TNXB

Tenascin X, znan i kao heksabrahionoliki protein, jest glikoprotein, član porodice tenascina (TN-X), koji je kod ljudi kodiran genom TNXB. Eksprimira se u vezivnom tkivu, uključujući kožu, zglobove i mišiće.^[5]

TNXB
Dostupne strukture PDB Pretraga Human UniProta: PDBe RCSB Spisak PDB ID kodova 2CUH, 2CUI, 2CUM
Identifikatori
Aliasi	TNXB
Vanjski ID-jevi	OMIM: 600985 MGI: 1932137 HomoloGene: 49589 GeneCards: TNXB
Lokacija gena (čovjek) Hrom. Hromosom 6 (čovjek)[1] Bend 6p21.33-p21.32 Početak 32,041,153 bp[1] Kraj 32,115,334 bp[1]
Lokacija gena (miš) Hrom. Hromosom 17 (miš)[2] Bend 17 B1|17 18.24 cM Početak 34,879,431 bp[2] Kraj 34,938,789 bp[2]
Ontologija gena Molekularna funkcija • integrin binding • GO:0001948, GO:0016582 vezivanje za proteine • heparin binding • extracellular matrix structural constituent • collagen fibril binding Ćelijska komponenta • GO:0005578 Vanćelijski matriks • intracellular anatomical structure • fibrillar collagen trimer • Egzosom • Vanćelijsko • extracellular region • collagen-containing extracellular matrix Biološki proces • collagen fibril organization • collagen metabolic process • extracellular matrix organization • Ćelijska adhezija • elastic fiber assembly • actin cytoskeleton organization Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	7148	81877
Ensembl	ENSG00000236236 ENSG00000236221 ENSG00000229353 ENSG00000229341 ENSG00000233323 ENSG00000231608 ENSG00000206258 ENSG00000168477	ENSMUSG00000033327
UniProt	P22105	n/a
RefSeq (mRNK)	NM_032470 NM_019105 NM_001365276	NM_031176
RefSeq (bjelančevina)	NP_061978 NP_115859 NP_001352205	n/a
Lokacija (UCSC)	Chr 6: 32.04 – 32.12 Mb	Chr 17: 34.88 – 34.94 Mb
PubMed pretraga	[3]	[4]
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 4.242 aminokiseline, а molekulska težina 458.220 Da.^[6]

• C: Cistein
• D: Asparaginska kiselina
• E: Glutaminska kiselina
• F: Fenilalanin
• G: Glicin
• H: Histidin
• I: Izoleucin
• K: Lizin
• L: Leucin
• M: Metionin
• N: Asparagin
• P: Prolin
• Q: Glutamin
• R: Arginin
• S: Serin
• T: Treonin
• V: Valin
• W: Triptofan
• Y: Tirozin

