GenomeNet

Database: UniProt
Entry: A5D8T8
LinkDB: A5D8T8
Original site: A5D8T8 
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   10-APR-2019, entry version 103.
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};
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.ENSP00000484176; -.
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
//
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