CLEC3B

Protein-coding gene in the species Homo sapiens

CLEC3B
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1HTN, 1RJH, 1TN3, 3L9J

Identifiers
AliasesCLEC3B, TN, TNA, C-type lectin domain family 3 member B
External IDsOMIM: 187520; MGI: 104540; HomoloGene: 31145; GeneCards: CLEC3B; OMA:CLEC3B - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for CLEC3B
Genomic location for CLEC3B
Band3p21.31Start45,001,548 bp[1]
End45,036,071 bp[1]
Gene location (Mouse)
Chromosome 9 (mouse)
Chr.Chromosome 9 (mouse)[2]
Chromosome 9 (mouse)
Genomic location for CLEC3B
Genomic location for CLEC3B
Band9 F4|9 73.91 cMStart122,980,011 bp[2]
End122,986,497 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • subcutaneous adipose tissue

  • apex of heart

  • right auricle

  • tibial nerve

  • right lung

  • placenta

  • spleen

  • right testis

  • right coronary artery

  • upper lobe of left lung
Top expressed in
  • lip

  • ankle

  • esophagus

  • muscle of thigh

  • skin of external ear

  • ankle joint

  • right lung

  • right lung lobe

  • intercostal muscle

  • left lung lobe
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • calcium ion binding
  • heparin binding
  • kringle domain binding
  • carbohydrate binding
Cellular component
  • cytoplasm
  • extracellular matrix
  • extracellular exosome
  • granular component
  • platelet dense granule lumen
  • extracellular space
  • extracellular region
  • collagen-containing extracellular matrix
Biological process
  • cellular response to organic substance
  • bone mineralization
  • cellular response to transforming growth factor beta stimulus
  • positive regulation of plasminogen activation
  • ossification
  • platelet degranulation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7123

21922

Ensembl

ENSG00000163815

ENSMUSG00000025784

UniProt

P05452

P43025
Q8CFZ6

RefSeq (mRNA)

NM_001308394
NM_003278

NM_011606

RefSeq (protein)

NP_001295323
NP_003269

NP_035736

Location (UCSC)Chr 3: 45 – 45.04 MbChr 9: 122.98 – 122.99 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Tetranectin is a protein that in humans is encoded by the CLEC3B gene.[5]


References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000163815 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025784 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: CLEC3B C-type lectin domain family 3, member B".

