TNXB

Protein identityUniProt · HPA

UniProt accession

P22105

Gene

TNXB

Ensembl

ENSG00000168477

Chromosome

6

Canonical length

4244 aa

Protein class

Disease related genes, Human disease related genes, Plasma proteins, Predicted intracellular proteins, Predicted secreted proteins

Subcellular location

Vesicles

Secretome location

Secreted to extracellular matrix

Quaternary structure

Homotrimer

OverviewNCBI Gene

This gene encodes a member of the tenascin family of extracellular matrix glycoproteins. The tenascins have anti-adhesive effects, as opposed to fibronectin which is adhesive. This protein is thought to function in matrix maturation during wound healing, and its deficiency has been associated with the connective tissue disorder Ehlers-Danlos syndrome. This gene localizes to the major histocompatibility complex (MHC) class III region on chromosome 6. It is one of four genes in this cluster which have been duplicated. The duplicated copy of this gene is incomplete and is a pseudogene which is transcribed but does not encode a protein. The structure of this gene is unusual in that it overlaps the CREBL1 and CYP21A2 genes at its 5' and 3' ends, respectively. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

4244 residues, UniProt reviewed canonical sequence.

>P22105|TNXB
     1  MMPAQYALTS SLVLLVLLST ARAGPFSSRS NVTLPAPRPP PQPGGHTVGA GVGSPSSQLY
    61  EHTVEGGEKQ VVFTHRINLP PSTGCGCPPG TEPPVLASEV QALRVRLEIL EELVKGLKEQ
   121  CTGGCCPASA QAGTGQTDVR TLCSLHGVFD LSRCTCSCEP GWGGPTCSDP TDAEIPPSSP
   181  PSASGSCPDD CNDQGRCVRG RCVCFPGYTG PSCGWPSCPG DCQGRGRCVQ GVCVCRAGFS
   241  GPDCSQRSCP RGCSQRGRCE GGRCVCDPGY TGDDCGMRSC PRGCSQRGRC ENGRCVCNPG
   301  YTGEDCGVRS CPRGCSQRGR CKDGRCVCDP GYTGEDCGTR SCPWDCGEGG RCVDGRCVCW
   361  PGYTGEDCST RTCPRDCRGR GRCEDGECIC DTGYSGDDCG VRSCPGDCNQ RGRCEDGRCV
   421  CWPGYTGTDC GSRACPRDCR GRGRCENGVC VCNAGYSGED CGVRSCPGDC RGRGRCESGR
   481  CMCWPGYTGR DCGTRACPGD CRGRGRCVDG RCVCNPGFTG EDCGSRRCPG DCRGHGLCED
   541  GVCVCDAGYS GEDCSTRSCP GGCRGRGQCL DGRCVCEDGY SGEDCGVRQC PNDCSQHGVC
   601  QDGVCICWEG YVSEDCSIRT CPSNCHGRGR CEEGRCLCDP GYTGPTCATR MCPADCRGRG
   661  RCVQGVCLCH VGYGGEDCGQ EEPPASACPG GCGPRELCRA GQCVCVEGFR GPDCAIQTCP
   721  GDCRGRGECH DGSCVCKDGY AGEDCGEEVP TIEGMRMHLL EETTVRTEWT PAPGPVDAYE
   781  IQFIPTTEGA SPPFTARVPS SASAYDQRGL APGQEYQVTV RALRGTSWGL PASKTITTMI
   841  DGPQDLRVVA VTPTTLELGW LRPQAEVDRF VVSYVSAGNQ RVRLEVPPEA DGTLLTDLMP
   901  GVEYVVTVTA ERGRAVSYPA SVRANTGSSP LGLLGTTDEP PPSGPSTTQG AQAPLLQQRP
   961  QELGELRVLG RDETGRLRVV WTAQPDTFAY FQLRMRVPEG PGAHEEVLPG DVRQALVPPP
  1021  PPGTPYELSL HGVPPGGKPS DPIIYQGIMD KDEEKPGKSS GPPRLGELTV TDRTSDSLLL
  1081  RWTVPEGEFD SFVIQYKDRD GQPQVVPVEG PQRSAVITSL DPGRKYKFVL YGFVGKKRHG
  1141  PLVAEAKILP QSDPSPGTPP HLGNLWVTDP TPDSLHLSWT VPEGQFDTFM VQYRDRDGRP
  1201  QVVPVEGPER SFVVSSLDPD HKYRFTLFGI ANKKRYGPLT ADGTTAPERK EEPPRPEFLE
  1261  QPLLGELTVT GVTPDSLRLS WTVAQGPFDS FMVQYKDAQG QPQAVPVAGD ENEVTVPGLD
  1321  PDRKYKMNLY GLRGRQRVGP ESVVAKTAPQ EDVDETPSPT ELGTEAPESP EEPLLGELTV
  1381  TGSSPDSLSL FWTVPQGSFD SFTVQYKDRD GRPRAVRVGG KESEVTVGGL EPGHKYKMHL
  1441  YGLHEGQRVG PVSAVGVTAP QQEETPPATE SPLEPRLGEL TVTDVTPNSV GLSWTVPEGQ
  1501  FDSFIVQYKD KDGQPQVVPV AADQREVTVY NLEPERKYKM NMYGLHDGQR MGPLSVVIVT
  1561  APLPPAPATE ASKPPLEPRL GELTVTDITP DSVGLSWTVP EGEFDSFVVQ YKDRDGQPQV
