ID   CLC3A_HUMAN             Reviewed;         197 AA.
AC   O75596; B2R8C4; Q3SX91; Q6UXF5;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   13-FEB-2019, entry version 132.
DE   RecName: Full=C-type lectin domain family 3 member A;
DE   AltName: Full=C-type lectin superfamily member 1;
DE   AltName: Full=Cartilage-derived C-type lectin;
DE   Flags: Precursor;
GN   Name=CLEC3A; Synonyms=CLECSF1; ORFNames=UNQ700/PRO1345;
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 [GENOMIC DNA].
RC   TISSUE=Cartilage;
RX   PubMed=10524194; DOI=10.1016/S0167-4781(99)00087-1;
RA   Neame P.J., Tapp H., Grimm D.R.;
RT   "The cartilage-derived, C-type lectin (CLECSF1): structure of the gene
RT   and chromosomal location.";
RL   Biochim. Biophys. Acta 1446:193-202(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-197.
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.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
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   [4]
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 23-48; 58-77 AND 152-163, CLEAVAGE OF INITIATOR
RP   METHIONINE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19173304; DOI=10.1002/jcb.22062;
RA   Tsunezumi J., Higashi S., Miyazaki K.;
RT   "Matrilysin (MMP-7) cleaves C-type lectin domain family 3 member A
RT   (CLEC3A) on tumor cell surface and modulates its cell adhesion
RT   activity.";
RL   J. Cell. Biochem. 106:693-702(2009).
CC   -!- FUNCTION: Promotes cell adhesion to laminin-332 and fibronectin.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19173304}.
CC   -!- TISSUE SPECIFICITY: Restricted to cartilage and breast. Also
CC       expressed in breast cancers. {ECO:0000269|PubMed:19173304}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ88742.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Cartilage C-Type lectin;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_258";
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; AF077345; AAD12542.1; -; Genomic_DNA.
DR   EMBL; AF077344; AAD12542.1; JOINED; Genomic_DNA.
DR   EMBL; AY358376; AAQ88742.1; ALT_INIT; mRNA.
DR   EMBL; AK313316; BAG36121.1; -; mRNA.
DR   EMBL; BC104415; AAI04416.1; -; mRNA.
DR   CCDS; CCDS10927.2; -.
DR   RefSeq; NP_005743.4; NM_005752.4.
DR   UniGene; Hs.177936; -.
DR   UniGene; Hs.735656; -.
DR   ProteinModelPortal; O75596; -.
DR   SMR; O75596; -.
DR   BioGrid; 115446; 49.
DR   STRING; 9606.ENSP00000460682; -.
DR   iPTMnet; O75596; -.
DR   PhosphoSitePlus; O75596; -.
DR   BioMuta; CLEC3A; -.
DR   PaxDb; O75596; -.
DR   PeptideAtlas; O75596; -.
DR   PRIDE; O75596; -.
DR   ProteomicsDB; 50105; -.
DR   Ensembl; ENST00000575655; ENSP00000460682; ENSG00000166509.
DR   GeneID; 10143; -.
DR   KEGG; hsa:10143; -.
DR   CTD; 10143; -.
DR   DisGeNET; 10143; -.
DR   GeneCards; CLEC3A; -.
DR   HGNC; HGNC:2052; CLEC3A.
DR   HPA; HPA051511; -.
DR   MIM; 613588; gene.
DR   neXtProt; NX_O75596; -.
DR   PharmGKB; PA26578; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   eggNOG; ENOG410XPJ1; LUCA.
DR   HOGENOM; HOG000060248; -.
DR   HOVERGEN; HBG108270; -.
DR   InParanoid; O75596; -.
DR   KO; K17519; -.
DR   OrthoDB; 1236353at2759; -.
DR   PhylomeDB; O75596; -.
DR   TreeFam; TF330481; -.
DR   GenomeRNAi; 10143; -.
DR   PRO; PR:O75596; -.
DR   Proteomes; UP000005640; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
DR   GO; GO:0001503; P:ossification; IBA:GO_Central.
DR   GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
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; IPR016187; CTDL_fold.
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   Complete proteome; Direct protein sequencing; Disulfide bond; Lectin;
KW   Polymorphism; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     22       {ECO:0000269|PubMed:19173304}.
FT   CHAIN        23    197       C-type lectin domain family 3 member A.
FT                                /FTId=PRO_0000017374.
FT   DOMAIN       74    192       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DISULFID     68     78       {ECO:0000255|PROSITE-ProRule:PRU00040}.
FT   DISULFID     95    191       {ECO:0000255|PROSITE-ProRule:PRU00040}.
FT   DISULFID    167    183       {ECO:0000255|PROSITE-ProRule:PRU00040}.
FT   VARIANT     197    197       Q -> K (in dbSNP:rs2072663).
FT                                {ECO:0000269|PubMed:12975309}.
FT                                /FTId=VAR_021259.
SQ   SEQUENCE   197 AA;  22233 MW;  BB924DBDDB7729A4 CRC64;
     MAKNGLVICI LVITLLLDQT TSHTSRLKAR KHSKRRVRDK DGDLKTQIEK LWTEVNALKE
     IQALQTVCLR GTKVHKKCYL ASEGLKHFHE ANEDCISKGG ILVIPRNSDE INALQDYGKR
     SLPGVNDFWL GINDMVTEGK FVDVNGIAIS FLNWDRAQPN GGKRENCVLF SQSAQGKWSD
     EACRSSKRYI CEFTIPQ
//