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P22105 (TENX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tenascin-X

Short name=TN-X
Alternative name(s):
Hexabrachion-like protein
Gene names
Name:TNXB
Synonyms:HXBL, TNX, TNXB1, TNXB2, XB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length4289 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Appears to mediate interactions between cells and the extracellular matrix. Substrate-adhesion molecule that appears to inhibit cell migration. Accelerates collagen fibril formation. May play a role in supporting the growth of epithelial tumors. Ref.13

Subunit structure

Homotrimer. Interacts with type I, III and V collagens and tropoelastin via its 29th fibronectin type-III domain. Ref.9 Ref.13

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

Highly expressed in fetal adrenal, in fetal testis, fetal smooth, striated and cardiac muscle. Isoform XB-short is only expressed in the adrenal gland.

Developmental stage

Expression levels are lower in adults than in children. Ref.9

Involvement in disease

Tenascin-X deficiency (TNXD) [MIM:606408]: TNXD leads to an Ehlers-Danlos-like syndrome characterized by hyperextensible skin, hypermobile joints, and tissue fragility. Tenascin-X-deficient patients, however, lack atrophic scars, a major diagnostic criteria for classic Ehlers-Danlos. Delayed wound healing, which is also common in classic EDS, is only present in a subset of patients.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the tenascin family.

Contains 19 EGF-like domains.

Contains 1 fibrinogen C-terminal domain.

Contains 32 fibronectin type-III domains.

Caution

There are two genes for TN-X: TNXA and TNXB. TNXA is a partial gene which can sometimes recombine with TNXB.

Sequence caution

The sequence AAH33740.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAB89296.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI17414.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI17471.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI18078.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI18332.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAQ09268.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseEhlers-Danlos syndrome
   DomainCoiled coil
EGF-like domain
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

collagen fibril organization

Inferred from electronic annotation. Source: Ensembl

collagen metabolic process

Inferred from mutant phenotype PubMed 15102077. Source: UniProtKB

elastic fiber assembly

Inferred from mutant phenotype PubMed 15102077. Source: UniProtKB

extracellular fibril organization

Inferred from electronic annotation. Source: Ensembl

fatty acid metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

single organismal cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

triglyceride metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

intracellular

Inferred from direct assay PubMed 15102077. Source: UniProtKB

proteinaceous extracellular matrix

Non-traceable author statement Ref.6. Source: UniProtKB

   Molecular_functionheparin binding

Inferred from sequence or structural similarity. Source: UniProtKB

integrin binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform XB (identifier: P22105-1)

Also known as: 1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform XB-short (identifier: P22105-2)

Also known as: 2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-3616: Missing.
Isoform 3 (identifier: P22105-3)

The sequence of this isoform differs from the canonical sequence as follows:
     747-747: E → EEVPTIEGMRMHLLEETTVRTEWTPAPGPVDAYEIQFIPTTEGASPPFT
     878-1013: Missing.
     1014-1030: GVRAGQTSKSYAFITTT → TGSSPLGLLGTTDEPPPS
     1648-1648: A → APLPPA
     2155-2155: T → TAAEEETPSPT
     2353-2353: A → APGKDEEMAPA
     2451-2451: T → TAA
     2774-2774: T → TAA
     2880-2880: T → TEDEAETTQA
     2977-2977: T → TAA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 42894266Tenascin-X
PRO_0000007751

