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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

  1. calcium ion binding Source: UniProtKB
  2. carbohydrate binding Source: UniProtKB-KW
  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
Complete GO annotation...

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: UniProtKB
  5. granular component Source: UniProtKB
Complete GO annotation...

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.
ExpressionAtlasiP05452. baseline.
GenevestigatoriP05452.

Organism-specific databases

HPAiCAB002582.
HPA034794.

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 – 734Combined sources
Beta strandi75 – 8915Combined sources
Helixi91 – 10010Combined sources
Beta strandi103 – 1053Combined sources
Helixi111 – 12414Combined sources
Beta strandi130 – 14011Combined sources
Beta strandi143 – 1464Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi157 – 1593Combined sources
Turni160 – 1623Combined sources
Beta strandi165 – 1673Combined sources
Helixi168 – 1703Combined sources
Beta strandi173 – 1775Combined sources
Turni178 – 1825Combined sources
Beta strandi183 – 1875Combined sources
Beta strandi193 – 2008Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00610000086061.
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

        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)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:
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.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:
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
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...

Protein-protein interaction databases

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

Chemistry

DrugBankiDB00031. Tenecteplase.

Polymorphism databases

DMDMi317373499.

Proteomic databases

MaxQBiP05452.
PaxDbiP05452.
PeptideAtlasiP05452.
PRIDEiP05452.

Protocols and materials databases

DNASUi7123.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7123.
GeneCardsiGC03P045043.
H-InvDBHIX0163464.
HGNCiHGNC:11891. CLEC3B.
HPAiCAB002582.
HPA034794.
MIMi187520. gene.
neXtProtiNX_P05452.
PharmGKBiPA36590.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG252273.
GeneTreeiENSGT00610000086061.
HOGENOMiHOG000060248.
HOVERGENiHBG108270.
InParanoidiP05452.
KOiK17520.
OMAiICQFAIV.
OrthoDBiEOG754HQT.
PhylomeDBiP05452.
TreeFamiTF330481.

Miscellaneous databases

ChiTaRSiCLEC3B. human.
EvolutionaryTraceiP05452.
GeneWikiiCLEC3B.
GenomeRNAii7123.
NextBioi27875.
PROiP05452.
SOURCEiSearch...

Gene expression databases

BgeeiP05452.
CleanExiHS_CLEC3B.
ExpressionAtlasiP05452. baseline.
GenevestigatoriP05452.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "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).
  11. "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: March 4, 2015
This is version 153 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

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 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.