ID TETN_HUMAN Reviewed; 202 AA. AC P05452; Q6FGX6; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 3. DT 02-OCT-2024, entry version 215. DE RecName: Full=Tetranectin; DE Short=TN; DE AltName: Full=C-type lectin domain family 3 member B; DE AltName: Full=Plasminogen kringle 4-binding protein; DE Flags: Precursor; GN Name=CLEC3B; Synonyms=TNA; 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], AND VARIANT SER-106. RC TISSUE=Placenta; RX PubMed=1354271; RA Wewer U.M., Albrechtsen R.; RT "Tetranectin, a plasminogen kringle 4-binding protein. Cloning and gene RT expression pattern in human colon cancer."; RL Lab. Invest. 67:253-262(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-106. RX PubMed=1511740; DOI=10.1016/0014-5793(92)80729-z; RA Berglund L., Petersen T.E.; RT "The gene structure of tetranectin, a plasminogen binding protein."; RL FEBS Lett. 309:15-19(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-106. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-106. RC TISSUE=Lung; 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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36. RC TISSUE=Placenta; RA Sorensen C.B., Berglund L., Petersen T.E.; RT "Cloning and mapping of the murine tetranectin gene."; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [7] RP PROTEIN SEQUENCE OF 22-202, AND VARIANTS SER-55; MET-58 AND SER-106. RX PubMed=3427041; DOI=10.1021/bi00395a027; RA Fuhlendorff J., Clemmensen I., Magnusson S.; RT "Primary structure of tetranectin, a plasminogen kringle 4 binding plasma RT protein: homology with asialoglycoprotein receptors and cartilage RT proteoglycan core protein."; RL Biochemistry 26:6757-6764(1987). RN [8] RP PARTIAL PROTEIN SEQUENCE, AND MASS SPECTROMETRY. RC TISSUE=Plasma; RX PubMed=10614823; DOI=10.1515/bc.1999.166; RA Jaquinod M., Holtet T.L., Etzerodt M., Clemmensen I., Thoegersen H.C., RA Roepstorff P.; RT "Mass spectrometric characterisation of post-translational modification and RT genetic variation in human tetranectin."; RL Biol. Chem. 380:1307-1314(1999). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=9256258; DOI=10.1016/s0014-5793(97)00664-9; RA Nielsen B.B., Kastrup J.S., Rasmussen H., Holtet T.L., Graversen J.H., RA Etzerodt M., Thoegersen H.C., Larsen I.K.; RT "Crystal structure of tetranectin, a trimeric plasminogen-binding protein RT with an alpha-helical coiled coil."; RL FEBS Lett. 412:388-396(1997). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 66-202. RX PubMed=9757090; DOI=10.1107/s0907444997016806; RA Kastrup J.S., Nielsen B.B., Rasmussen H., Holtet T.L., Graversen J.H., RA Etzerodt M., Thoegersen H.C., Larsen I.K.; RT "Structure of the C-type lectin carbohydrate recognition domain of human RT tetranectin."; RL Acta Crystallogr. D 54:757-766(1998). RN [12] RP INVOLVEMENT IN MCDR4, VARIANT MCDR4 ASP-180, AND FUNCTION. RX PubMed=35331648; DOI=10.1016/j.gim.2022.02.012; RA Zhou R., Mawatari G., Cai X.B., Shen R.J., Wang Y.H., Wang Y.T., Guo Y.M., RA Guo F.Y., Yuan J., Pan D., Nao-I N., Jin Z.B.; RT "CLEC3B is a novel causative gene for macular-retinal dystrophy."; RL Genet. Med. 24:1249-1260(2022). CC -!- FUNCTION: Tetranectin binds to plasminogen and to isolated kringle 4. CC May be involved in the packaging of molecules destined for exocytosis. CC Plays a role in retinal function (PubMed:35331648). CC {ECO:0000269|PubMed:35331648}. CC -!- SUBUNIT: Homotrimer. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Found in plasma. CC -!