Regions

Domain156 – 16813EGF-like 1; incomplete
Domain183 – 21331EGF-like 2
Domain214 – 24431EGF-like 3
Domain245 – 27531EGF-like 4
Domain276 – 30631EGF-like 5
Domain307 – 33731EGF-like 6
Domain338 – 36831EGF-like 7
Domain369 – 39931EGF-like 8
Domain400 – 43031EGF-like 9
Domain431 – 46131EGF-like 10
Domain462 – 49231EGF-like 11
Domain493 – 52331EGF-like 12
Domain524 – 55431EGF-like 13
Domain555 – 58531EGF-like 14
Domain586 – 61631EGF-like 15
Domain617 – 64731EGF-like 16
Domain648 – 67932EGF-like 17
Domain684 – 71431EGF-like 18
Domain715 – 74632EGF-like 19
Domain794 – 88188Fibronectin type-III 1
Domain940 – 103495Fibronectin type-III 2
Domain1046 – 113893Fibronectin type-III 3
Domain1151 – 124090Fibronectin type-III 4
Domain1248 – 133689Fibronectin type-III 5
Domain1350 – 143990Fibronectin type-III 6
Domain1461 – 155595Fibronectin type-III 7
Domain1563 – 165492Fibronectin type-III 8
Domain1656 – 175196Fibronectin type-III 9
Domain1756 – 184691Fibronectin type-III 10
Domain1860 – 195091Fibronectin type-III 11
Domain1965 – 205389Fibronectin type-III 12
Domain2071 – 216191Fibronectin type-III 13
Domain2169 – 225789Fibronectin type-III 14
Domain2268 – 235891Fibronectin type-III 15
Domain2367 – 245892Fibronectin type-III 16
Domain2468 – 256295Fibronectin type-III 17
Domain2579 – 267799Fibronectin type-III 18
Domain2685 – 278197Fibronectin type-III 19
Domain2791 – 288797Fibronectin type-III 20
Domain2888 – 298497Fibronectin type-III 21
Domain2994 – 308794Fibronectin type-III 22
Domain3107 – 319892Fibronectin type-III 23
Domain3213 – 330593Fibronectin type-III 24
Domain3309 – 340092Fibronectin type-III 25
Domain3402 – 349190Fibronectin type-III 26
Domain3496 – 358994Fibronectin type-III 27
Domain3598 – 369295Fibronectin type-III 28
Domain3702 – 379998Fibronectin type-III 29
Domain3803 – 389290Fibronectin type-III 30
Domain3893 – 397987Fibronectin type-III 31
Domain3980 – 407091Fibronectin type-III 32
Domain4066 – 4281216Fibrinogen C-terminal
Coiled coil901 – 92222 Potential
Motif1748 – 17503Cell attachment site Potential

Amino acid modifications

Glycosylation311N-linked (GlcNAc...) Potential
Glycosylation9011N-linked (GlcNAc...) Ref.14
Glycosylation9301N-linked (GlcNAc...) Ref.14
Glycosylation39001N-linked (GlcNAc...) Potential
Glycosylation39531N-linked (GlcNAc...) Potential
Glycosylation39651N-linked (GlcNAc...) Ref.12
Glycosylation41401N-linked (GlcNAc...) Potential
Disulfide bond187 ↔ 197 By similarity
Disulfide bond191 ↔ 202 By similarity
Disulfide bond204 ↔ 213 By similarity
Disulfide bond218 ↔ 228 By similarity
Disulfide bond222 ↔ 233 By similarity
Disulfide bond235 ↔ 244 By similarity
Disulfide bond249 ↔ 259 By similarity
Disulfide bond253 ↔ 264 By similarity
Disulfide bond266 ↔ 275 By similarity
Disulfide bond280 ↔ 290 By similarity
Disulfide bond284 ↔ 295 By similarity
Disulfide bond297 ↔ 306 By similarity
Disulfide bond311 ↔ 321 By similarity
Disulfide bond315 ↔ 326 By similarity
Disulfide bond328 ↔ 337 By similarity
Disulfide bond342 ↔ 352 By similarity
Disulfide bond346 ↔ 357 By similarity
Disulfide bond359 ↔ 368 By similarity
Disulfide bond373 ↔ 383 By similarity
Disulfide bond377 ↔ 388 By similarity
Disulfide bond390 ↔ 399 By similarity
Disulfide bond404 ↔ 414 By similarity
Disulfide bond408 ↔ 419 By similarity
Disulfide bond421 ↔ 430 By similarity
Disulfide bond435 ↔ 445 By similarity
Disulfide bond439 ↔ 450 By similarity
Disulfide bond452 ↔ 461 By similarity
Disulfide bond466 ↔ 476 By similarity
Disulfide bond470 ↔ 481 By similarity
Disulfide bond483 ↔ 492 By similarity
Disulfide bond497 ↔ 507 By similarity
Disulfide bond501 ↔ 512 By similarity
Disulfide bond514 ↔ 523 By similarity
Disulfide bond528 ↔ 538 By similarity
Disulfide bond532 ↔ 543 By similarity
Disulfide bond545 ↔ 554 By similarity
Disulfide bond559 ↔ 569 By similarity
Disulfide bond563 ↔ 574 By similarity
Disulfide bond576 ↔ 585 By similarity
Disulfide bond590 ↔ 600 By similarity
Disulfide bond594 ↔ 605 By similarity
Disulfide bond607 ↔ 616 By similarity
Disulfide bond621 ↔ 631 By similarity
Disulfide bond625 ↔ 636 By similarity
Disulfide bond638 ↔ 647 By similarity
Disulfide bond652 ↔ 662 By similarity
Disulfide bond656 ↔ 667 By similarity
Disulfide bond669 ↔ 678 By similarity
Disulfide bond688 ↔ 698 By similarity
Disulfide bond692 ↔ 703 By similarity
Disulfide bond705 ↔ 714 By similarity
Disulfide bond719 ↔ 729 By similarity
Disulfide bond723 ↔ 734 By similarity
Disulfide bond736 ↔ 745 By similarity
Disulfide bond4075 ↔ 4105 By similarity
Disulfide bond4227 ↔ 4240 By similarity

