ID CL18A_HUMAN Reviewed; 446 AA. AC A5D8T8; A8K1G9; Q6DCB3; Q7Z5K9; Q96HH2; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 3. DT 13-FEB-2019, entry version 102. DE RecName: Full=C-type lectin domain family 18 member A; DE AltName: Full=Mannose receptor-like protein 2; DE Flags: Precursor; GN Name=CLEC18A; Synonyms=MRLP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-118. RA Ding P., Han W., Rui M., Wang Y., Zhang Y., Song Q., Ma D.; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP ALA-118. RC TISSUE=Caudate nucleus; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND RP VARIANTS ALA-118; MET-151 AND ARG-339. RC TISSUE=Brain, and Colon; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS ALA-118; RP MET-151 AND ARG-339, GLYCOSYLATION, MUTAGENESIS OF ASP-421, AND RP CHARACTERIZATION OF VARIANT ARG-339. RX PubMed=26170455; DOI=10.1074/jbc.M115.649814; RA Huang Y.L., Pai F.S., Tsou Y.T., Mon H.C., Hsu T.L., Wu C.Y., RA Chou T.Y., Yang W.B., Chen C.H., Wong C.H., Hsieh S.L.; RT "Human CLEC18 gene cluster contains C-type lectins with differential RT glycan-binding specificity."; RL J. Biol. Chem. 290:21252-21263(2015). CC -!- FUNCTION: Binds polysaccharides in a Ca(2+)-independent manner CC with a preferentially binding to fucoidan, beta-glucans and CC galactans (PubMed:26170455). {ECO:0000269|PubMed:26170455}. CC -!- INTERACTION: CC Q6UY14-3:ADAMTSL4; NbExp=3; IntAct=EBI-10173491, EBI-10173507; CC Q6A162:KRT40; NbExp=3; IntAct=EBI-10173491, EBI-10171697; CC Q7Z3S9:NOTCH2NLA; NbExp=3; IntAct=EBI-10173491, EBI-945833; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26170455}. CC Endoplasmic reticulum {ECO:0000305|PubMed:26170455}. Golgi CC apparatus {ECO:0000305|PubMed:26170455}. Endosome CC {ECO:0000305|PubMed:26170455}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=A5D8T8-1; Sequence=Displayed; CC Name=2; CC IsoId=A5D8T8-2; Sequence=VSP_032204, VSP_032205; CC -!- TISSUE SPECIFICITY: Dectected in all cell lines tested and in CC peripheral blood cells. {ECO:0000269|PubMed:26170455}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:26170455}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH08616.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AF521893; AAP80866.1; -; mRNA. DR EMBL; AK289884; BAF82573.1; -; mRNA. DR EMBL; AC026468; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008616; AAH08616.1; ALT_INIT; mRNA. DR EMBL; BC078143; AAH78143.1; -; mRNA. DR EMBL; BC141808; AAI41809.1; -; mRNA. DR CCDS; CCDS10886.1; -. [A5D8T8-1] DR RefSeq; NP_001129686.1; NM_001136214.2. [A5D8T8-1] DR RefSeq; NP_001258126.1; NM_001271197.1. [A5D8T8-1] DR RefSeq; NP_872425.2; NM_182619.3. [A5D8T8-1] DR RefSeq; XP_005255991.1; XM_005255934.1. [A5D8T8-1] DR UniGene; Hs.592064; -. DR ProteinModelPortal; A5D8T8; -. DR SMR; A5D8T8; -. DR BioGrid; 131512; 11. DR IntAct; A5D8T8; 6. DR STRING; 9606.ENSP00000288040; -. DR iPTMnet; A5D8T8; -. DR PhosphoSitePlus; A5D8T8; -. DR BioMuta; CLEC18A; -. DR PaxDb; A5D8T8; -. DR PRIDE; A5D8T8; -. DR ProteomicsDB; 710; -. DR ProteomicsDB; 711; -. [A5D8T8-2] DR DNASU; 348174; -. DR Ensembl; ENST00000288040; ENSP00000288040; ENSG00000157322. [A5D8T8-1] DR Ensembl; ENST00000393701; ENSP00000377304; ENSG00000157322. [A5D8T8-1] DR Ensembl; ENST00000568461; ENSP00000454685; ENSG00000157322. [A5D8T8-1] DR Ensembl; ENST00000615430; ENSP00000484176; ENSG00000157322. [A5D8T8-1] DR GeneID; 348174; -. DR KEGG; hsa:348174; -. DR UCSC; uc002exz.5; human. [A5D8T8-1] DR CTD; 348174; -. DR EuPathDB; HostDB:ENSG00000157322.16; -. DR GeneCards; CLEC18A; -. DR HGNC; HGNC:30388; CLEC18A. DR HPA; HPA048976; -. DR MIM; 616571; gene. DR neXtProt; NX_A5D8T8; -. DR PharmGKB; PA164717976; -. DR eggNOG; KOG3017; Eukaryota. DR eggNOG; KOG4297; Eukaryota. DR eggNOG; COG2340; LUCA. DR GeneTree; ENSGT00900000141128; -. DR HOGENOM; HOG000111780; -. DR InParanoid; A5D8T8; -. DR KO; K22682; -. DR OrthoDB; 1528782at2759; -. DR PhylomeDB; A5D8T8; -. DR TreeFam; TF350472; -. DR ChiTaRS; CLEC18A; human. DR GenomeRNAi; 348174; -. DR PRO; PR:A5D8T8; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000157322; Expressed in 79 organ(s), highest expression level in adult mammalian kidney. DR ExpressionAtlas; A5D8T8; baseline and differential. DR Genevisible; A5D8T8; HS. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:UniProtKB. DR GO; GO:0005768; C:endosome; TAS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB. DR GO; GO:0030247; F:polysaccharide binding; IDA:UniProtKB. DR Gene3D; 3.10.100.10; -; 1. DR Gene3D; 3.40.33.10; -; 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; IPR014044; CAP_domain. DR InterPro; IPR035940; CAP_sf. DR InterPro; IPR001283; CRISP-related. DR InterPro; IPR016187; CTDL_fold. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR PANTHER; PTHR10334; PTHR10334; 1. DR Pfam; PF00188; CAP; 1. DR Pfam; PF00059; Lectin_C; 1. DR PRINTS; PR00837; V5TPXLIKE. DR SMART; SM00034; CLECT; 1. DR SMART; SM00181; EGF; 2. DR SMART; SM00198; SCP; 1. DR SUPFAM; SSF55797; SSF55797; 1. DR SUPFAM; SSF56436; SSF56436; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. DR PROSITE; PS00022; EGF_1; 2. DR PROSITE; PS01186; EGF_2; 2. DR PROSITE; PS50026; EGF_3; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Disulfide bond; KW EGF-like domain; Endoplasmic reticulum; Endosome; Glycoprotein; KW Golgi apparatus; Lectin; Polymorphism; Reference proteome; Secreted; KW Signal. FT SIGNAL 1 26 {ECO:0000255}. FT CHAIN 27 446 C-type lectin domain family 18 member A. FT /FTId=PRO_0000324316. FT DOMAIN 52 182 SCP. FT DOMAIN 228 261 EGF-like. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 306 433 C-type lectin. {ECO:0000255|PROSITE- FT ProRule:PRU00040}. FT CARBOHYD 144 144 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 236 249 {ECO:0000250}. FT DISULFID 251 260 {ECO:0000250}. FT DISULFID 327 432 {ECO:0000250}. FT DISULFID 408 424 {ECO:0000250}. FT VAR_SEQ 1 340 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_032204. FT VAR_SEQ 341 371 KVQDILAFYLGRLETTNEVIDSDFETRNFWI -> MGAASA FT GKRGQKGSWQQTPGSEWANLDYPGP (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_032205. FT VARIANT 118 118 V -> A (in allele CLEC18A-1; FT dbSNP:rs2549097). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:26170455, FT ECO:0000269|Ref.1}. FT /FTId=VAR_059449. FT VARIANT 151 151 T -> M (in allele CLEC18A-1; FT dbSNP:rs75776403). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:26170455}. FT /FTId=VAR_074610. FT VARIANT 339 339 S -> R (in allele CLEC18A-1; abolishes FT binding to polysaccharides). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:26170455}. FT /FTId=VAR_074611. FT MUTAGEN 421 421 D->N: Has a mild effect on FT polysaccharides binding. FT {ECO:0000269|PubMed:26170455}. FT CONFLICT 273 273 F -> L (in Ref. 4; AAH78143). FT {ECO:0000305}. FT CONFLICT 401 402 DN -> AT (in Ref. 4; AAH08616). FT {ECO:0000305}. FT CONFLICT 421 421 D -> N (in Ref. 4; AAH78143). FT {ECO:0000305}. SQ SEQUENCE 446 AA; 49602 MW; C33BD9480D47DB9B CRC64; MLHPETSPGR GHLLAVLLAL LGTAWAEVWP PQLQEQAPMA GALNRKESFL LLSLHNRLRS WVQPPAADMR RLDWSDSLAQ LAQARAALCG TPTPSLASGL WRTLQVGWNM QLLPAGLVSF VEVVSLWFAE GQRYSHAAGE CARNATCTHY TQLVWATSSQ LGCGRHLCSA GQAAIEAFVC AYSPRGNWEV NGKTIVPYKK GAWCSLCTAS VSGCFKAWDH AGGLCEVPRN PCRMSCQNHG RLNISTCHCH CPPGYTGRYC QVRCSLQCVH GRFREEECSC VCDIGYGGAQ CATKVHFPFH TCDLRIDGDC FMVSSEADTY YRARMKCQRK GGVLAQIKSQ KVQDILAFYL GRLETTNEVI DSDFETRNFW IGLTYKTAKD SFRWATGEHQ AFTSFAFGQP DNHGFGNCVE LQASAAFNWN DQRCKTRNRY ICQFAQEHIS RWGPGS //