P22105 (TENX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tenascin-X
Short name=TN-X

Alternative name(s):
Hexabrachion-like protein

Gene names

Name:	TNXB
Synonyms:	HXBL, TNX, TNXB1, TNXB2, XB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	4289 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular 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 process	Cell adhesion
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Ehlers-Danlos syndrome
Domain	Coiled coil EGF-like domain Repeat Signal
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB cell-cell adhesion Inferred from electronic annotation. Source: Compara cell-matrix adhesion Inferred from electronic annotation. Source: Compara collagen fibril organization Inferred from electronic annotation. Source: Compara 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: Compara fatty acid metabolic process Inferred from electronic annotation. Source: Compara regulation of JUN kinase activity Inferred from electronic annotation. Source: Compara triglyceride metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular 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_function	heparin 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Potential

Chain

24 – 4289

4266

Tenascin-X

PRO_0000007751

Regions

Domain

156 – 168

13

EGF-like 1; incomplete

Domain

183 – 213

31

EGF-like 2

Domain

214 – 244

31

EGF-like 3

Domain

245 – 275

31

EGF-like 4

Domain

276 – 306

31

EGF-like 5

Domain

307 – 337

31

EGF-like 6

Domain

338 – 368

31

EGF-like 7

Domain

369 – 399

31

EGF-like 8

Domain

400 – 430

31

EGF-like 9

Domain

431 – 461

31

EGF-like 10

Domain

462 – 492

31

EGF-like 11

Domain

493 – 523

31

EGF-like 12

Domain

524 – 554

31

EGF-like 13

Domain

555 – 585

31

EGF-like 14

Domain

586 – 616

31

EGF-like 15

Domain

617 – 647

31

EGF-like 16

Domain

648 – 679

32

EGF-like 17

Domain

684 – 714

31

EGF-like 18

Domain

715 – 746

32

EGF-like 19

Domain

792 – 872

81

Fibronectin type-III 1

Domain

941 – 1021

81

Fibronectin type-III 2

Domain

1047 – 1127

81

Fibronectin type-III 3

Domain

1149 – 1226

78

Fibronectin type-III 4

Domain

1246 – 1327

82

Fibronectin type-III 5

Domain

1348 – 1429

82

Fibronectin type-III 6

Domain

1459 – 1540

82

Fibronectin type-III 7

Domain

1561 – 1642

82

Fibronectin type-III 8

Domain

1659 – 1736

78

Fibronectin type-III 9

Domain

1756 – 1836

81

Fibronectin type-III 10

Domain

1856 – 1939

84

Fibronectin type-III 11

Domain

1962 – 2039

78

Fibronectin type-III 12

Domain

2069 – 2150

82

Fibronectin type-III 13

Domain

2167 – 2248

82

Fibronectin type-III 14

Domain

2266 – 2347

82

Fibronectin type-III 15

Domain

2365 – 2446

82

Fibronectin type-III 16

Domain

2471 – 2552

82

Fibronectin type-III 17

Domain

2582 – 2663

82

Fibronectin type-III 18

Domain

2688 – 2769

82

Fibronectin type-III 19

Domain

2794 – 2875

82

Fibronectin type-III 20

Domain

2889 – 2972

84

Fibronectin type-III 21

Domain

2997 – 3078

82

Fibronectin type-III 22

Domain

3105 – 3186

82

Fibronectin type-III 23

Domain

3211 – 3292

82

Fibronectin type-III 24

Domain

3307 – 3384

78

Fibronectin type-III 25

Domain

3399 – 3481

83

Fibronectin type-III 26

Domain

3494 – 3575

82

Fibronectin type-III 27

Domain

3601 – 3682

82

Fibronectin type-III 28

Domain

3699 – 3787

89

Fibronectin type-III 29

Domain

3801 – 3879

79

Fibronectin type-III 30

Domain

3890 – 3971