Natural variations

Alternative sequence1 – 36163616Missing in isoform XB-short.
VSP_001418
Alternative sequence7471E → EEVPTIEGMRMHLLEETTVR TEWTPAPGPVDAYEIQFIPT TEGASPPFT in isoform 3.
VSP_034569
Alternative sequence878 – 1013136Missing in isoform 3.
VSP_034570
Alternative sequence1014 – 103017GVRAG…FITTT → TGSSPLGLLGTTDEPPPS in isoform 3.
VSP_034571
Alternative sequence16481A → APLPPA in isoform 3.
VSP_034572
Alternative sequence21551T → TAAEEETPSPT in isoform 3.
VSP_034573
Alternative sequence23531A → APGKDEEMAPA in isoform 3.
VSP_034574
Alternative sequence24511T → TAA in isoform 3.
VSP_034575
Alternative sequence27741T → TAA in isoform 3.
VSP_034576
Alternative sequence28801T → TEDEAETTQA in isoform 3.
VSP_034578
Alternative sequence29771T → TAA in isoform 3.
VSP_034577
Natural variant291R → W in EDS3. Ref.17
VAR_046499
Natural variant3021T → A. Ref.3
Corresponds to variant rs1150752 [ dbSNP | Ensembl ].
VAR_044347
Natural variant5111R → H.
Corresponds to variant rs204896 [ dbSNP | Ensembl ].
VAR_021908
Natural variant6411G → C.
Corresponds to variant rs17201609 [ dbSNP | Ensembl ].
VAR_055781
Natural variant6501R → H.
Corresponds to variant rs17201602 [ dbSNP | Ensembl ].
VAR_055782
Natural variant8251S → A.
Corresponds to variant rs204900 [ dbSNP | Ensembl ].
VAR_055783
Natural variant11951V → M in EDS3. Ref.17
VAR_046500
Natural variant12481H → R.
Corresponds to variant rs185819 [ dbSNP | Ensembl ].
VAR_024270
Natural variant19871E → K.
Corresponds to variant rs17207923 [ dbSNP | Ensembl ].
VAR_059276
Natural variant23631P → H.
Corresponds to variant rs2269428 [ dbSNP | Ensembl ].
VAR_020170
Natural variant24251P → H.
Corresponds to variant rs2269428 [ dbSNP | Ensembl ].
VAR_055784
Natural variant24721P → L.
Corresponds to variant rs12524664 [ dbSNP | Ensembl ].
VAR_059277
Natural variant25551G → S.
Corresponds to variant rs2269429 [ dbSNP | Ensembl ].
VAR_020171
Natural variant25781G → E. Ref.2 Ref.3
Corresponds to variant rs1009382 [ dbSNP | Ensembl ].
VAR_020172
Natural variant40331L → I. Ref.17
VAR_046501

Experimental info

Sequence conflict1351G → GEQG in CAA50739. Ref.6
Sequence conflict27891P → R in AAB67981. Ref.2
Sequence conflict27891P → R in AAB47488. Ref.2
Sequence conflict38361Q → L in AAH33740. Ref.5
Sequence conflict39221V → I in AAI25115. Ref.5
Sequence conflict39221V → I in AAI25116. Ref.5
Sequence conflict39221V → I in BAD92249. Ref.10
Sequence conflict40191N → T in AAI25115. Ref.5
Sequence conflict40191N → T in AAI25116. Ref.5
Sequence conflict40191N → T in BAD92249. Ref.10
Sequence conflict40381P → G in AAB41287. Ref.1
Sequence conflict40381P → G in AAA35884. Ref.11
Sequence conflict40491M → T in AAI25116. Ref.5
Sequence conflict40491M → T in BAD92249. Ref.10
Sequence conflict41021N → I in AAI25115. Ref.5
Sequence conflict41631M → I in AAB41287. Ref.1
Sequence conflict41631M → I in AAA35884. Ref.11

Secondary structure

.................................................. 4289
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform XB (1) [UniParc].

