CLC3A_HUMAN
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 03-AUG-2022, entry version 152.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 and
RT 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., 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=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., 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 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 [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 (CLEC3A)
RT on tumor cell surface and modulates its cell adhesion 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 expressed
CC in breast cancers. {ECO:0000269|PubMed:19173304}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ88742.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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 AlphaFoldDB; O75596; -.
DR SMR; O75596; -.
DR BioGRID; 115446; 51.
DR IntAct; O75596; 42.
DR STRING; 9606.ENSP00000299642; -.
DR iPTMnet; O75596; -.
DR PhosphoSitePlus; O75596; -.
DR BioMuta; CLEC3A; -.
DR MassIVE; O75596; -.
DR PaxDb; O75596; -.
DR PeptideAtlas; O75596; -.
DR PRIDE; O75596; -.
DR ProteomicsDB; 50105; -.
DR Antibodypedia; 30410; 61 antibodies from 13 providers.
DR DNASU; 10143; -.
DR Ensembl; ENST00000299642.10; ENSP00000299642.5; ENSG00000166509.12.
DR GeneID; 10143; -.
DR KEGG; hsa:10143; -.
DR MANE-Select; ENST00000299642.10; ENSP00000299642.5; NM_005752.6; NP_005743.5.
DR CTD; 10143; -.
DR DisGeNET; 10143; -.
DR GeneCards; CLEC3A; -.
DR HGNC; HGNC:2052; CLEC3A.
DR HPA; ENSG00000166509; Tissue enhanced (brain, breast, urinary bladder).
DR MIM; 613588; gene.
DR neXtProt; NX_O75596; -.
DR OpenTargets; ENSG00000166509; -.
DR PharmGKB; PA26578; -.
DR VEuPathDB; HostDB:ENSG00000166509; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00950000183186; -.
DR InParanoid; O75596; -.
DR OMA; WIGVADI; -.
DR OrthoDB; 1236353at2759; -.
DR PhylomeDB; O75596; -.
DR TreeFam; TF330481; -.
DR PathwayCommons; O75596; -.
DR SignaLink; O75596; -.
DR BioGRID-ORCS; 10143; 9 hits in 1057 CRISPR screens.
DR GenomeRNAi; 10143; -.
DR Pharos; O75596; Tdark.
DR PRO; PR:O75596; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O75596; protein.
DR Bgee; ENSG00000166509; Expressed in tibia and 57 other tissues.
DR ExpressionAtlas; O75596; baseline and differential.
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 Direct protein sequencing; Disulfide bond; Lectin; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:19173304"
FT CHAIN 23..197
FT /note="C-type lectin domain family 3 member A"
FT /id="PRO_0000017374"
FT DOMAIN 74..192
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 68..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 95..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 167..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VARIANT 197
FT /note="Q -> K (in dbSNP:rs2072663)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="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
