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P05452

- TETN_HUMAN

UniProt

P05452 - TETN_HUMAN

Protein

Tetranectin

Gene

CLEC3B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis.

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. carbohydrate binding Source: InterPro
    3. heparin binding Source: UniProtKB
    4. kringle domain binding Source: UniProtKB

    GO - Biological processi

    1. bone mineralization Source: UniProtKB
    2. cellular response to organic substance Source: UniProtKB
    3. cellular response to transforming growth factor beta stimulus Source: UniProtKB
    4. ossification Source: UniProtKB
    5. positive regulation of plasminogen activation Source: UniProtKB
    6. skeletal system development Source: Ensembl

    Keywords - Ligandi

    Lectin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tetranectin
    Short name:
    TN
    Alternative name(s):
    C-type lectin domain family 3 member B
    Plasminogen kringle 4-binding protein
    Gene namesi
    Name:CLEC3B
    Synonyms:TNA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:11891. CLEC3B.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. granular component Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36590.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 21211 PublicationAdd
    BLAST
    Chaini22 – 202181Tetranectin1 PublicationPRO_0000017471Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi25 – 251O-linked (GalNAc...)
    Disulfide bondi71 ↔ 811 PublicationPROSITE-ProRule annotation
    Disulfide bondi98 ↔ 1971 PublicationPROSITE-ProRule annotation
    Disulfide bondi173 ↔ 1891 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP05452.
    PaxDbiP05452.
    PeptideAtlasiP05452.
    PRIDEiP05452.

    Expressioni

    Tissue specificityi

    Found in plasma.

    Gene expression databases

    BgeeiP05452.
    CleanExiHS_CLEC3B.
    GenevestigatoriP05452.

    Organism-specific databases

    HPAiCAB002582.

    Interactioni

    Subunit structurei

    Homotrimer.

    Protein-protein interaction databases

    BioGridi112978. 15 interactions.
    IntActiP05452. 8 interactions.
    MINTiMINT-8247353.
    STRINGi9606.ENSP00000296130.

    Structurei

    Secondary structure

    1
    202
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi70 – 734
    Beta strandi75 – 8915
    Helixi91 – 10010
    Beta strandi103 – 1053
    Helixi111 – 12414
    Beta strandi130 – 14011
    Beta strandi143 – 1464
    Beta strandi149 – 1513
    Beta strandi157 – 1593
    Turni160 – 1623
    Beta strandi165 – 1673
    Helixi168 – 1703
    Beta strandi173 – 1775
    Turni178 – 1825
    Beta strandi183 – 1875
    Beta strandi193 – 2008

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HTNX-ray2.80A22-202[»]
    1RJHNMR-A85-202[»]
    1TN3X-ray2.00A66-202[»]
    3L9JX-ray2.10C67-201[»]
    ProteinModelPortaliP05452.
    SMRiP05452. Positions 66-202.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05452.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini77 – 198122C-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG252273.
    HOGENOMiHOG000060248.
    HOVERGENiHBG108270.
    InParanoidiP05452.
    KOiK17520.
    OMAiICQFAIV.
    OrthoDBiEOG754HQT.
    PhylomeDBiP05452.
    TreeFamiTF330481.

    Family and domain databases

    Gene3Di3.10.100.10. 1 hit.
    InterProiIPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    [Graphical view]
    PfamiPF00059. Lectin_C. 1 hit.
    [Graphical view]
    SMARTiSM00034. CLECT. 1 hit.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 1 hit.
    PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P05452-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELWGAYLLL CLFSLLTQVT TEPPTQKPKK IVNAKKDVVN TKMFEELKSR    50
    LDTLAQEVAL LKEQQALQTV CLKGTKVHMK CFLAFTQTKT FHEASEDCIS 100
    RGGTLGTPQT GSENDALYEY LRQSVGNEAE IWLGLNDMAA EGTWVDMTGA 150
    RIAYKNWETE ITAQPDGGKT ENCAVLSGAA NGKWFDKRCR DQLPYICQFG 200
    IV 202
    Length:202
    Mass (Da):22,537
    Last modified:January 11, 2011 - v3
    Checksum:i370C174033F21B78
    GO

    Mass spectrometryi

    Molecular mass is 20535.8±2.4 Da from positions 22 - 202. Determined by ESI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551A → S.1 Publication
    VAR_004189
    Natural varianti58 – 581V → M.1 Publication
    VAR_004190
    Natural varianti106 – 1061G → S.5 Publications
    Corresponds to variant rs13963 [ dbSNP | Ensembl ].
    VAR_012318

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64559 mRNA. Translation: CAA45860.1.
    X70910, X70911, X70912 Genomic DNA. Translation: CAA50265.1.
    CR541981 mRNA. Translation: CAG46778.1.
    CR542009 mRNA. Translation: CAG46806.1.
    AC104165 Genomic DNA. No translation available.
    BC011024 mRNA. Translation: AAH11024.1.
    X98121 Genomic DNA. Translation: CAA66803.1.
    CCDSiCCDS2726.1.
    PIRiS24126. TTHUN.
    RefSeqiNP_003269.2. NM_003278.2.
    UniGeneiHs.476092.

    Genome annotation databases

    EnsembliENST00000296130; ENSP00000296130; ENSG00000163815.
    GeneIDi7123.
    KEGGihsa:7123.
    UCSCiuc003cok.4. human.