- MASS SPECTROMETRY: Mass=20535.8; Mass_error=2.4; Method=Electrospray; CC Evidence={ECO:0000269|PubMed:10614823}; CC -!- DISEASE: Macular dystrophy, retinal, 4 (MCDR4) [MIM:619977]: An CC autosomal dominant retinal disease characterized by late-onset macular CC degeneration, with multiple drusen-like deposits, macular geographic CC atrophy, and choroidal neovascularization. Patients also exhibit CC extensive retinal dysfunction with impaired rod function. CC {ECO:0000269|PubMed:35331648}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=Tetranectin; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_260"; 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; X64559; CAA45860.1; -; mRNA. DR EMBL; X70910; CAA50265.1; -; Genomic_DNA. DR EMBL; X70911; CAA50265.1; JOINED; Genomic_DNA. DR EMBL; X70912; CAA50265.1; JOINED; Genomic_DNA. DR EMBL; CR541981; CAG46778.1; -; mRNA. DR EMBL; CR542009; CAG46806.1; -; mRNA. DR EMBL; AC104165; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC011024; AAH11024.1; -; mRNA. DR EMBL; X98121; CAA66803.1; -; Genomic_DNA. DR CCDS; CCDS2726.1; -. DR PIR; S24126; TTHUN. DR RefSeq; NP_003269.2; NM_003278.2. DR PDB; 1HTN; X-ray; 2.80 A; A=22-202. DR PDB; 1RJH; NMR; -; A=85-202. DR PDB; 1TN3; X-ray; 2.00 A; A=66-202. DR PDB; 3L9J; X-ray; 2.10 A; C=67-201. DR PDBsum; 1HTN; -. DR PDBsum; 1RJH; -. DR PDBsum; 1TN3; -. DR PDBsum; 3L9J; -. DR AlphaFoldDB; P05452; -. DR SMR; P05452; -. DR BioGRID; 112978; 20. DR IntAct; P05452; 10. DR MINT; P05452; -. DR STRING; 9606.ENSP00000296130; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB06245; Lanoteplase. DR DrugBank; DB00031; Tenecteplase. DR UniLectin; P05452; -. DR GlyCosmos; P05452; 1 site, No reported glycans. DR GlyGen; P05452; 1 site. DR BioMuta; CLEC3B; -. DR DMDM; 317373499; -. DR jPOST; P05452; -. DR MassIVE; P05452; -. DR PaxDb; 9606-ENSP00000296130; -. DR PeptideAtlas; P05452; -. DR ProteomicsDB; 51840; -. DR Antibodypedia; 29547; 425 antibodies from 34 providers. DR DNASU; 7123; -. DR Ensembl; ENST00000296130.5; ENSP00000296130.4; ENSG00000163815.6. DR GeneID; 7123; -. DR KEGG; hsa:7123; -. DR MANE-Select; ENST00000296130.5; ENSP00000296130.4; NM_003278.3; NP_003269.2. DR UCSC; uc003cok.5; human. DR AGR; HGNC:11891; -. DR CTD; 7123; -. DR DisGeNET; 7123; -. DR GeneCards; CLEC3B; -. DR HGNC; HGNC:11891; CLEC3B. DR HPA; ENSG00000163815; Tissue enhanced (adipose). DR MalaCards; CLEC3B; -. DR MIM; 187520; gene. DR MIM; 619977; phenotype. DR neXtProt; NX_P05452; -. DR OpenTargets; ENSG00000163815; -. DR PharmGKB; PA36590; -. DR VEuPathDB; HostDB:ENSG00000163815; -. DR eggNOG; KOG4297; Eukaryota. DR GeneTree; ENSGT00950000183186; -. DR InParanoid; P05452; -. DR OMA; DGHWVDQ; -. DR OrthoDB; 3028705at2759; -. DR PhylomeDB; P05452; -. DR TreeFam; TF330481; -. DR PathwayCommons; P05452; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR SignaLink; P05452; -. DR BioGRID-ORCS; 7123; 18 hits in 1155 CRISPR screens. DR ChiTaRS; CLEC3B; human. DR EvolutionaryTrace; P05452; -. DR GeneWiki; CLEC3B; -. DR GenomeRNAi; 7123; -. DR Pharos; P05452; Tbio. DR PRO; PR:P05452; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P05452; protein. DR Bgee; ENSG00000163815; Expressed in subcutaneous adipose tissue and 101 other cell types or tissues. DR ExpressionAtlas; P05452; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0001652; C:granular component; IDA:UniProtKB. DR GO; GO:0031089; C:platelet dense granule lumen; TAS:Reactome. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0008201; F:heparin binding; IDA:UniProtKB. DR GO; GO:0036143; F:kringle domain binding; IPI:UniProtKB. DR GO; GO:0030282; P:bone mineralization; IDA:UniProtKB. DR GO; GO:0001503; P:ossification; IEP:UniProtKB. DR GO; GO:0010756; P:positive regulation of plasminogen activation; ISS:UniProtKB. DR CDD; cd03596; CLECT_tetranectin_like; 1. DR DisProt; DP02801; -. DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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; IPR051663; CLec_Tetranectin-domain. DR InterPro; IPR016187; CTDL_fold. DR PANTHER; PTHR22799:SF3; TETRANECTIN; 1. DR PANTHER; PTHR22799; TETRANECTIN-RELATED; 1. DR Pfam; PF00059; Lectin_C; 1. DR PRINTS; PR01504; PNCREATITSAP. DR SMART; SM00034; CLECT; 1. DR SUPFAM; SSF56436; C-type lectin-like; 1. DR SUPFAM; SSF57944; Triple coiled coil domain of C-type lectins; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disease variant; Disulfide bond; KW Glycoprotein; Lectin; Proteomics identification; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000269|PubMed:3427041" FT CHAIN 22..202 FT /note="Tetranectin" FT /evidence="ECO:0000269|PubMed:1354271" FT /id="PRO_0000017471" FT DOMAIN 77..198 FT /note="C-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT CARBOHYD 25 FT /note="O-linked (GalNAc...) threonine" FT DISULFID 71..81 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040, FT ECO:0000269|PubMed:3427041" FT DISULFID 98..197 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040, FT ECO:0000269|PubMed:3427041" FT DISULFID 173..189 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040, FT ECO:0000269|PubMed:3427041" FT VARIANT 55 FT /note="A -> S" FT /evidence="ECO:0000269|PubMed:3427041" FT /id="VAR_004189" FT VARIANT 58 FT /note="V -> M" FT /evidence="ECO:0000269|PubMed:3427041" FT /id="VAR_004190" FT VARIANT 106 FT /note="G -> S (in dbSNP:rs13963)" FT /evidence="ECO:0000269|PubMed:1354271, FT ECO:0000269|PubMed:1511740, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:3427041, ECO:0000269|Ref.3" FT /id="VAR_012318" FT VARIANT 180 FT /note="A -> D (in MCDR4; leads to thinning in both the FT outer nuclear layer and whole retina and to impaired FT retinal function, when tested in a heterologous system)" FT /evidence="ECO:0000269|PubMed:35331648" FT /id="VAR_087508" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:1TN3" FT STRAND 75..89 FT /evidence="ECO:0007829|PDB:1TN3" FT HELIX 91..100 FT /evidence="ECO:0007829|PDB:1TN3" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:1RJH" FT HELIX 111..124 FT /evidence="ECO:0007829|PDB:1TN3" FT STRAND 130..140 FT /evidence="ECO:0007829|PDB:1TN3" FT STRAND 143..146 FT /evidence="ECO:0007829|PDB:1TN3" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:3L9J" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:1RJH" FT TURN 160..162 FT /evidence="ECO:0007829|PDB:1TN3" FT STRAND 165..167 FT /evidence="ECO:0007829|PDB:1RJH" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:1TN3" FT STRAND 173..177 FT /evidence="ECO:0007829|PDB:1TN3" FT TURN 178..182 FT /evidence="ECO:0007829|PDB:1TN3" FT STRAND 183..187 FT /evidence="ECO:0007829|PDB:1TN3" FT STRAND 193..200 FT /evidence="ECO:0007829|PDB:1TN3" SQ SEQUENCE 202 AA; 22537 MW; 370C174033F21B78 CRC64; MELWGAYLLL CLFSLLTQVT TEPPTQKPKK IVNAKKDVVN TKMFEELKSR LDTLAQEVAL LKEQQALQTV CLKGTKVHMK CFLAFTQTKT FHEASEDCIS RGGTLGTPQT GSENDALYEY LRQSVGNEAE IWLGLNDMAA EGTWVDMTGA RIAYKNWETE ITAQPDGGKT ENCAVLSGAA NGKWFDKRCR DQLPYICQFG IV //