Further reading

  • Wewer UM, Albrechtsen R (1992). "Tetranectin, a plasminogen kringle 4-binding protein. Cloning and gene expression pattern in human colon cancer". Lab. Invest. 67 (2): 253–62. PMID 1354271.
  • Berglund L, Petersen TE (1992). "The gene structure of tetranectin, a plasminogen binding protein". FEBS Lett. 309 (1): 15–9. doi:10.1016/0014-5793(92)80729-Z. PMID 1511740. S2CID 35630722.
  • Borregaard N, Christensen L, Bejerrum OW, et al. (1990). "Identification of a highly mobilizable subset of human neutrophil intracellular vesicles that contains tetranectin and latent alkaline phosphatase". J. Clin. Invest. 85 (2): 408–16. doi:10.1172/JCI114453. PMC 296439. PMID 2298916.
  • Clemmensen I (1990). "Interaction of tetranectin with sulphated polysaccharides and trypan blue". Scand. J. Clin. Lab. Invest. 49 (8): 719–25. doi:10.3109/00365518909091550. PMID 2533389.
  • Clemmensen I, Petersen LC, Kluft C (1986). "Purification and characterization of a novel, oligomeric, plasminogen kringle 4 binding protein from human plasma: tetranectin". Eur. J. Biochem. 156 (2): 327–33. doi:10.1111/j.1432-1033.1986.tb09586.x. PMID 3009181.
  • Fuhlendorff J, Clemmensen I, Magnusson S (1988). "Primary structure of tetranectin, a plasminogen kringle 4 binding plasma protein: homology with asialoglycoprotein receptors and cartilage proteoglycan core protein". Biochemistry. 26 (21): 6757–64. doi:10.1021/bi00395a027. PMID 3427041.
  • Wewer UM, Ibaraki K, Schjørring P, et al. (1995). "A potential role for tetranectin in mineralization during osteogenesis". J. Cell Biol. 127 (6 Pt 1): 1767–75. doi:10.1083/jcb.127.6.1767. PMC 2120295. PMID 7798325.
  • Nielsen H, Clemmensen I, Kharazmi A (1993). "Tetranectin: a novel secretory protein from human monocytes". Scand. J. Immunol. 37 (1): 39–42. doi:10.1111/j.1365-3083.1993.tb01662.x. PMID 8418471. S2CID 6469331.
  • Durkin ME, Naylor SL, Albrechtsen R, Wewer UM (1997). "Assignment of the gene for human tetranectin (TNA) to chromosome 3p22→p21.3 by somatic cell hybrid mapping". Cytogenet. Cell Genet. 76 (1–2): 39–40. doi:10.1159/000134509. PMID 9154122.
  • Nielsen BB, Kastrup JS, Rasmussen H, et al. (1997). "Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an alpha-helical coiled coil". FEBS Lett. 412 (2): 388–96. doi:10.1016/S0014-5793(97)00664-9. PMID 9256258. S2CID 9290914.
  • Kastrup JS, Nielsen BB, Rasmussen H, et al. (1998). "Structure of the C-type lectin carbohydrate recognition domain of human tetranectin". Acta Crystallogr. D. 54 (Pt 5): 757–66. Bibcode:1998AcCrD..54..757K. doi:10.1107/S0907444997016806. PMID 9757090.
  • Jaquinod M, Holtet TL, Etzerodt M, et al. (2000). "Mass spectrometric characterisation of post-translational modification and genetic variation in human tetranectin". Biol. Chem. 380 (11): 1307–14. doi:10.1515/BC.1999.166. PMID 10614823. S2CID 9060086.
  • Lorentsen RH, Graversen JH, Caterer NR, et al. (2000). "The heparin-binding site in tetranectin is located in the N-terminal region and binding does not involve the carbohydrate recognition domain". Biochem. J. 347. Pt 1 (1): 83–7. doi:10.1042/0264-6021:3470083. PMC 1220934. PMID 10727405.
  • Graversen JH, Jacobsen C, Sigurskjold BW, et al. (2001). "Mutational analysis of affinity and selectivity of kringle-tetranectin interaction. Grafting novel kringle affinity ontp the trtranectin lectin scaffold". J. Biol. Chem. 275 (48): 37390–6. doi:10.1074/jbc.M004873200. PMID 10964919.
  • Arvanitis DL, Kamper EF, Kopeikina L, et al. (2002). "Tetranectin expression in gastric adenocarcinomas". Histol. Histopathol. 17 (2): 471–5. PMID 11962752.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Westergaard UB, Andersen MH, Heegaard CW, et al. (2003). "Tetranectin binds hepatocyte growth factor and tissue-type plasminogen activator". Eur. J. Biochem. 270 (8): 1850–4. doi:10.1046/j.1432-1033.2003.03549.x. PMID 12694198.
  • Anderson NL, Polanski M, Pieper R, et al. (2004). "The human plasma proteome: a nonredundant list developed by combination of four separate sources". Mol. Cell. Proteomics. 3 (4): 311–26. doi:10.1074/mcp.M300127-MCP200. PMID 14718574.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Hermann M, Pirkebner D, Draxl A, et al. (2005). "In the search of potential human islet stem cells: is tetranectin showing us the way?". Transplant. Proc. 37 (2): 1322–5. doi:10.1016/j.transproceed.2004.12.050. PMID 15848710.
  • v
  • t
  • e
  • 1htn: HUMAN TETRANECTIN, A TRIMERIC PLASMINOGEN BINDING PROTEIN WITH AN ALPHA-HELICAL COILED COIL
    1htn: HUMAN TETRANECTIN, A TRIMERIC PLASMINOGEN BINDING PROTEIN WITH AN ALPHA-HELICAL COILED COIL
  • 1rjh: Structure of the Calcium Free Form of the C-type Lectin-like Domain of Tetranectin
    1rjh: Structure of the Calcium Free Form of the C-type Lectin-like Domain of Tetranectin
  • 1tn3: THE C-TYPE LECTIN CARBOHYDRATE RECOGNITION DOMAIN OF HUMAN TETRANECTIN
    1tn3: THE C-TYPE LECTIN CARBOHYDRATE RECOGNITION DOMAIN OF HUMAN TETRANECTIN


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