGEPS
DPYGHEDCVE MLSSGRWNDT ECHLTMYFVC EFIKKKK