10		20		30		40		50
MMPAQYALTS		SLVLLVLLST		ARAGPFSSRS		NVTLPAPRPP		PQPGGHTVGA
GVGSPSSQLY		EHTVEGGEKQ		VVFTHRINLP		PSTGCGCPPG		TEPPVLASEV
QALRVRLEIL		EELVKGLKEQ		CTGGCCPASA		QAGTGQTDVR		TLCSLHGVFD
LSRCTCSCEP		GWGGPTCSDP		TDAEIPPSSP		PSASGSCPDD		CNDQGRCVRG
RCVCFPGYTG		PSCGWPSCPG		DCQGRGRCVQ		GVCVCRAGFS		GPDCSQRSCP
RGCSQRGRCE		GGRCVCDPGY		TGDDCGMRSC		PRGCSQRGRC		ENGRCVCNPG
YTGEDCGVRS		CPRGCSQRGR		CKDGRCVCDP		GYTGEDCGTR		SCPWDCGEGG
RCVDGRCVCW		PGYTGEDCST		RTCPRDCRGR		GRCEDGECIC		DTGYSGDDCG
VRSCPGDCNQ		RGRCEDGRCV		CWPGYTGTDC		GSRACPRDCR		GRGRCENGVC
VCNAGYSGED		CGVRSCPGDC		RGRGRCESGR		CMCWPGYTGR		DCGTRACPGD
CRGRGRCVDG		RCVCNPGFTG		EDCGSRRCPG		DCRGHGLCED		GVCVCDAGYS
GEDCSTRSCP		GGCRGRGQCL		DGRCVCEDGY		SGEDCGVRQC		PNDCSQHGVC
QDGVCICWEG		YVSEDCSIRT		CPSNCHGRGR		CEEGRCLCDP		GYTGPTCATR
MCPADCRGRG		RCVQGVCLCH		VGYGGEDCGQ		EEPPASACPG		GCGPRELCRA
GQCVCVEGFR		GPDCAIQTCP		GDCRGRGECH		DGSCVCKDGY		AGEDCGEEVP
TIEGMRMHLL		EETTVRTEWT		PAPGPVDAYE		IQFIPTTEGA		SPPFTARVPS
SASAYDQRGL		APGQEYQVTV		RALRGTSWGL		PASKTITTMI		DGPQDLRVVA
VTPTTLELGW		LRPQAEVDRF		VVSYVSAGNQ		RVRLEVPPEA		DGTLLTDLMP
GVEYVVTVTA		ERGRAVSYPA		SVRANTGSSP		LGLLGTTDEP		PPSGPSTTQG
AQAPLLQQRP		QELGELRVLG		RDETGRLRVV		WTAQPDTFAY		FQLRMRVPEG
PGAHEEVLPG		DVRQALVPPP		PPGTPYELSL		HGVPPGGKPS		DPIIYQGIMD
KDEEKPGKSS		GPPRLGELTV		TDRTSDSLLL		RWTVPEGEFD		SFVIQYKDRD
GQPQVVPVEG		PQRSAVITSL		DPGRKYKFVL		YGFVGKKRHG		PLVAEAKILP
QSDPSPGTPP		HLGNLWVTDP		TPDSLHLSWT		VPEGQFDTFM		VQYRDRDGRP
QVVPVEGPER		SFVVSSLDPD		HKYRFTLFGI		ANKKRYGPLT		ADGTTAPERK
EEPPRPEFLE		QPLLGELTVT		GVTPDSLRLS		WTVAQGPFDS		FMVQYKDAQG
QPQAVPVAGD		ENEVTVPGLD		PDRKYKMNLY		GLRGRQRVGP		ESVVAKTAPQ
EDVDETPSPT		ELGTEAPESP		EEPLLGELTV		TGSSPDSLSL		FWTVPQGSFD
SFTVQYKDRD		GRPRAVRVGG		KESEVTVGGL		EPGHKYKMHL		YGLHEGQRVG
PVSAVGVTAP		QQEETPPATE		SPLEPRLGEL		TVTDVTPNSV		GLSWTVPEGQ
FDSFIVQYKD		KDGQPQVVPV		AADQREVTVY		NLEPERKYKM		NMYGLHDGQR
MGPLSVVIVT		APLPPAPATE		ASKPPLEPRL		GELTVTDITP		DSVGLSWTVP
EGEFDSFVVQ		YKDRDGQPQV		VPVAADQREV		TIPDLEPSRK		YKFLLFGIQD
GKRRSPVSVE		AKTVARGDAS		PGAPPRLGEL		WVTDPTPDSL		RLSWTVPEGQ
FDSFVVQFKD		KDGPQVVPVE		GHERSVTVTP		LDAGRKYRFL		LYGLLGKKRH
GPLTADGTTE		ARSAMDDTGT		KRPPKPRLGE		ELQVTTVTQN		SVGLSWTVPE
GQFDSFVVQY		KDRDGQPQVV		PVEGSLREVS		VPGLDPAHRY		KLLLYGLHHG
KRVGPISAVA		ITAGREETET		ETTAPTPPAP		EPHLGELTVE		EATSHTLHLS
WMVTEGEFDS		FEIQYTDRDG		QLQMVRIGGD		RNDITLSGLE		SDHRYLVTLY
GFSDGKHVGP		VHVEALTVPE		EEKPSEPPTA		TPEPPIKPRL		GELTVTDATP
DSLSLSWTVP		EGQFDHFLVQ		YRNGDGQPKA		VRVPGHEEGV		TISGLEPDHK
YKMNLYGFHG		GQRMGPVSVV		GVTAAEEETP		SPTEPSMEAP		EPAEEPLLGE
