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Protein

Tetranectin

Gene

CLEC3B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • carbohydrate binding Source: UniProtKB-KW
  • heparin binding Source: UniProtKB
  • kringle domain binding Source: UniProtKB

GO - Biological processi

  • bone mineralization Source: UniProtKB
  • cellular response to organic substance Source: UniProtKB
  • cellular response to transforming growth factor beta stimulus Source: UniProtKB
  • ossification Source: UniProtKB
  • platelet degranulation Source: Reactome
  • positive regulation of plasminogen activation Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Lectin

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163815-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:11891. CLEC3B.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • granular component Source: UniProtKB
  • platelet dense granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi7123.
OpenTargetsiENSG00000163815.
PharmGKBiPA36590.

Chemistry databases

DrugBankiDB00031. Tenecteplase.

Polymorphism and mutation databases

BioMutaiCLEC3B.
DMDMi317373499.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000001747122 – 202Tetranectin1 PublicationAdd BLAST181

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi25O-linked (GalNAc...)1
Disulfide bondi71 ↔ 81PROSITE-ProRule annotation1 Publication
Disulfide bondi98 ↔ 197PROSITE-ProRule annotation1 Publication
Disulfide bondi173 ↔ 189PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP05452.
PaxDbiP05452.
PeptideAtlasiP05452.
PRIDEiP05452.

Expressioni

Tissue specificityi

Found in plasma.

Gene expression databases

BgeeiENSG00000163815.
CleanExiHS_CLEC3B.
ExpressionAtlasiP05452. baseline and differential.
GenevisibleiP05452. HS.

Organism-specific databases

HPAiCAB002582.
HPA034794.

Interactioni

Subunit structurei

Homotrimer.

GO - Molecular functioni

  • kringle domain binding Source: UniProtKB

Protein-protein interaction databases

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

Structurei

Secondary structure

1202
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi70 – 73Combined sources4
Beta strandi75 – 89Combined sources15
Helixi91 – 100Combined sources10
Beta strandi103 – 105Combined sources3
Helixi111 – 124Combined sources14
Beta strandi130 – 140Combined sources11
Beta strandi143 – 146Combined sources4
Beta strandi149 – 151Combined sources3
Beta strandi157 – 159Combined sources3
Turni160 – 162Combined sources3
Beta strandi165 – 167Combined sources3
Helixi168 – 170Combined sources3
Beta strandi173 – 177Combined sources5
Turni178 – 182Combined sources5
Beta strandi183 – 187Combined sources5
Beta strandi193 – 200Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP05452.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini77 – 198C-type lectinPROSITE-ProRule annotationAdd BLAST122

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IS3U. Eukaryota.
ENOG4111IV3. LUCA.
GeneTreeiENSGT00610000086061.
HOGENOMiHOG000060248.
HOVERGENiHBG108270.
InParanoidiP05452.
KOiK17520.
OMAiGKAENCA.
OrthoDBiEOG091G0NMQ.
PhylomeDBiP05452.
TreeFamiTF330481.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_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

        10         20         30         40         50
MELWGAYLLL CLFSLLTQVT TEPPTQKPKK IVNAKKDVVN TKMFEELKSR
60 70 80 90 100
LDTLAQEVAL LKEQQALQTV CLKGTKVHMK CFLAFTQTKT FHEASEDCIS
110 120 130 140 150
RGGTLGTPQT GSENDALYEY LRQSVGNEAE IWLGLNDMAA EGTWVDMTGA
160 170 180 190 200
RIAYKNWETE ITAQPDGGKT ENCAVLSGAA NGKWFDKRCR DQLPYICQFG

IV
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_00418955A → S.1 Publication1
Natural variantiVAR_00419058V → M.1 Publication1
Natural variantiVAR_012318106G → S.5 PublicationsCorresponds to variant rs13963dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Tetranectin

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry databases

DrugBankiDB00031. Tenecteplase.

Polymorphism and mutation databases

BioMutaiCLEC3B.
DMDMi317373499.

Proteomic databases

EPDiP05452.
PaxDbiP05452.
PeptideAtlasiP05452.
PRIDEiP05452.

Protocols and materials databases

DNASUi7123.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296130; ENSP00000296130; ENSG00000163815.
GeneIDi7123.
KEGGihsa:7123.
UCSCiuc003cok.5. human.

Organism-specific databases

CTDi7123.
DisGeNETi7123.
GeneCardsiCLEC3B.
H-InvDBHIX0163464.
HGNCiHGNC:11891. CLEC3B.
HPAiCAB002582.
HPA034794.
MIMi187520. gene.
neXtProtiNX_P05452.
OpenTargetsiENSG00000163815.
PharmGKBiPA36590.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IS3U. Eukaryota.
ENOG4111IV3. LUCA.
GeneTreeiENSGT00610000086061.
HOGENOMiHOG000060248.
HOVERGENiHBG108270.
InParanoidiP05452.
KOiK17520.
OMAiGKAENCA.
OrthoDBiEOG091G0NMQ.
PhylomeDBiP05452.
TreeFamiTF330481.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163815-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.

Miscellaneous databases

ChiTaRSiCLEC3B. human.
EvolutionaryTraceiP05452.
GeneWikiiCLEC3B.
GenomeRNAii7123.
PROiP05452.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163815.
CleanExiHS_CLEC3B.
ExpressionAtlasiP05452. baseline and differential.
GenevisibleiP05452. HS.

Family and domain databases

Gene3Di3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin-like.
IPR016186. C-type_lectin-like/link.
IPR018378. C-type_lectin_CS.
IPR016187. CTDL_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]
ProtoNetiSearch...

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: November 30, 2016
This is version 168 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.