Last modified March 2, 2010. Version 3.
Checksum: 3E26AA5923D1AAA2

FASTA4,289464,325
        10         20         30         40         50         60 
MMPAQYALTS SLVLLVLLST ARAGPFSSRS NVTLPAPRPP PQPGGHTVGA GVGSPSSQLY 

        70         80         90        100        110        120 
EHTVEGGEKQ VVFTHRINLP PSTGCGCPPG TEPPVLASEV QALRVRLEIL EELVKGLKEQ 

       130        140        150        160        170        180 
CTGGCCPASA QAGTGQTDVR TLCSLHGVFD LSRCTCSCEP GWGGPTCSDP TDAEIPPSSP 

       190        200        210        220        230        240 
PSASGSCPDD CNDQGRCVRG RCVCFPGYTG PSCGWPSCPG DCQGRGRCVQ GVCVCRAGFS 

       250        260        270        280        290        300 
GPDCSQRSCP RGCSQRGRCE GGRCVCDPGY TGDDCGMRSC PRGCSQRGRC ENGRCVCNPG 

       310        320        330        340        350        360 
YTGEDCGVRS CPRGCSQRGR CKDGRCVCDP GYTGEDCGTR SCPWDCGEGG RCVDGRCVCW 

       370        380        390        400        410        420 
PGYTGEDCST RTCPRDCRGR GRCEDGECIC DTGYSGDDCG VRSCPGDCNQ RGRCEDGRCV 

       430        440        450        460        470        480 
CWPGYTGTDC GSRACPRDCR GRGRCENGVC VCNAGYSGED CGVRSCPGDC RGRGRCESGR 

       490        500        510        520        530        540 
CMCWPGYTGR DCGTRACPGD CRGRGRCVDG RCVCNPGFTG EDCGSRRCPG DCRGHGLCED 

       550        560        570        580        590        600 
GVCVCDAGYS GEDCSTRSCP GGCRGRGQCL DGRCVCEDGY SGEDCGVRQC PNDCSQHGVC 

       610        620        630        640        650        660 
QDGVCICWEG YVSEDCSIRT CPSNCHGRGR CEEGRCLCDP GYTGPTCATR MCPADCRGRG 

       670        680        690        700        710        720 
RCVQGVCLCH VGYGGEDCGQ EEPPASACPG GCGPRELCRA GQCVCVEGFR GPDCAIQTCP 

       730        740        750        760        770        780 
GDCRGRGECH DGSCVCKDGY AGEDCGEARV PSSASAYDQR GLAPGQEYQV TVRALRGTSW 

       790        800        810        820        830        840 
GLPASKTITT MIDGPQDLRV VAVTPTTLEL GWLRPQAEVD RFVVSYVSAG NQRVRLEVPP 

       850        860        870        880        890        900 
EADGTLLTDL MPGVEYVVTV TAERGRAVSY PASVRANTEE REEESPPRPS LSQPPRRPWG 

       910        920        930        940        950        960 
NLTAELSRFR GTVQDLERHL RAHGYPLRAN QTYTSVARHI HEYLQRQVLG SSADGALLVS 

       970        980        990       1000       1010       1020 
LDGLRGQFER VVLRWRPQPP AEGPGGELTV PGTTRTVSLP DLRPGTTYHV EVHGVRAGQT 

      1030       1040       1050       1060       1070       1080 
SKSYAFITTT GPSTTQGAQA PLLQQRPQEL GELRVLGRDE TGRLRVVWTA QPDTFAYFQL 

      1090       1100       1110       1120       1130       1140 
RMRVPEGPGA HEEVLPGDVR QALVPPPPPG TPYELSLHGV PPGGKPSDPI IYQGIMDKDE 

      1150       1160       1170       1180       1190       1200 
EKPGKSSGPP RLGELTVTDR TSDSLLLRWT VPEGEFDSFV IQYKDRDGQP QVVPVEGPQR 

      1210       1220       1230       1240       1250       1260 
SAVITSLDPG RKYKFVLYGF VGKKRHGPLV AEAKILPQSD PSPGTPPHLG NLWVTDPTPD 

      1270       1280       1290       1300       1310       1320 
SLHLSWTVPE GQFDTFMVQY RDRDGRPQVV PVEGPERSFV VSSLDPDHKY RFTLFGIANK 

      1330       1340       1350       1360       1370       1380 
KRYGPLTADG TTAPERKEEP PRPEFLEQPL LGELTVTGVT PDSLRLSWTV AQGPFDSFMV 

      1390       1400       1410       1420       1430       1440 
QYKDAQGQPQ AVPVAGDENE VTVPGLDPDR KYKMNLYGLR GRQRVGPESV VAKTAPQEDV 