    Polymorphism databases

    DMDMi317373499.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    Tetranectin

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64559 mRNA. Translation: CAA45860.1 .
    X70910 , X70911 , X70912 Genomic DNA. Translation: CAA50265.1 .
    CR541981 mRNA. Translation: CAG46778.1 .
    CR542009 mRNA. Translation: CAG46806.1 .
    AC104165 Genomic DNA. No translation available.
    BC011024 mRNA. Translation: AAH11024.1 .
    X98121 Genomic DNA. Translation: CAA66803.1 .
    CCDSi CCDS2726.1.
    PIRi S24126. TTHUN.
    RefSeqi NP_003269.2. NM_003278.2.
    UniGenei Hs.476092.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HTN X-ray 2.80 A 22-202 [» ]
    1RJH NMR - A 85-202 [» ]
    1TN3 X-ray 2.00 A 66-202 [» ]
    3L9J X-ray 2.10 C 67-201 [» ]
    ProteinModelPortali P05452.
    SMRi P05452. Positions 66-202.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112978. 15 interactions.
    IntActi P05452. 8 interactions.
    MINTi MINT-8247353.
    STRINGi 9606.ENSP00000296130.

    Chemistry

    DrugBanki DB00009. Alteplase.
    DB00029. Anistreplase.
    DB00015. Reteplase.
    DB00031. Tenecteplase.

    Polymorphism databases

    DMDMi 317373499.

    Proteomic databases

    MaxQBi P05452.
    PaxDbi P05452.
    PeptideAtlasi P05452.
    PRIDEi P05452.

    Protocols and materials databases

    DNASUi 7123.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296130 ; ENSP00000296130 ; ENSG00000163815 .
    GeneIDi 7123.
    KEGGi hsa:7123.
    UCSCi uc003cok.4. human.

    Organism-specific databases

    CTDi 7123.
    GeneCardsi GC03P045043.
    H-InvDB HIX0163464.
    HGNCi HGNC:11891. CLEC3B.
    HPAi CAB002582.
    MIMi 187520. gene.
    neXtProti NX_P05452.
    PharmGKBi PA36590.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG252273.
    HOGENOMi HOG000060248.
    HOVERGENi HBG108270.
    InParanoidi P05452.
    KOi K17520.
    OMAi ICQFAIV.
    OrthoDBi EOG754HQT.
    PhylomeDBi P05452.
    TreeFami TF330481.

    Miscellaneous databases

    ChiTaRSi CLEC3B. human.
    EvolutionaryTracei P05452.
    GeneWikii CLEC3B.
    GenomeRNAii 7123.
    NextBioi 27875.
    PROi P05452.
    SOURCEi Search...

    Gene expression databases

    Bgeei P05452.
    CleanExi HS_CLEC3B.
    Genevestigatori P05452.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi IPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    [Graphical view ]
    Pfami PF00059. Lectin_C. 1 hit.
    [Graphical view ]
    SMARTi SM00034. CLECT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    PROSITEi PS00615. C_TYPE_LECTIN_1. 1 hit.
    PS50041. C_TYPE_LECTIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Tetranectin, a plasminogen kringle 4-binding protein. Cloning and gene expression pattern in human colon cancer."
      Wewer U.M., Albrechtsen R.
      Lab. Invest. 67:253-262(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-106.
      Tissue: Placenta.
    2. "The gene structure of tetranectin, a plasminogen binding protein."
      Berglund L., Petersen T.E.
      FEBS Lett. 309:15-19(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-106.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-106.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-106.
      Tissue: Lung.
    6. "Cloning and mapping of the murine tetranectin gene."
      Sorensen C.B., Berglund L., Petersen T.E.
      Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
      Tissue: Placenta.
    7. "Primary structure of tetranectin, a plasminogen kringle 4 binding plasma protein: homology with asialoglycoprotein receptors and cartilage proteoglycan core protein."
      Fuhlendorff J., Clemmensen I., Magnusson S.
      Biochemistry 26:6757-6764(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 22-202, VARIANTS SER-55; MET-58 AND SER-106.
    8. "Mass spectrometric characterisation of post-translational modification and genetic variation in human tetranectin."
      Jaquinod M., Holtet T.L., Etzerodt M., Clemmensen I., Thoegersen H.C., Roepstorff P.
      Biol. Chem. 380:1307-1314(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY.
      Tissue: Plasma.
    9. "Crystal structure of tetranectin, a trimeric plasminogen-binding protein with an alpha-helical coiled coil."
      Nielsen B.B., Kastrup J.S., Rasmussen H., Holtet T.L., Graversen J.H., Etzerodt M., Thoegersen H.C., Larsen I.K.
      FEBS Lett. 412:388-396(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    10. "Structure of the C-type lectin carbohydrate recognition domain of human tetranectin."
      Kastrup J.S., Nielsen B.B., Rasmussen H., Holtet T.L., Graversen J.H., Etzerodt M., Thoegersen H.C., Larsen I.K.
      Acta Crystallogr. D 54:757-766(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 66-202.

    Entry informationi

    Entry nameiTETN_HUMAN
    AccessioniPrimary (citable) accession number: P05452
    Secondary accession number(s): Q6FGX6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 149 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3