CL18A_HUMAN
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 03-AUG-2022, entry version 121.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 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., 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 [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., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., 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., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., 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 VARIANTS
RP 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 project:
RT 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., Chou T.Y.,
RA 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 with a
CC preferentially binding to fucoidan, beta-glucans and galactans
CC (PubMed:26170455). {ECO:0000269|PubMed:26170455}.
CC -!- INTERACTION:
CC A5D8T8; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-10173491, EBI-10173507;
CC A5D8T8; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10173491, EBI-3867333;
CC A5D8T8; Q15323: KRT31; NbExp=3; IntAct=EBI-10173491, EBI-948001;
CC A5D8T8; O76011: KRT34; NbExp=3; IntAct=EBI-10173491, EBI-1047093;
CC A5D8T8; Q6A162: KRT40; NbExp=3; IntAct=EBI-10173491, EBI-10171697;
CC A5D8T8; 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 apparatus
CC {ECO:0000305|PubMed:26170455}. Endosome {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};
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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.
DR AlphaFoldDB; A5D8T8; -.
DR SMR; A5D8T8; -.
DR BioGRID; 131512; 18.
DR IntAct; A5D8T8; 11.
DR STRING; 9606.ENSP00000484176; -.
DR GlyGen; A5D8T8; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; A5D8T8; -.
DR PhosphoSitePlus; A5D8T8; -.
DR BioMuta; CLEC18A; -.
DR MassIVE; A5D8T8; -.
DR PaxDb; A5D8T8; -.
DR PeptideAtlas; A5D8T8; -.
DR PRIDE; A5D8T8; -.
DR Antibodypedia; 44487; 130 antibodies from 18 providers.
DR DNASU; 348174; -.
DR Ensembl; ENST00000288040.11; ENSP00000288040.6; ENSG00000157322.18. [A5D8T8-1]
DR Ensembl; ENST00000393701.6; ENSP00000377304.2; ENSG00000157322.18. [A5D8T8-1]
DR Ensembl; ENST00000568461.5; ENSP00000454685.1; ENSG00000157322.18. [A5D8T8-1]
DR Ensembl; ENST00000615430.4; ENSP00000484176.1; ENSG00000157322.18. [A5D8T8-1]
DR GeneID; 348174; -.
DR KEGG; hsa:348174; -.
DR MANE-Select; ENST00000288040.11; ENSP00000288040.6; NM_001370523.4; NP_001357452.1.
DR UCSC; uc002exz.5; human. [A5D8T8-1]
DR CTD; 348174; -.
DR GeneCards; CLEC18A; -.
DR HGNC; HGNC:30388; CLEC18A.
DR HPA; ENSG00000157322; Tissue enriched (kidney).
DR MIM; 616571; gene.
DR neXtProt; NX_A5D8T8; -.
DR PharmGKB; PA164717976; -.
DR VEuPathDB; HostDB:ENSG00000157322; -.
DR eggNOG; KOG3017; Eukaryota.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00900000141128; -.
DR InParanoid; A5D8T8; -.
DR OMA; ICVQNAQ; -.
DR OrthoDB; 1528782at2759; -.
DR PhylomeDB; A5D8T8; -.
DR TreeFam; TF350472; -.
DR PathwayCommons; A5D8T8; -.
DR SignaLink; A5D8T8; -.
DR BioGRID-ORCS; 348174; 13 hits in 942 CRISPR screens.
DR GenomeRNAi; 348174; -.
DR Pharos; A5D8T8; Tbio.
DR PRO; PR:A5D8T8; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; A5D8T8; protein.
DR Bgee; ENSG00000157322; Expressed in adult mammalian kidney and 88 other tissues.
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; 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; Disulfide bond; EGF-like domain;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; Lectin;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..446
FT /note="C-type lectin domain family 18 member A"
FT /id="PRO_0000324316"
FT DOMAIN 52..182
FT /note="SCP"
FT DOMAIN 228..261
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 306..433
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 236..249
FT /evidence="ECO:0000250"
FT DISULFID 251..260
FT /evidence="ECO:0000250"
FT DISULFID 327..432
FT /evidence="ECO:0000250"
FT DISULFID 408..424
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..340
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032204"
FT VAR_SEQ 341..371
FT /note="KVQDILAFYLGRLETTNEVIDSDFETRNFWI -> MGAASAGKRGQKGSWQQ
FT TPGSEWANLDYPGP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032205"
FT VARIANT 118
FT /note="V -> A (in allele CLEC18A-1; dbSNP:rs2549097)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:26170455,
FT ECO:0000269|Ref.1"
FT /id="VAR_059449"
FT VARIANT 151
FT /note="T -> M (in allele CLEC18A-1; dbSNP:rs75776403)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:26170455"
FT /id="VAR_074610"
FT VARIANT 339
FT /note="S -> R (in allele CLEC18A-1; abolishes binding to
FT polysaccharides)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:26170455"
FT /id="VAR_074611"
FT MUTAGEN 421
FT /note="D->N: Has a mild effect on polysaccharides binding."
FT /evidence="ECO:0000269|PubMed:26170455"
FT CONFLICT 273
FT /note="F -> L (in Ref. 4; AAH78143)"
FT /evidence="ECO:0000305"
FT CONFLICT 401..402
FT /note="DN -> AT (in Ref. 4; AAH08616)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="D -> N (in Ref. 4; AAH78143)"
FT /evidence="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