      1450       1460       1470       1480       1490       1500 
DETPSPTELG TEAPESPEEP LLGELTVTGS SPDSLSLFWT VPQGSFDSFT VQYKDRDGRP 

      1510       1520       1530       1540       1550       1560 
RAVRVGGKES EVTVGGLEPG HKYKMHLYGL HEGQRVGPVS AVGVTAPQQE ETPPATESPL 

      1570       1580       1590       1600       1610       1620 
EPRLGELTVT DVTPNSVGLS WTVPEGQFDS FIVQYKDKDG QPQVVPVAAD QREVTVYNLE 

      1630       1640       1650       1660       1670       1680 
PERKYKMNMY GLHDGQRMGP LSVVIVTAPA TEASKPPLEP RLGELTVTDI TPDSVGLSWT 

      1690       1700       1710       1720       1730       1740 
VPEGEFDSFV VQYKDRDGQP QVVPVAADQR EVTIPDLEPS RKYKFLLFGI QDGKRRSPVS 

      1750       1760       1770       1780       1790       1800 
VEAKTVARGD ASPGAPPRLG ELWVTDPTPD SLRLSWTVPE GQFDSFVVQF KDKDGPQVVP 

      1810       1820       1830       1840       1850       1860 
VEGHERSVTV TPLDAGRKYR FLLYGLLGKK RHGPLTADGT TEARSAMDDT GTKRPPKPRL 

      1870       1880       1890       1900       1910       1920 
GEELQVTTVT QNSVGLSWTV PEGQFDSFVV QYKDRDGQPQ VVPVEGSLRE VSVPGLDPAH 

      1930       1940       1950       1960       1970       1980 
RYKLLLYGLH HGKRVGPISA VAITAGREET ETETTAPTPP APEPHLGELT VEEATSHTLH 

      1990       2000       2010       2020       2030       2040 
LSWMVTEGEF DSFEIQYTDR DGQLQMVRIG GDRNDITLSG LESDHRYLVT LYGFSDGKHV 

      2050       2060       2070       2080       2090       2100 
GPVHVEALTV PEEEKPSEPP TATPEPPIKP RLGELTVTDA TPDSLSLSWT VPEGQFDHFL 

      2110       2120       2130       2140       2150       2160 
VQYRNGDGQP KAVRVPGHEE GVTISGLEPD HKYKMNLYGF HGGQRMGPVS VVGVTEPSME 

      2170       2180       2190       2200       2210       2220 
APEPAEEPLL GELTVTGSSP DSLSLSWTVP QGRFDSFTVQ YKDRDGRPQV VRVGGEESEV 

      2230       2240       2250       2260       2270       2280 
TVGGLEPGRK YKMHLYGLHE GRRVGPVSAV GVTAPEEESP DAPLAKLRLG QMTVRDITSD 

      2290       2300       2310       2320       2330       2340 
SLSLSWTVPE GQFDHFLVQF KNGDGQPKAV RVPGHEDGVT ISGLEPDHKY KMNLYGFHGG 

      2350       2360       2370       2380       2390       2400 
QRVGPVSAVG LTASTEPPTP EPPIKPRLEE LTVTDATPDS LSLSWTVPEG QFDHFLVQYK 

      2410       2420       2430       2440       2450       2460 
NGDGQPKATR VPGHEDRVTI SGLEPDNKYK MNLYGFHGGQ RVGPVSAIGV TEEETPSPTE 

      2470       2480       2490       2500       2510       2520 
PSMEAPEPPE EPLLGELTVT GSSPDSLSLS WTVPQGRFDS FTVQYKDRDG RPQVVRVGGE 

      2530       2540       2550       2560       2570       2580 
ESEVTVGGLE PGRKYKMHLY GLHEGRRVGP VSTVGVTAPQ EDVDETPSPT EPGTEAPGPP 

      2590       2600       2610       2620       2630       2640 
EEPLLGELTV TGSSPDSLSL SWTVPQGRFD SFTVQYKDRD GRPQAVRVGG QESKVTVRGL 

      2650       2660       2670       2680       2690       2700 
EPGRKYKMHL YGLHEGRRLG PVSAVGVTED EAETTQAVPT MTPEPPIKPR LGELTMTDAT 

      2710       2720       2730       2740       2750       2760 
PDSLSLSWTV PEGQFDHFLV QYRNGDGQPK AVRVPGHEDG VTISGLEPDH KYKMNLYGFH 

      2770       2780       2790       2800       2810       2820 
GGQRVGPISV IGVTEEETPS PTELSTEAPE PPEEPLLGEL TVTGSSPDSL SLSWTIPQGH 