LTVTGSSPDS		LSLSWTVPQG		RFDSFTVQYK		DRDGRPQVVR		VGGEESEVTV
GGLEPGRKYK		MHLYGLHEGR		RVGPVSAVGV		TAPEEESPDA		PLAKLRLGQM
TVRDITSDSL		SLSWTVPEGQ		FDHFLVQFKN		GDGQPKAVRV		PGHEDGVTIS
GLEPDHKYKM		NLYGFHGGQR		VGPVSAVGLT		APGKDEEMAP		ASTEPPTPEP
PIKPRLEELT		VTDATPDSLS		LSWTVPEGQF		DHFLVQYKNG		DGQPKATRVP
GHEDRVTISG		LEPDNKYKMN		LYGFHGGQRV		GPVSAIGVTA		AEEETPSPTE
PSMEAPEPPE		EPLLGELTVT		GSSPDSLSLS		WTVPQGRFDS		FTVQYKDRDG
RPQVVRVGGE		ESEVTVGGLE		PGRKYKMHLY		GLHEGRRVGP		VSTVGVTAPQ
EDVDETPSPT		EPGTEAPGPP		EEPLLGELTV		TGSSPDSLSL		SWTVPQGRFD
SFTVQYKDRD		GRPQAVRVGG		QESKVTVRGL		EPGRKYKMHL		YGLHEGRRLG
PVSAVGVTED		EAETTQAVPT		MTPEPPIKPR		LGELTMTDAT		PDSLSLSWTV
PEGQFDHFLV		QYRNGDGQPK		AVRVPGHEDG		VTISGLEPDH		KYKMNLYGFH
GGQRVGPISV		IGVTAAEEET		PSPTELSTEA		PEPPEEPLLG		ELTVTGSSPD
SLSLSWTIPQ		GHFDSFTVQY		KDRDGRPQVM		RVRGEESEVT		VGGLEPGRKY
KMHLYGLHEG		RRVGPVSTVG		VTEDEAETTQ		AVPTTTPEPP		NKPRLGELTV
TDATPDSLSL		SWMVPEGQFD		HFLVQYRNGD		GQPKVVRVPG		HEDGVTISGL
EPDHKYKMNL		YGFHGGQRVG		PISVIGVTAA		EEETPAPTEP		STEAPEPPEE
PLLGELTVTG		SSPDSLSLSW		TIPQGRFDSF		TVQYKDRDGR		PQVVRVRGEE
SEVTVGGLEP		GCKYKMHLYG		LHEGQRVGPV		SAVGVTAPKD		EAETTQAVPT
MTPEPPIKPR		LGELTVTDAT		PDSLSLSWMV		PEGQFDHFLV		QYRNGDGQPK
AVRVPGHEDG		VTISGLEPDH		KYKMNLYGFH		GGQRVGPVSA		IGVTEEETPS
PTEPSTEAPE		APEEPLLGEL		TVTGSSPDSL		SLSWTVPQGR		FDSFTVQYKD
RDGQPQVVRV		RGEESEVTVG		GLEPGRKYKM		HLYGLHEGQR		VGPVSTVGIT
APLPTPLPVE		PRLGELAVAA		VTSDSVGLSW		TVAQGPFDSF		LVQYRDAQGQ
PQAVPVSGDL		RAVAVSGLDP		ARKYKFLLFG		LQNGKRHGPV		PVEARTAPDT
KPSPRLGELT		VTDATPDSVG		LSWTVPEGEF		DSFVVQYKDK		DGRLQVVPVA
ANQREVTVQG		LEPSRKYRFL		LYGLSGRKRL		GPISADSTTA		PLEKELPPHL
GELTVAEETS		SSLRLSWTVA		QGPFDSFVVQ		YRDTDGQPRA		VPVAADQRTV
TVEDLEPGKK		YKFLLYGLLG		GKRLGPVSAL		GMTAPEEDTP		APELAPEAPE
PPEEPRLGVL		TVTDTTPDSM		RLSWSVAQGP		FDSFVVQYED		TNGQPQALLV
DGDQSKILIS		GLEPSTPYRF		LLYGLHEGKR		LGPLSAEGTT		GLAPAGQTSE
ESRPRLSQLS		VTDVTTSSLR		LNWEAPPGAF		DSFLLRFGVP		SPSTLEPHPR
PLLQRELMVP		GTRHSAVLRD		LRSGTLYSLT		LYGLRGPHKA		DSIQGTARTL
SPVLESPRDL		QFSEIRETSA		KVNWMPPPSR		ADSFKVSYQL		ADGGEPQSVQ
VDGQARTQKL		QGLIPGARYE		VTVVSVRGFE		ESEPLTGFLT		TVPDGPTQLR
ALNLTEGFAV		LHWKPPQNPV		DTYDVQVTAP		GAPPLQAETP		GSAVDYPLHD
LVLHTNYTAT		VRGLRGPNLT		SPASITFTTG		LEAPRDLEAK		EVTPRTALLT
WTEPPVRPAG		YLLSFHTPGG		QNQEILLPGG		ITSHQLLGLF		PSTSYNARLQ
AMWGQSLLPP		VSTSFTTGGL		RIPFPRDCGE		EMQNGAGASR		TSTIFLNGNR
ERPLNVFCDM		ETDGGGWLVF		QRRMDGQTDF		WRDWEDYAHG		FGNISGEFWL
GNEALHSLTQ		AGDYSMRVDL		RAGDEAVFAQ		YDSFHVDSAA		EYYRLHLEGY
HGTAGDSMSY		HSGSVFSARD		RDPNSLLISC		AVSYRGAWWY		RNCHYANLNG
LYGSTVDHQG		VSWYHWKGFE		FSVPFTEMKL		RPRNFRSPAG		GG