  1621  VPVAADQREV TIPDLEPSRK YKFLLFGIQD GKRRSPVSVE AKTVARGDAS PGAPPRLGEL
  1681  WVTDPTPDSL RLSWTVPEGQ FDSFVVQFKD KDGPQVVPVE GHERSVTVTP LDAGRKYRFL
  1741  LYGLLGKKRH GPLTADGTTE ARSAMDDTGT KRPPKPRLGE ELQVTTVTQN SVGLSWTVPE
  1801  GQFDSFVVQY KDRDGQPQVV PVEGSLREVS VPGLDPAHRY KLLLYGLHHG KRVGPISAVA
  1861  ITAGREETET ETTAPTPPAP EPHLGELTVE EATSHTLHLS WMVTEGEFDS FEIQYTDRDG
  1921  QLQMVRIGGD RNDITLSGLE SDHRYLVTLY GFSDGKHVGP VHVEALTVPE EEKPSEPPTA
  1981  TPEPPIKPRL GELTVTDATP DSLSLSWTVP EGQFDHFLVQ YRNGDGQPKA VRVPGHEEGV
  2041  TISGLEPDHK YKMNLYGFHG GQRMGPVSVV GVTAAEEETP SPTEPSMEAP EPAEEPLLGE
  2101  LTVTGSSPDS LSLSWTVPQG RFDSFTVQYK DRDGRPQVVR VGGEESEVTV GGLEPGRKYK
  2161  MHLYGLHEGR RVGPVSAVGV TAPEEESPDA PLAKLRLGQM TVRDITSDSL SLSWTVPEGQ
  2221  FDHFLVQFKN GDGQPKAVRV PGHEDGVTIS GLEPDHKYKM NLYGFHGGQR VGPVSAVGLT
  2281  APGKDEEMAP ASTEPPTPEP PIKPRLEELT VTDATPDSLS LSWTVPEGQF DHFLVQYKNG
  2341  DGQPKATRVP GHEDRVTISG LEPDNKYKMN LYGFHGGQRV GPVSAIGVTA AEEETPSPTE
  2401  PSMEAPEPPE EPLLGELTVT GSSPDSLSLS WTVPQGRFDS FTVQYKDRDG RPQVVRVGGE
  2461  ESEVTVGGLE PGRKYKMHLY GLHEGRRVGP VSTVGVTAPQ EDVDETPSPT EPGTEAPGPP
  2521  EEPLLGELTV TGSSPDSLSL SWTVPQGRFD SFTVQYKDRD GRPQAVRVGG QESKVTVRGL
  2581  EPGRKYKMHL YGLHEGRRLG PVSAVGVTED EAETTQAVPT MTPEPPIKPR LGELTMTDAT
  2641  PDSLSLSWTV PEGQFDHFLV QYRNGDGQPK AVRVPGHEDG VTISGLEPDH KYKMNLYGFH
  2701  GGQRVGPISV IGVTAAEEET PSPTELSTEA PEPPEEPLLG ELTVTGSSPD SLSLSWTIPQ
  2761  GHFDSFTVQY KDRDGRPQVM RVRGEESEVT VGGLEPGRKY KMHLYGLHEG RRVGPVSTVG
  2821  VTAPEDEAET TQAVPTTTPE PPNKPRLGEL TVTDATPDSL SLSWMVPEGQ FDHFLVQYRN
  2881  GDGQPKVVRV PGHEDGVTIS GLEPDHKYKM NLYGFHGGQR VGPISVIGVT AAEEETPAPT
  2941  EPSTEAPEPP EEPLLGELTV TGSSPDSLSL SWTIPQGRFD SFTVQYKDRD GRPQVVRVRG
  3001  EESEVTVGGL EPGCKYKMHL YGLHEGQRVG PVSAVGVTAP KDEAETTQAV PTMTPEPPIK
  3061  PRLGELTVTD ATPDSLSLSW MVPEGQFDHF LVQYRNGDGQ PKAVRVPGHE DGVTISGLEP
  3121  DHKYKMNLYG FHGGQRVGPV SAIGVTEEET PSPTEPSTEA PEAPEEPLLG ELTVTGSSPD
  3181  SLSLSWTVPQ GRFDSFTVQY KDRDGQPQVV RVRGEESEVT VGGLEPGRKY KMHLYGLHEG
  3241  QRVGPVSTVG ITAPLPTPLP VEPRLGELAV AAVTSDSVGL SWTVAQGPFD SFLVQYRDAQ
  3301  GQPQAVPVSG DLRAVAVSGL DPARKYKFLL FGLQNGKRHG PVPVEARTAP DTKPSPRLGE
  3361  LTVTDATPDS VGLSWTVPEG EFDSFVVQYK DKDGRLQVVP VAANQREVTV QGLEPSRKYR
  3421  FLLYGLSGRK RLGPISADST TAPLEKELPP HLGELTVAEE TSSSLRLSWT VAQGPFDSFV
  3481  VQYRDTDGQP RAVPVAADQR TVTVEDLEPG KKYKFLLYGL LGGKRLGPVS ALGMTAPEED
  3541  TPAPELAPEA PEPPEEPRLG VLTVTDTTPD SMRLSWSVAQ GPFDSFVVQY EDTNGQPQAL
  3601  LVDGDQSKIL ISGLEPSTPY RFLLYGLHEG KRLGPLSAEG TTGLAPAGQT SEESRPRLSQ
  3661  LSVTDVTTSS LRLNWEAPPG AFDSFLLRFG VPSPSTLEPH PRPLLQRELM VPGTRHSAVL
  3721  RDLRSGTLYS LTLYGLRGPH KADSIQGTAR TLSPVLESPR DLQFSEIRET SAKVNWMPPP
  3781  SRADSFKVSY QLADGGEPQS VQVDGQARTQ KLQGLIPGAR YEVTVVSVRG FEESEPLTGF
  3841  LTTVPDGPTQ LRALNLTEGF AVLHWKPPQN PVDTYDVQVT APGAPPLQAE TPGSAVDYPL
  3901  HDLVLHTNYT ATVRGLRGPN LTSPASITFT TGLEAPRDLE AKEVTPRTAL LTWTEPPVRP
  3961  AGYLLSFHTP GGQNQEILLP GGITSHQLLG LFPSTSYNAR LQAMWGQSLL PPVSTSFTTG
  4021  GLRIPFPRDC GEEMQNGAGA SRTSTIFLNG NRERPLNVFC DMETDGGGWL VFQRRMDGQT
  4081  DFWRDWEDYA HGFGNISGEF WLGNEALHSL TQAGDYSMRV DLRAGDEAVF AQYDSFHVDS
  4141  AAEYYRLHLE GYHGTAGDSM SYHSGSVFSA RDRDPNSLLI SCAVSYRGAW WYRNCHYANL
  4201  NGLYGSTVDH QGVSWYHWKG FEFSVPFTEM KLRPRNFRSP AGGG