      2830       2840       2850       2860       2870       2880 
FDSFTVQYKD RDGRPQVMRV RGEESEVTVG GLEPGRKYKM HLYGLHEGRR VGPVSTVGVT 

      2890       2900       2910       2920       2930       2940 
VPTTTPEPPN KPRLGELTVT DATPDSLSLS WMVPEGQFDH FLVQYRNGDG QPKVVRVPGH 

      2950       2960       2970       2980       2990       3000 
EDGVTISGLE PDHKYKMNLY GFHGGQRVGP ISVIGVTEEE TPAPTEPSTE APEPPEEPLL 

      3010       3020       3030       3040       3050       3060 
GELTVTGSSP DSLSLSWTIP QGRFDSFTVQ YKDRDGRPQV VRVRGEESEV TVGGLEPGCK 

      3070       3080       3090       3100       3110       3120 
YKMHLYGLHE GQRVGPVSAV GVTAPKDEAE TTQAVPTMTP EPPIKPRLGE LTVTDATPDS 

      3130       3140       3150       3160       3170       3180 
LSLSWMVPEG QFDHFLVQYR NGDGQPKAVR VPGHEDGVTI SGLEPDHKYK MNLYGFHGGQ 

      3190       3200       3210       3220       3230       3240 
RVGPVSAIGV TEEETPSPTE PSTEAPEAPE EPLLGELTVT GSSPDSLSLS WTVPQGRFDS 

      3250       3260       3270       3280       3290       3300 
FTVQYKDRDG QPQVVRVRGE ESEVTVGGLE PGRKYKMHLY GLHEGQRVGP VSTVGITAPL 

      3310       3320       3330       3340       3350       3360 
PTPLPVEPRL GELAVAAVTS DSVGLSWTVA QGPFDSFLVQ YRDAQGQPQA VPVSGDLRAV 

      3370       3380       3390       3400       3410       3420 
AVSGLDPARK YKFLLFGLQN GKRHGPVPVE ARTAPDTKPS PRLGELTVTD ATPDSVGLSW 

      3430       3440       3450       3460       3470       3480 
TVPEGEFDSF VVQYKDKDGR LQVVPVAANQ REVTVQGLEP SRKYRFLLYG LSGRKRLGPI 

      3490       3500       3510       3520       3530       3540 
SADSTTAPLE KELPPHLGEL TVAEETSSSL RLSWTVAQGP FDSFVVQYRD TDGQPRAVPV 

      3550       3560       3570       3580       3590       3600 
AADQRTVTVE DLEPGKKYKF LLYGLLGGKR LGPVSALGMT APEEDTPAPE LAPEAPEPPE 

      3610       3620       3630       3640       3650       3660 
EPRLGVLTVT DTTPDSMRLS WSVAQGPFDS FVVQYEDTNG QPQALLVDGD QSKILISGLE 

      3670       3680       3690       3700       3710       3720 
PSTPYRFLLY GLHEGKRLGP LSAEGTTGLA PAGQTSEESR PRLSQLSVTD VTTSSLRLNW 

      3730       3740       3750       3760       3770       3780 
EAPPGAFDSF LLRFGVPSPS TLEPHPRPLL QRELMVPGTR HSAVLRDLRS GTLYSLTLYG 

      3790       3800       3810       3820       3830       3840 
LRGPHKADSI QGTARTLSPV LESPRDLQFS EIRETSAKVN WMPPPSRADS FKVSYQLADG 

      3850       3860       3870       3880       3890       3900 
GEPQSVQVDG QARTQKLQGL IPGARYEVTV VSVRGFEESE PLTGFLTTVP DGPTQLRALN 

      3910       3920       3930       3940       3950       3960 
LTEGFAVLHW KPPQNPVDTY DVQVTAPGAP PLQAETPGSA VDYPLHDLVL HTNYTATVRG 

      3970       3980       3990       4000       4010       4020 
LRGPNLTSPA SITFTTGLEA PRDLEAKEVT PRTALLTWTE PPVRPAGYLL SFHTPGGQNQ 

      4030       4040       4050       4060       4070       4080 
EILLPGGITS HQLLGLFPST SYNARLQAMW GQSLLPPVST SFTTGGLRIP FPRDCGEEMQ 

      4090       4100       4110       4120       4130       4140 
NGAGASRTST IFLNGNRERP LNVFCDMETD GGGWLVFQRR MDGQTDFWRD WEDYAHGFGN 

      4150       4160       4170       4180       4190       4200 
ISGEFWLGNE ALHSLTQAGD YSMRVDLRAG DEAVFAQYDS FHVDSAAEYY RLHLEGYHGT 

      4210       4220       4230       4240       4250       4260 
AGDSMSYHSG SVFSARDRDP NSLLISCAVS YRGAWWYRNC HYANLNGLYG STVDHQGVSW 

      4270       4280 
YHWKGFEFSV PFTEMKLRPR NFRSPAGGG 

« Hide

Isoform XB-short (2) [UniParc].