Gen

Ovaj gen nalazi se u područje glavnog kompleksa histokompatibilnosti (MHC-klasa III) na hromosomu 6. Struktura ovog gena je neobična po tome što se preklapa s genima CREBL1 i CYP21A2 na svom 5' i 3' kraju.^[7]

Funkcija

Ovaj gen kodira člana tenascinske porodice glikoproteina vanćelijskog matriksa. Tenascini imaju anti-adhezivno dejstvo, za razliku od fibronektina koji je ljepljiv. Smatra se da ovaj protein funkcionira u sazrijevanju matriksa tokom zacjeljivanja rana.^[7]

Klinički značaj

Nedostatak tenascina uzrokuje klasični oblik Ehlers-Danlosovog sindroma, gdje se gustoća kolagena smanjuje, a elastična vlakna fragmentiraju.^[8]

Reference

1. ENSG00000236221, ENSG00000229353, ENSG00000229341, ENSG00000233323, ENSG00000231608, ENSG00000206258, ENSG00000168477 GRCh38: Ensembl release 89: ENSG00000236236, ENSG00000236221, ENSG00000229353, ENSG00000229341, ENSG00000233323, ENSG00000231608, ENSG00000206258, ENSG00000168477 - Ensembl, maj 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000033327 - Ensembl, maj 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Tee MK, Thomson AA, Bristow J, Miller WL (juli 1995). "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". Genomics. 28 (2): 171–8. doi:10.1006/geno.1995.1128. PMID 8530023.
6. "UniProt, P22105". Pristupljeno 5. 10. 2021. Zanemaren tekst "languageeng." (pomoć)
7. "Entrez Gene: tenascin XB".
8. Zweers, MC; Schalkwijk, J; Van Kuppevelt, TH; Van Vlijmen-Willems, IM; Bergers, M; Lethias, C; Lamme, EN (2005). "Transplantation of reconstructed human skin on nude mice: a model system to study expression of human tenascin-X and elastic fiber components". Cell and Tissue Research. 319 (2): 279–87. doi:10.1007/s00441-004-1011-6. PMID 15558324. S2CID 5889106.