82

Fibronectin type-III 31

Domain

3978 – 4059

82

Fibronectin type-III 32

Domain

4066 – 4281

216

Fibrinogen C-terminal

Coiled coil

901 – 922

22

Potential

Motif

1748 – 1750

3

Cell attachment site Potential

Amino acid modifications

Glycosylation

31

1

N-linked (GlcNAc...) Potential

Glycosylation

901

1

N-linked (GlcNAc...) Ref.14

Glycosylation

930

1

N-linked (GlcNAc...) Ref.14

Glycosylation

3900

1

N-linked (GlcNAc...) Potential

Glycosylation

3953

1

N-linked (GlcNAc...) Potential

Glycosylation

3965

1

N-linked (GlcNAc...) Ref.12

Glycosylation

4140

1

N-linked (GlcNAc...) Potential

Disulfide bond

187 ↔ 197

By similarity

Disulfide bond

191 ↔ 202

By similarity

Disulfide bond

204 ↔ 213

By similarity

Disulfide bond

218 ↔ 228

By similarity

Disulfide bond

222 ↔ 233

By similarity

Disulfide bond

235 ↔ 244

By similarity

Disulfide bond

249 ↔ 259

By similarity

Disulfide bond

253 ↔ 264

By similarity

Disulfide bond

266 ↔ 275

By similarity

Disulfide bond

280 ↔ 290

By similarity

Disulfide bond

284 ↔ 295

By similarity

Disulfide bond

297 ↔ 306

By similarity

Disulfide bond

311 ↔ 321

By similarity

Disulfide bond

315 ↔ 326

By similarity

Disulfide bond

328 ↔ 337

By similarity

Disulfide bond

342 ↔ 352

By similarity

Disulfide bond

346 ↔ 357

By similarity

Disulfide bond

359 ↔ 368

By similarity

Disulfide bond

373 ↔ 383

By similarity

Disulfide bond

377 ↔ 388

By similarity

Disulfide bond

390 ↔ 399

By similarity

Disulfide bond

404 ↔ 414

By similarity

Disulfide bond

408 ↔ 419

By similarity

Disulfide bond

421 ↔ 430

By similarity

Disulfide bond

435 ↔ 445

By similarity

Disulfide bond

439 ↔ 450

By similarity

Disulfide bond

452 ↔ 461

By similarity

Disulfide bond

466 ↔ 476

By similarity

Disulfide bond

470 ↔ 481

By similarity

Disulfide bond

483 ↔ 492

By similarity

Disulfide bond

497 ↔ 507

By similarity

Disulfide bond

501 ↔ 512

By similarity

Disulfide bond

514 ↔ 523

By similarity

Disulfide bond

528 ↔ 538

By similarity

Disulfide bond

532 ↔ 543

By similarity

Disulfide bond

545 ↔ 554

By similarity

Disulfide bond

559 ↔ 569

By similarity

Disulfide bond

563 ↔ 574

By similarity

Disulfide bond

576 ↔ 585

By similarity

Disulfide bond

590 ↔ 600

By similarity

Disulfide bond

594 ↔ 605

By similarity

Disulfide bond

607 ↔ 616

By similarity

Disulfide bond

621 ↔ 631

By similarity

Disulfide bond

625 ↔ 636

By similarity

Disulfide bond

638 ↔ 647

By similarity

Disulfide bond

652 ↔ 662

By similarity

Disulfide bond

656 ↔ 667

By similarity

Disulfide bond

669 ↔ 678

By similarity

Disulfide bond

688 ↔ 698

By similarity

Disulfide bond

692 ↔ 703

By similarity

Disulfide bond

705 ↔ 714

By similarity

Disulfide bond

719 ↔ 729

By similarity

Disulfide bond

723 ↔ 734

By similarity

Disulfide bond

736 ↔ 745

By similarity

Disulfide bond

4075 ↔ 4105

By similarity

Disulfide bond

4227 ↔ 4240

By similarity

Natural variations

Alternative sequence

1 – 3616

3616

Missing in isoform XB-short.

VSP_001418

Alternative sequence

747

1

E → EEVPTIEGMRMHLLEETTVR TEWTPAPGPVDAYEIQFIPT TEGASPPFT in isoform 3.

VSP_034569

Alternative sequence

878 – 1013

136

Missing in isoform 3.

VSP_034570

Alternative sequence

1014 – 1030

17

GVRAG…FITTT → TGSSPLGLLGTTDEPPPS in isoform 3.

VSP_034571

Alternative sequence

1648

1

A → APLPPA in isoform 3.

VSP_034572

Alternative sequence

2155

1

T → TAAEEETPSPT in isoform 3.

VSP_034573

Alternative sequence

2353

1

A → APGKDEEMAPA in isoform 3.

VSP_034574

Alternative sequence

2451

1

T → TAA in isoform 3.

VSP_034575

Alternative sequence

2774

1

T → TAA in isoform 3.

VSP_034576

Alternative sequence

2880

1

T → TEDEAETTQA in isoform 3.

VSP_034578

Alternative sequence

2977

1

T → TAA in isoform 3.

VSP_034577

Natural variant

29

1

R → W in EDS3. Ref.17

VAR_046499

Natural variant

302

1

T → A. Ref.3
Corresponds to variant rs1150752 [ dbSNP | Ensembl ].

VAR_044347

Natural variant

511

1

R → H.
Corresponds to variant rs204896 [ dbSNP | Ensembl ].

VAR_021908

Natural variant

641

1

G → C.
Corresponds to variant rs17201609 [ dbSNP | Ensembl ].

VAR_055781

Natural variant

650

1

R → H.
Corresponds to variant rs17201602 [ dbSNP | Ensembl ].

VAR_055782

Natural variant

825

1

S → A.
Corresponds to variant rs204900 [ dbSNP | Ensembl ].

VAR_055783

Natural variant

1195

1

V → M in EDS3. Ref.17

VAR_046500

Natural variant

1248

1

H → R.
Corresponds to variant rs185819 [ dbSNP | Ensembl ].

VAR_024270

Natural variant

1987

1

E → K.
Corresponds to variant rs17207923 [ dbSNP | Ensembl ].

VAR_059276

Natural variant

2363

1

P → H.
Corresponds to variant rs2269428 [ dbSNP | Ensembl ].

VAR_020170

Natural variant

2425

1

P → H.
Corresponds to variant rs2269428 [ dbSNP | Ensembl ].

VAR_055784

Natural variant

2472

1

P → L.
Corresponds to variant rs12524664 [ dbSNP | Ensembl ].

VAR_059277

Natural variant

2555

1

G → S.
Corresponds to variant rs2269429 [ dbSNP | Ensembl ].

VAR_020171

Natural variant

2578

1

G → E. Ref.2 Ref.3
Corresponds to variant rs1009382 [ dbSNP | Ensembl ].

VAR_020172

Natural variant

4033

1

L → I. Ref.17

VAR_046501

Experimental info

Sequence conflict

135

1

G → GEQG in CAA50739. Ref.6

Sequence conflict

2789

1

P → R in AAB67981. Ref.2

Sequence conflict

2789

1

P → R in AAB47488. Ref.2

Sequence conflict

3836

1

Q → L in AAH33740. Ref.5

Sequence conflict

3922

1

V → I in AAI25115. Ref.5

Sequence conflict

3922

1

V → I in AAI25116. Ref.5

Sequence conflict

3922

1

V → I in BAD92249. Ref.10

Sequence conflict

4019

1

N → T in AAI25115. Ref.5

Sequence conflict

4019

1

N → T in AAI25116. Ref.5

Sequence conflict

4019

1

N → T in BAD92249. Ref.10

Sequence conflict

4038

1

P → G in AAB41287. Ref.1

Sequence conflict

4038

1

P → G in AAA35884. Ref.11

Sequence conflict

4049

1

M → T in AAI25116. Ref.5

Sequence conflict

4049

1

M → T in BAD92249. Ref.10

Sequence conflict

4102

1

N → I in AAI25115. Ref.5

Sequence conflict

4163

1

M → I in AAB41287. Ref.1

Sequence conflict

4163

1

M → I in AAA35884. Ref.11

Secondary structure

1

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4289

Helix Strand Turn

Details...

Beta strand

3707 – 3710

4

Beta strand

3716 – 3719

4

Beta strand

3728 – 3735

8

Beta strand

3740 – 3742

3

Beta strand

3752 – 3757

6

Beta strand

3762 – 3765

4

Beta strand

3773 – 3781

9

Beta strand

3783 – 3795

13

Beta strand

3894 – 3897

4

Beta strand

3902 – 3904

3

Beta strand

3906 – 3911

6

Beta strand

3918 – 3925

8

Beta strand

3927 – 3929

3

Beta strand

3932 – 3937

6

Beta strand

3941 – 3945

5

Beta strand

3950 – 3962

13

Beta strand

3970 – 3976

7

Turn

3981 – 3983

3

Beta strand

3984 – 3986

3

Beta strand

3994 – 3999

6

Beta strand

4006 – 4013

8

Beta strand

4019 – 4024

6

Beta strand

4029 – 4033

5

Beta strand

4041 – 4050

10

Beta strand

4058 – 4063

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform XB (1) [UniParc]. Last modified March 2, 2010. Version 3. Checksum: 3E26AA5923D1AAA2	FASTA	4,289	464,325
	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
	Isoform XB-short (2) [UniParc]. Checksum: 2A14010E8A633FA1	FASTA	673	74,030
	10 20 30 40 50 60 MRLSWSVAQG PFDSFVVQYE DTNGQPQALL VDGDQSKILI SGLEPSTPYR FLLYGLHEGK 70 80 90 100 110 120 RLGPLSAEGT TGLAPAGQTS EESRPRLSQL SVTDVTTSSL RLNWEAPPGA FDSFLLRFGV 130 140 150 160 170 180 PSPSTLEPHP RPLLQRELMV PGTRHSAVLR DLRSGTLYSL TLYGLRGPHK ADSIQGTART 190 200 210 220 230 240 LSPVLESPRD LQFSEIRETS AKVNWMPPPS RADSFKVSYQ LADGGEPQSV QVDGQARTQK 250 260 270 280 290 300 LQGLIPGARY EVTVVSVRGF EESEPLTGFL TTVPDGPTQL RALNLTEGFA VLHWKPPQNP 310 320 330 340 350 360 VDTYDVQVTA PGAPPLQAET PGSAVDYPLH DLVLHTNYTA TVRGLRGPNL TSPASITFTT 370 380 390 400 410 420 GLEAPRDLEA KEVTPRTALL TWTEPPVRPA GYLLSFHTPG GQNQEILLPG GITSHQLLGL 430 440 450 460 470 480 FPSTSYNARL QAMWGQSLLP PVSTSFTTGG LRIPFPRDCG EEMQNGAGAS RTSTIFLNGN 490 500 510 520 530 540 RERPLNVFCD METDGGGWLV FQRRMDGQTD FWRDWEDYAH GFGNISGEFW LGNEALHSLT 550 560 570 580 590 600 QAGDYSMRVD LRAGDEAVFA QYDSFHVDSA AEYYRLHLEG YHGTAGDSMS YHSGSVFSAR 610 620 630 640 650 660 DRDPNSLLIS CAVSYRGAWW YRNCHYANLN GLYGSTVDHQ GVSWYHWKGF EFSVPFTEMK 670 LRPRNFRSPA GGG
	Isoform 3 [UniParc]. Checksum: 7E07AC46BF6F2599	FASTA	4,242	458,220
	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 AGEDCGEEVP TIEGMRMHLL EETTVRTEWT PAPGPVDAYE 790 800 810 820 830 840 IQFIPTTEGA SPPFTARVPS SASAYDQRGL APGQEYQVTV RALRGTSWGL PASKTITTMI 850 860 870 880 890 900 DGPQDLRVVA VTPTTLELGW LRPQAEVDRF VVSYVSAGNQ RVRLEVPPEA DGTLLTDLMP 910 920 930 940 950 960 GVEYVVTVTA ERGRAVSYPA SVRANTGSSP LGLLGTTDEP PPSGPSTTQG AQAPLLQQRP 970 980 990 1000 1010 1020 QELGELRVLG RDETGRLRVV WTAQPDTFAY FQLRMRVPEG PGAHEEVLPG DVRQALVPPP 1030 1040 1050 1060 1070 1080 PPGTPYELSL HGVPPGGKPS DPIIYQGIMD KDEEKPGKSS GPPRLGELTV TDRTSDSLLL 1090 1100 1110 1120 1130 1140 RWTVPEGEFD SFVIQYKDRD GQPQVVPVEG PQRSAVITSL DPGRKYKFVL YGFVGKKRHG 1150 1160 1170 1180 1190 1200 PLVAEAKILP QSDPSPGTPP HLGNLWVTDP TPDSLHLSWT VPEGQFDTFM VQYRDRDGRP 1210 1220 1230 1240 1250 1260 QVVPVEGPER SFVVSSLDPD HKYRFTLFGI ANKKRYGPLT ADGTTAPERK EEPPRPEFLE 1270 1280 1290 1300 1310 1320 QPLLGELTVT GVTPDSLRLS WTVAQGPFDS FMVQYKDAQG QPQAVPVAGD ENEVTVPGLD 1330 1340 1350 1360 1370 1380 PDRKYKMNLY GLRGRQRVGP ESVVAKTAPQ EDVDETPSPT ELGTEAPESP EEPLLGELTV 1390 1400 1410 1420 1430 1440 TGSSPDSLSL FWTVPQGSFD SFTVQYKDRD GRPRAVRVGG KESEVTVGGL EPGHKYKMHL 1450 1460 1470 1480 1490 1500 YGLHEGQRVG PVSAVGVTAP QQEETPPATE SPLEPRLGEL TVTDVTPNSV GLSWTVPEGQ 1510 1520 1530 1540 1550 1560 FDSFIVQYKD KDGQPQVVPV AADQREVTVY NLEPERKYKM NMYGLHDGQR MGPLSVVIVT 1570 1580 1590 1600 1610 1620 APLPPAPATE ASKPPLEPRL GELTVTDITP DSVGLSWTVP EGEFDSFVVQ YKDRDGQPQV 1630 1640 1650 1660 1670 1680 VPVAADQREV TIPDLEPSRK YKFLLFGIQD GKRRSPVSVE AKTVARGDAS PGAPPRLGEL 1690 1700 1710 1720 1730 1740 WVTDPTPDSL RLSWTVPEGQ FDSFVVQFKD KDGPQVVPVE GHERSVTVTP LDAGRKYRFL 1750 1760 1770 1780 1790 1800 LYGLLGKKRH GPLTADGTTE ARSAMDDTGT KRPPKPRLGE ELQVTTVTQN SVGLSWTVPE 1810 1820 1830 1840 1850 1860 GQFDSFVVQY KDRDGQPQVV PVEGSLREVS VPGLDPAHRY KLLLYGLHHG KRVGPISAVA 1870 1880 1890 1900 1910 1920 ITAGREETET ETTAPTPPAP EPHLGELTVE EATSHTLHLS WMVTEGEFDS FEIQYTDRDG 1930 1940 1950 1960 1970 1980 QLQMVRIGGD RNDITLSGLE SDHRYLVTLY GFSDGKHVGP VHVEALTVPE EEKPSEPPTA 1990 2000 2010 2020 2030 2040 TPEPPIKPRL GELTVTDATP DSLSLSWTVP EGQFDHFLVQ YRNGDGQPKA VRVPGHEEGV 2050 2060 2070 2080 2090 2100 TISGLEPDHK YKMNLYGFHG GQRMGPVSVV GVTAAEEETP SPTEPSMEAP EPAEEPLLGE 2110 2120 2130 2140 2150 2160 LTVTGSSPDS LSLSWTVPQG RFDSFTVQYK DRDGRPQVVR VGGEESEVTV GGLEPGRKYK 2170 2180 2190 2200 2210 2220 MHLYGLHEGR RVGPVSAVGV TAPEEESPDA PLAKLRLGQM TVRDITSDSL SLSWTVPEGQ 2230 2240 2250 2260 2270 2280 FDHFLVQFKN GDGQPKAVRV PGHEDGVTIS GLEPDHKYKM NLYGFHGGQR VGPVSAVGLT 2290 2300 2310 2320 2330 2340 APGKDEEMAP ASTEPPTPEP PIKPRLEELT VTDATPDSLS LSWTVPEGQF DHFLVQYKNG 2350 2360 2370 2380 2390 2400 DGQPKATRVP GHEDRVTISG LEPDNKYKMN LYGFHGGQRV GPVSAIGVTA AEEETPSPTE 2410 2420 2430 2440 2450 2460 PSMEAPEPPE EPLLGELTVT GSSPDSLSLS WTVPQGRFDS FTVQYKDRDG RPQVVRVGGE 2470 2480 2490 2500 2510 2520 ESEVTVGGLE PGRKYKMHLY GLHEGRRVGP VSTVGVTAPQ EDVDETPSPT EPGTEAPGPP 2530 2540 2550 2560 2570 2580 EEPLLGELTV TGSSPDSLSL SWTVPQGRFD SFTVQYKDRD GRPQAVRVGG QESKVTVRGL 2590 2600 2610 2620 2630 2640 EPGRKYKMHL YGLHEGRRLG PVSAVGVTED EAETTQAVPT MTPEPPIKPR LGELTMTDAT 2650 2660 2670 2680 2690 2700 PDSLSLSWTV PEGQFDHFLV QYRNGDGQPK AVRVPGHEDG VTISGLEPDH KYKMNLYGFH 2710 2720 2730 2740 2750 2760 GGQRVGPISV IGVTAAEEET PSPTELSTEA PEPPEEPLLG ELTVTGSSPD SLSLSWTIPQ 2770 2780 2790 2800 2810 2820 GHFDSFTVQY KDRDGRPQVM RVRGEESEVT VGGLEPGRKY KMHLYGLHEG RRVGPVSTVG 2830 2840 2850 2860 2870 2880 VTEDEAETTQ AVPTTTPEPP NKPRLGELTV TDATPDSLSL SWMVPEGQFD HFLVQYRNGD 2890 2900 2910 2920 2930 2940 GQPKVVRVPG HEDGVTISGL EPDHKYKMNL YGFHGGQRVG PISVIGVTAA EEETPAPTEP 2950 2960 2970 2980 2990 3000 STEAPEPPEE PLLGELTVTG SSPDSLSLSW TIPQGRFDSF TVQYKDRDGR PQVVRVRGEE 3010 3020 3030 3040 3050 3060 SEVTVGGLEP GCKYKMHLYG LHEGQRVGPV SAVGVTAPKD EAETTQAVPT MTPEPPIKPR 3070 3080 3090 3100 3110 3120 LGELTVTDAT PDSLSLSWMV PEGQFDHFLV QYRNGDGQPK AVRVPGHEDG VTISGLEPDH 3130 3140 3150 3160 3170 3180 KYKMNLYGFH GGQRVGPVSA IGVTEEETPS PTEPSTEAPE APEEPLLGEL TVTGSSPDSL 3190 3200 3210 3220 3230 3240 SLSWTVPQGR FDSFTVQYKD RDGQPQVVRV RGEESEVTVG GLEPGRKYKM HLYGLHEGQR 3250 3260 3270 3280 3290 3300 VGPVSTVGIT APLPTPLPVE PRLGELAVAA VTSDSVGLSW TVAQGPFDSF LVQYRDAQGQ 3310 3320 3330 3340 3350 3360 PQAVPVSGDL RAVAVSGLDP ARKYKFLLFG LQNGKRHGPV PVEARTAPDT KPSPRLGELT 3370 3380 3390 3400 3410 3420 VTDATPDSVG LSWTVPEGEF DSFVVQYKDK DGRLQVVPVA ANQREVTVQG LEPSRKYRFL 3430 3440 3450 3460 3470 3480 LYGLSGRKRL GPISADSTTA PLEKELPPHL GELTVAEETS SSLRLSWTVA QGPFDSFVVQ 3490 3500 3510 3520 3530 3540 YRDTDGQPRA VPVAADQRTV TVEDLEPGKK YKFLLYGLLG GKRLGPVSAL GMTAPEEDTP 3550 3560 3570 3580 3590 3600 APELAPEAPE PPEEPRLGVL TVTDTTPDSM RLSWSVAQGP FDSFVVQYED TNGQPQALLV 3610 3620 3630 3640 3650 3660 DGDQSKILIS GLEPSTPYRF LLYGLHEGKR LGPLSAEGTT GLAPAGQTSE ESRPRLSQLS 3670 3680 3690 3700 3710 3720 VTDVTTSSLR LNWEAPPGAF DSFLLRFGVP SPSTLEPHPR PLLQRELMVP GTRHSAVLRD 3730 3740 3750 3760 3770 3780 LRSGTLYSLT LYGLRGPHKA DSIQGTARTL SPVLESPRDL QFSEIRETSA KVNWMPPPSR 3790 3800 3810 3820 3830 3840 ADSFKVSYQL ADGGEPQSVQ VDGQARTQKL QGLIPGARYE VTVVSVRGFE ESEPLTGFLT 3850 3860 3870 3880 3890 3900 TVPDGPTQLR ALNLTEGFAV LHWKPPQNPV DTYDVQVTAP GAPPLQAETP GSAVDYPLHD 3910 3920 3930 3940 3950 3960 LVLHTNYTAT VRGLRGPNLT SPASITFTTG LEAPRDLEAK EVTPRTALLT WTEPPVRPAG 3970 3980 3990 4000 4010 4020 YLLSFHTPGG QNQEILLPGG ITSHQLLGLF PSTSYNARLQ AMWGQSLLPP VSTSFTTGGL 4030 4040 4050 4060 4070 4080 RIPFPRDCGE EMQNGAGASR TSTIFLNGNR ERPLNVFCDM ETDGGGWLVF QRRMDGQTDF 4090 4100 4110 4120 4130 4140 WRDWEDYAHG FGNISGEFWL GNEALHSLTQ AGDYSMRVDL RAGDEAVFAQ YDSFHVDSAA 4150 4160 4170 4180 4190 4200 EYYRLHLEGY HGTAGDSMSY HSGSVFSARD RDPNSLLISC AVSYRGAWWY RNCHYANLNG 4210 4220 4230 4240 LYGSTVDHQG VSWYHWKGFE FSVPFTEMKL RPRNFRSPAG GG

References

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[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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.

Web resources

GeneReviews

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.

IPI

IPI00025276.
IPI00218639.
IPI00895929.

PIR

A40701.
A42175.
B42175.
D42175.

RefSeq

NP_061978.6. NM_019105.6.
NP_115859.2. NM_032470.3.

UniGene

Hs.485104.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CUH	NMR	-	A	3890-3991	[»]
2CUI	NMR	-	A	3699-3797	[»]
2CUM	NMR	-	A	3977-4069	[»]

ProteinModelPortal

P22105.

SMR

P22105. Positions 136-878, 983-4279.

ModBase

Search...

Protein-protein interaction databases

IntAct

P22105. 2 interactions.

PTM databases

PhosphoSite

P22105.

Polymorphism databases

DMDM

290457668.

Proteomic databases

PRIDE

P22105.

Protocols and materials databases

DNASU

7148.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375247; ENSP00000364396; ENSG00000168477.
ENST00000451343; ENSP00000407685; ENSG00000168477.
ENST00000546684; ENSP00000447694; ENSG00000236236.
ENST00000550539; ENSP00000448326; ENSG00000229353.

GeneID

7148.

KEGG

hsa:7148.

UCSC

uc003nzg.1. human.
uc003nzl.2. human.

Organism-specific databases

CTD

7148.

GeneCards

GC06M032008.

H-InvDB

HIX0165968.
HIX0207682.

HGNC

HGNC:11976. TNXB.

HPA

CAB005373.

MIM

130020. phenotype.
600985. gene.
606408. phenotype.

neXtProt

NX_P22105.

Orphanet

230839. Ehlers-Danlos syndrome, classic-like type.
285. Ehlers-Danlos syndrome, hypermobility type.

PharmGKB

PA36662.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

HBG006855.

InParanoid

P22105.

KO

K06252.

Gene expression databases

ArrayExpress

P22105.

Bgee

P22105.

Genevestigator

P22105.

GermOnline

ENSG00000168477. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 32 hits.
3.90.215.10. 1 hit.
4.10.530.10. 1 hit.

InterPro

IPR000742. 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]

Pfam

PF00147. Fibrinogen_C. 1 hit.
PF00041. fn3. 31 hits.
PF12661. hEGF. 7 hits.
[Graphical view]

SMART

SM00181. EGF. 9 hits.
SM00186. FBG. 1 hit.
SM00060. FN3. 32 hits.
[Graphical view]

SUPFAM

SSF56496. Fibrinogen_a/b/g_C. 1 hit.
SSF49265. FN_III-like. 33 hits.

PROSITE

PS00022. 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. 33 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

TNXB. human.

EvolutionaryTrace

P22105.

GenomeRNAi

7148.

NextBio

27974.

SOURCE

Search...

Entry information

Entry name

TENX_HUMAN

Accession

Primary (citable) accession number: P22105
Secondary accession number(s): P78530 , 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:	May 1, 2013
This is version 159 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.