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against TNXB can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Secreted

Secreted

Yes

Transmembrane segments

0

Mean surface accessibility (rSASA)

0

Highest tissue expression

253 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about TNXB.

Disease | AllUniProt

Conditions TNXB is implicated in, by any mechanism.

• Ehlers-Danlos syndrome, classic-like, 1 (EDSCLL1) MIM:606408
• Vesicoureteral reflux 8 (VUR8) MIM:615963

Disease | GeneticClinVar

149 pathogenic / likely-pathogenic of 3,744 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Ehlers-Danlos syndrome due to tenascin-X deficiency
• Vesicoureteral reflux 8
• Cardiovascular phenotype
• TNXB-related disorder
• Ehlers-Danlos syndrome

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.6

gnomAD pLI

0.02

gnomAD missense Z

0.04

DepMap mean gene effect

-0.08

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• actin cytoskeleton organization
• cell adhesion
• cell-cell adhesion
• cell-matrix adhesion
• collagen fibril organization
• collagen metabolic process
• elastic fiber assembly
• fatty acid metabolic process
• neuron projection development
• positive regulation of cell population proliferation
• positive regulation of collagen fibril organization
• positive regulation of epithelial to mesenchymal transition
• positive regulation of vascular endothelial growth factor signaling pathway
• regulation of cell adhesion
• regulation of cell differentiation
• regulation of cell migration
• regulation of JNK cascade
• triglyceride metabolic process
• positive regulation of cell fate determination

Molecular functions

• collagen binding
• collagen fibril binding
• extracellular matrix structural constituent
• heparin binding
• integrin binding

Cellular components

• extracellular exosome
• extracellular matrix
• extracellular region
• extracellular space
• tenascin complex

Protein domainsUniProt · Pfam · InterPro

• EGF-like domain
• Fibrinogen, alpha/beta/gamma chain, C-terminal globular domain
• Fibronectin type III
• Immunoglobulin-like fold
• Fibrinogen, alpha/beta/gamma chain, C-terminal globular, subdomain 1
• Fibrinogen, conserved site
• Fibrinogen-like, C-terminal
• Fibronectin type III superfamily
• Tenascin, EGF-like domain
• Extracellular Matrix Regulatory Proteins
• Fibronectin type III domain
• Fibrinogen beta and gamma chains, C-terminal globular domain
• Tenascin EGF domain
• Teneurin-like EGF domain
• Teneurin EGF domain

KeywordsUniProt

• Cell adhesion
• Coiled coil
• Disulfide bond
• EGF-like domain
• Ehlers-Danlos syndrome
• Extracellular matrix
• Glycoprotein
• Repeat
• Secreted
• Signal

InteractionsUniProt · HPA

Protein binding partners of TNXB in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• III