Checksum: 2A14010E8A633FA1
Show »

FASTA67374,030
Isoform 3 [UniParc].

Checksum: 7E07AC46BF6F2599
Show »

FASTA4,242458,220

References

« Hide 'large scale' references
[1]"Sequences promoting the transcription of the human XA gene overlapping P450c21A correctly predict the presence of a novel, adrenal-specific, truncated form of tenascin-X."
Tee M.K., Thomson A.A., Bristow J., Miller W.L.
Genomics 28:171-178(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM XB-SHORT).
Tissue: Adrenal gland.
[2]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-2578.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ALA-302 AND GLU-2578.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM XB-SHORT), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3455-4289 (ISOFORMS XB/3).
[6]"Tenascin-X: a novel extracellular matrix protein encoded by the human XB gene overlapping P450c21B."
Bristow J., Tee M.K., Gitelman S.E., Mellon S.H., Miller W.L.
J. Cell Biol. 122:265-278(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-747 AND 1687-1944 (ISOFORMS XB/3).
Tissue: Leukocyte.
[7]"Alternate promoters and alternate splicing of human tenascin-X, a gene with 5' and 3' ends buried in other genes."
Speek M., Barry F., Miller W.L.
Hum. Mol. Genet. 5:1749-1758(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-23 (ISOFORMS XB/3).
Tissue: Fetal adrenal gland.
[8]"Cluster of fibronectin type III repeats found in the human major histocompatibility complex class III region shows the highest homology with the repeats in an extracellular matrix protein, tenascin."
Matsumoto K., Arai M., Ishihara N., Ando A., Inoko H., Ikemura T.
Genomics 12:485-491(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1148-1235; 2581-2668; 2687-2774 AND 2793-2880.
Tissue: B-cell.
[9]"Identification and characterization of multiple species of tenascin-X in human serum."
Egging D.F., Peeters A.C.T.M., Grebenchtchikov N., Geurts-Moespot A., Sweep C.G.J., den Heijer M., Schalkwijk J.
FEBS J. 274:1280-1289(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1486-1494; 1525-1535; 2194-2202; 2498-2506; 2609-2617; 2821-2829; 2840-2857; 3024-3032; 3063-3073; 3238-3246; 3257-3274; 3277-3287; 3654-3666 AND 3678-3710 (ISOFORMS XB/3), INTERACTION WITH TROPOELASTIN, DEVELOPMENTAL STAGE.
[10]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3406-4289 (ISOFORMS XB/3).
Tissue: Brain.
[11]"Transcript encoded on the opposite strand of the human steroid 21-hydroxylase/complement component C4 gene locus."
Morel Y., Bristow J., Gitelman S.E., Miller W.L.
Proc. Natl. Acad. Sci. U.S.A. 86:6582-6586(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3470-4289 (ISOFORMS XB/3).
[12]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3965.
Tissue: Plasma.
[13]"Interactions of human tenascin-X domains with dermal extracellular matrix molecules."
Egging D.F., van den Berkmortel F., Taylor G., Bristow J., Schalkwijk J.
Arch. Dermatol. Res. 298:389-396(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH COLLAGEN AND TROPOELASTIN.
[14]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-901 AND ASN-930.
Tissue: Liver.
[15]"Solution structure of the 29th, 31st and 33rd fibronectin type-III domains of the human tenascin-X."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 3699-4069.
[16]"A recessive form of the Ehlers-Danlos syndrome caused by tenascin-X deficiency."
Schalkwijk J., Zweers M.C., Steijlen P.M., Dean W.B., Taylor G., van Vlijmen I.M., van Haren B., Miller W.L., Bristow J.
N. Engl. J. Med. 345:1167-1175(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN EDSTNXD.
[17]"Elastic fiber abnormalities in hypermobility type Ehlers-Danlos syndrome patients with tenascin-X mutations."
Zweers M.C., Dean W.B., van Kuppevelt T.H., Bristow J., Schalkwijk J.
Clin. Genet. 67:330-334(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EDS3 TRP-29 AND MET-1195, VARIANT ILE-4033.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U24488 mRNA. Translation: AAB41287.1.
AF019413 Genomic DNA. Translation: AAB67981.1.
U89337 Genomic DNA. Translation: AAB47488.1.
AL049547 Genomic DNA. Translation: CAB89296.1. Different initiation.
AL049547 Genomic DNA. Translation: CAB89300.1.
AL645922, AL662884, AL772248 Genomic DNA. Translation: CAQ09268.1. Sequence problems.
AL662828, AL662849 Genomic DNA. Translation: CAI17414.1. Sequence problems.
AL662849, AL662828 Genomic DNA. Translation: CAI17471.1. Sequence problems.
AL662884, AL645922, AL772248 Genomic DNA. Translation: CAI18332.1. Sequence problems.
AL772248, AL645922, AL662884 Genomic DNA. Translation: CAI18078.1. Sequence problems.
CH471081 Genomic DNA. Translation: EAX03574.1.
BC033740 mRNA. Translation: AAH33740.1. Different initiation.
BC125114 mRNA. Translation: AAI25115.1.
BC125115 mRNA. Translation: AAI25116.1.
BC130037 mRNA. Translation: AAI30038.1.
X71923 mRNA. Translation: CAA50739.1.
Y13782 mRNA. Translation: CAA74109.1.
Y13783 Genomic DNA. Translation: CAA74110.1.
U52696 mRNA. Translation: AAC50889.1.
AB209012 mRNA. Translation: BAD92249.1.
M25813 mRNA. Translation: AAA35884.1.
CCDSCCDS4736.1. [P22105-2]
PIRA40701.
A42175.
B42175.
D42175.
RefSeqNP_061978.6. NM_019105.6. [P22105-3]
NP_115859.2. NM_032470.3. [P22105-2]
UniGeneHs.485104.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CUHNMR-A3890-3991[»]
2CUINMR-A3699-3797[»]
2CUMNMR-A3978-4069[»]
ProteinModelPortalP22105.
SMRP22105. Positions 140-878, 983-4279.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP22105. 5 interactions.

