TETN_HUMAN
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 03-AUG-2022, entry version 203.
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).
CC -!- FUNCTION: Tetranectin binds to plasminogen and to isolated kringle 4.
CC May be involved in the packaging of molecules destined for exocytosis.
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 -!- 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";
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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; 17.
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 GlyGen; P05452; 1 site.
DR BioMuta; CLEC3B; -.
DR DMDM; 317373499; -.
DR jPOST; P05452; -.
DR MassIVE; P05452; -.
DR PaxDb; P05452; -.
DR PeptideAtlas; P05452; -.
DR PRIDE; P05452; -.
DR ProteomicsDB; 51840; -.
DR Antibodypedia; 29547; 388 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 CTD; 7123; -.
DR DisGeNET; 7123; -.
DR GeneCards; CLEC3B; -.
DR HGNC; HGNC:11891; CLEC3B.
DR HPA; ENSG00000163815; Low tissue specificity.
DR MIM; 187520; gene.
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; ICQFAIV; -.
DR OrthoDB; 1236353at2759; -.
DR PhylomeDB; P05452; -.
DR TreeFam; TF330481; -.
DR PathwayCommons; P05452; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; P05452; -.
DR BioGRID-ORCS; 7123; 17 hits in 1068 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 100 other tissues.
DR ExpressionAtlas; P05452; baseline and differential.
DR Genevisible; P05452; HS.
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:0071310; P:cellular response to organic substance; IEP:UniProtKB.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB.
DR GO; GO:0001503; P:ossification; IEP:UniProtKB.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; ISS:UniProtKB.
DR DisProt; DP02801; -.
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 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Lectin; Reference proteome; 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 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