Dopunska literatura

• Goepel C (2008). "Differential elastin and tenascin immunolabeling in the uterosacral ligaments in postmenopausal women with and without pelvic organ prolapse". Acta Histochem. 110 (3): 204–9. doi:10.1016/j.acthis.2007.10.014. PMID 18155129.
• Yuan Y, Nymoen DA, Stavnes HT, et al. (2009). "Tenascin-X is a novel diagnostic marker of malignant mesothelioma". Am. J. Surg. Pathol. 33 (11): 1673–82. doi:10.1097/PAS.0b013e3181b6bde3. PMC 2783994. PMID 19738457.
• Egging D, van Vlijmen-Willems I, van Tongeren T, et al. (2007). "Wound healing in tenascin-X deficient mice suggests that tenascin-X is involved in matrix maturation rather than matrix deposition". Connect. Tissue Res. 48 (2): 93–8. doi:10.1080/03008200601166160. PMID 17453911. S2CID 34586536.
• Egging DF, van Vlijmen-Willems I, Choi J, et al. (2008). "Analysis of obstetric complications and uterine connective tissue in tenascin-X-deficient humans and mice". Cell Tissue Res. 332 (3): 523–32. doi:10.1007/s00441-008-0591-y. PMC 2386751. PMID 18335242.
• Kato A, Endo T, Abiko S, et al. (2008). "Induction of truncated form of tenascin-X (XB-S) through dissociation of HDAC1 from SP-1/HDAC1 complex in response to hypoxic conditions". Exp. Cell Res. 314 (14): 2661–73. doi:10.1016/j.yexcr.2008.05.019. PMID 18588874.
• Bristow J, Carey W, Egging D, Schalkwijk J (2005). "Tenascin-X, collagen, elastin, and the Ehlers-Danlos syndrome". American Journal of Medical Genetics. 139C (1): 24–30. doi:10.1002/ajmg.c.30071. PMID 16278880. S2CID 23825221.
• Fellay J, Ge D, Shianna KV, et al. (2009). McCarthy MI (ured.). "Common genetic variation and the control of HIV-1 in humans". PLOS Genet. 5 (12): e1000791. doi:10.1371/journal.pgen.1000791. PMC 2791220. PMID 20041166.
• Kamatani Y, Matsuda K, Ohishi T, et al. (2008). "Identification of a significant association of a single nucleotide polymorphism in TNXB with systemic lupus erythematosus in a Japanese population". J. Hum. Genet. 53 (1): 64–73. doi:10.1007/s10038-007-0219-1. PMID 18058064.
• Valdes AM, Thomson G (2009). "Several loci in the HLA class III region are associated with T1D risk after adjusting for DRB1-DQB1". Diabetes Obes Metab. 11. Suppl 1: 46–52. doi:10.1111/j.1463-1326.2008.01002.x. PMC 2755069. PMID 19143814.
• Yu CY (1998). "Molecular genetics of the human MHC complement gene cluster". Exp. Clin. Immunogenet. 15 (4): 213–30. doi:10.1159/000019075. PMID 10072631. S2CID 25061446.
• Endo T, Ariga H, Matsumoto K (2009). "Truncated form of tenascin-X, XB-S, interacts with mitotic motor kinesin Eg5". Mol. Cell. Biochem. 320 (1–2): 53–66. doi:10.1007/s11010-008-9898-y. PMID 18679583. S2CID 23394214.
• Sovio U, Bennett AJ, Millwood IY, et al. (2009). Gibson G (ured.). "Genetic determinants of height growth assessed longitudinally from infancy to adulthood in the northern Finland birth cohort 1966". PLOS Genet. 5 (3): e1000409. doi:10.1371/journal.pgen.1000409. PMC 2646138. PMID 19266077.
• Araújo VC, Furuse C, Cury PR, et al. (2008). "Tenascin and fibronectin expression in carcinoma ex pleomorphic adenoma". Appl. Immunohistochem. Mol. Morphol. 16 (1): 48–53. doi:10.1097/PAI.0b013e31802eff1c. PMID 18091320. S2CID 23304572.
• Gudbjartsson DF, Walters GB, Thorleifsson G, et al. (2008). "Many sequence variants affecting diversity of adult human height". Nat. Genet. 40 (5): 609–15. doi:10.1038/ng.122. PMID 18391951. S2CID 3005450.
• Barcellos LF, May SL, Ramsay PP, et al. (2009). Roopenian DC (ured.). "High-density SNP screening of the major histocompatibility complex in systemic lupus erythematosus demonstrates strong evidence for independent susceptibility regions". PLOS Genet. 5 (10): e1000696. doi:10.1371/journal.pgen.1000696. PMC 2758598. PMID 19851445.
• McKinnon E, Morahan G, Nolan D, et al. (2009). "Association of MHC SNP genotype with susceptibility to type 1 diabetes: a modified survival approach". Diabetes Obes Metab. 11 (Suppl 1): 92–100. doi:10.1111/j.1463-1326.2008.01009.x. PMC 2755510. PMID 19143821.
• Chapuis J, Hot D, Hansmannel F, et al. (2009). "Transcriptomic and genetic studies identify IL-33 as a candidate gene for Alzheimer's disease". Mol. Psychiatry. 14 (11): 1004–16. doi:10.1038/mp.2009.10. PMC 2860783. PMID 19204726.
• Vignal C, Bansal AT, Balding DJ, et al. (2009). "Genetic association of the major histocompatibility complex with rheumatoid arthritis implicates two non-DRB1 loci". Arthritis Rheum. 60 (1): 53–62. doi:10.1002/art.24138. PMID 19116923.
• Buysschaert ID, Grulois V, Eloy P, et al. (2010). "Genetic evidence for a role of IL33 in nasal polyposis". Allergy. 65 (5): 616–22. doi:10.1111/j.1398-9995.2009.02227.x. PMID 19860791. S2CID 33878118.
• Gudbjartsson DF, Bjornsdottir US, Halapi E, et al. (2009). "Sequence variants affecting eosinophil numbers associate with asthma and myocardial infarction". Nat. Genet. 41 (3): 342–7. doi:10.1038/ng.323. PMID 19198610. S2CID 4964308.

Vanjski linkovi

• GeneReviews/NCBI/NIH/UW entry on Ehlers-Danlos Syndrome, Hypermobility Type

Ovaj članak uključuje tekst iz Nacionalne medicinske biblioteke Sjedinjenih Država, koji je u javnom vlasništvu.