PTM databases

PhosphoSiteP22105.

Polymorphism databases

DMDM290457668.

Proteomic databases

MaxQBP22105.
PRIDEP22105.

Protocols and materials databases

DNASU7148.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375247; ENSP00000364396; ENSG00000168477. [P22105-3]
ENST00000451343; ENSP00000407685; ENSG00000168477. [P22105-2]
ENST00000546684; ENSP00000447694; ENSG00000236236.
ENST00000550539; ENSP00000448326; ENSG00000229353. [P22105-2]
GeneID7148.
KEGGhsa:7148.
UCSCuc003nzg.1. human. [P22105-2]
uc003nzl.2. human. [P22105-3]

Organism-specific databases

CTD7148.
GeneCardsGC06M032008.
GC06Mn31966.
GC06Mo32000.
GeneReviewsTNXB.
H-InvDBHIX0165968.
HIX0207682.
HGNCHGNC:11976. TNXB.
HPACAB005373.
MIM130020. phenotype.
600985. gene.
606408. phenotype.
neXtProtNX_P22105.
Orphanet230839. Ehlers-Danlos syndrome due to tenascin-X deficiency.
285. Ehlers-Danlos syndrome, hypermobility type.
PharmGKBPA36662.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG006855.
InParanoidP22105.
KOK06252.
PhylomeDBP22105.
TreeFamTF329915.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP22105.
BgeeP22105.
GenevestigatorP22105.

Family and domain databases

Gene3D2.60.40.10. 32 hits.
3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
[Graphical view]
PfamPF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 31 hits.
PF12661. hEGF. 7 hits.
[Graphical view]
SMARTSM00181. EGF. 9 hits.
SM00186. FBG. 1 hit.
SM00060. FN3. 32 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 31 hits.
SSF56496. SSF56496. 1 hit.
PROSITEPS00022. EGF_1. 18 hits.
PS01186. EGF_2. 19 hits.
PS50026. EGF_3. 8 hits.
PS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
PS50853. FN3. 32 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTNXB. human.
EvolutionaryTraceP22105.
GeneWikiTenascin_X.
GenomeRNAi7148.
NextBio27974.
PROP22105.
SOURCESearch...

Entry information

Entry nameTENX_HUMAN
AccessionPrimary (citable) accession number: P22105
Secondary accession number(s): P78530 expand/collapse secondary AC list , P78531, Q08424, Q08AM0, Q08AM1, Q59GU7, Q5SQD3, Q5ST74, Q7L8Q4, Q8N4R1, Q9NPK9, Q9UC10, Q9UC11, Q9UC12, Q9UC13, Q9UMG7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: March 2, 2010
Last modified: July 9, 2014
This is version 170 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM