Titin

TTN
Dostupne strukture PDB Pretraga ortologa: PDBe RCSB Spisak PDB ID kodova 4UOW, 1BPV, 1G1C, 1NCT, 1NCU, 1TIT, 1TIU, 1TKI, 1TNM, 1TNN, 1WAA, 1YA5, 2A38, 2BK8, 2F8V, 2ILL, 2J8H, 2J8O, 2NZI, 2RQ8, 2WP3, 2WWK, 2WWM, 2Y9R, 3KNB, 3LCY, 3LPW, 3PUC, 3Q5O, 3QP3, 4C4K, 4JNW, 4O00, 4QEG, 5BS0
Identifikatori
Aliasi	TTN, CMD1G, CMH9, CMPD4, EOMFC, HMERF, LGMD2J, MYLK5, TMD, titin, SALMY, LGMDR10
Vanjski ID-jevi	OMIM: 188840 MGI: 98864 HomoloGene: 130650 GeneCards: TTN
EC broj	2.7.11.1
Lokacija gena (čovjek) Hrom. Hromosom 2 (čovjek)[1] Bend 2q31.2 Početak 178,525,989 bp[1] Kraj 178,830,802 bp[1]
Lokacija gena (miš) Hrom. Hromosom 2 (miš)[2] Bend 2 C3|2 45.13 cM Početak 76,703,980 bp[2] Kraj 76,982,547 bp[2]
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • aktivnost sa transferazom • nucleotide binding • calcium ion binding • protein kinase activity • actinin binding • muscle alpha-actinin binding • structural molecule activity conferring elasticity • vezivanje iona metala • telethonin binding • protease binding • protein self-association • actin filament binding • protein serine/threonine kinase activity • kinase activity • GO:0001948, GO:0016582 vezivanje za proteine • vezivanje identičnih proteina • vezivanje enzima • protein tyrosine kinase activity • structural constituent of muscle • ATP binding • protein kinase binding • calmodulin binding Ćelijska komponenta • citoplazma • citosol • I band • striated muscle thin filament • kondenzovani nuklearni hromosom • extracellular region • Z discdkac • muscle myosin complex • Egzosom • jedro • M band • Sarkomera Biološki proces • sarcomerogenesis • Mišićna kontrakcija • mitotic chromosome condensation • cardiac muscle contraction • Fosforilacija • cardiac muscle hypertrophy • platelet degranulation • cardiac muscle tissue morphogenesis • skeletal muscle thin filament assembly • detection of muscle stretch • response to calcium ion • cardiac myofibril assembly • protein phosphorylation • muscle filament sliding • regulation of protein kinase activity • GO:0048552 regulation of catalytic activity • sarcomere organization • skeletal muscle myosin thick filament assembly • striated muscle contraction • peptidyl-tyrosine phosphorylation • GO:1901313 positive regulation of gene expression • protein kinase A signaling • positive regulation of protein secretion Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	7273	22138
Ensembl	ENSG00000155657	ENSMUSG00000051747
UniProt	Q8WZ42	A2ASS6
RefSeq (mRNK)	NM_001256850 NM_001267550 NM_003319 NM_133378 NM_133379 NM_133432 NM_133437	NM_011652 NM_028004
RefSeq (bjelančevina)	NP_001243779 NP_001254479 NP_003310 NP_596869 NP_596870 NP_597676 NP_597681	NP_035782 NP_082280 NP_001372637
Lokacija (UCSC)	Chr 2: 178.53 – 178.83 Mb	Chr 2: 76.7 – 76.98 Mb
PubMed pretraga	[3]	[4]
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Titin – poznat i kao konektin – je protein kojeg kod čovjeka kodira genTTN.^[5][6] Titin je džinovski protein, dužine veće od 1 µm,^[7] koja funkcionira kao molekularna opruga koja je odgovorna za pasivnu elastičnost mišića, uz to što održava molekule miozina na mjestu. Sastoji se od 244 pojedinačno presavijenih domena proteina povezanih nestrukturiranim peptidnim sekvencama.^[8] Ovi domeni se opružaju kada se protein proteže i ponovo se savijaju kada prestane napetost.^[9]

Titin je važan u kontrakciji prugastog mišićnog tkiva . Povezuje Z-linije sa M linijamq u sarkomerama. Protein doprinosi prenošenju sile na liniji Z i napetosti u mirovanju u regiji I pruge.^[10] Ograničava opseg pokreta sarkomera u napetosti, pridonoseći tako pasivnoj krutosti mišića. Varijacije u sekvenci titina između različitih vrsta mišića (npr. srčanog ili skeletnog) povezane su sa razlikama u mehaničkim svojstvima tih mišića.^[5][11]

Titin je treći najzastupljeniji protein u mišićima (nakon miozina i aktina), a odrasli čovjek sadrži otprilike 0,5 kg titina.^[12] Sa svojom dužinom od ~27.000 do ~35.000 aminokiselina (ovisno o izomorfnom spoju), titin je najveći poznati protein.^[13] Gen za titin sadrži najveći broj egzona (363) otkrivenih u bilo kojem jedinom genu,^[14] kao i najduži pojedinačni egzon (17.106 bp).

1. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000155657 - Ensembl, maj 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000051747 - 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. ^ ^{a b} "Entrez Gene: TTN titin".
6. ^ Labeit S, Barlow DP, Gautel M, Gibson T, Holt J, Hsieh CL, Francke U, Leonard K, Wardale J, Whiting A (maj 1990). "A regular pattern of two types of 100-residue motif in the sequence of titin". Nature. 345 (6272): 273–6. doi:10.1038/345273a0. PMID 2129545.
7. ^ Eric H. Lee. "The Chain-like Elasticity of Titin". Theoretical and Computational Biophysics Group, University of Illinois. Pristupljeno 25. 9. 2014.
8. ^ Labeit S, Kolmerer B (oktobar 1995). "Titins: giant proteins in charge of muscle ultrastructure and elasticity". Science. 270 (5234): 293–6. doi:10.1126/science.270.5234.293. PMID 7569978.
9. ^ Minajeva A, Kulke M, Fernandez JM, Linke WA (mart 2001). "Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils". Biophysical Journal. 80 (3): 1442–51. doi:10.1016/S0006-3495(01)76116-4. PMC 1301335. PMID 11222304.
10. ^ Itoh-Satoh M, Hayashi T, Nishi H, Koga Y, Arimura T, Koyanagi T, Takahashi M, Hohda S, Ueda K, Nouchi T, Hiroe M, Marumo F, Imaizumi T, Yasunami M, Kimura A (februar 2002). "Titin mutations as the molecular basis for dilated cardiomyopathy". Biochemical and Biophysical Research Communications. 291 (2): 385–93. doi:10.1006/bbrc.2002.6448. PMID 11846417.
11. ^ OMIM: 188840
12. ^ Labeit S, Kolmerer B, Linke WA (februar 1997). "The giant protein titin. Emerging roles in physiology and pathophysiology". Circulation Research. 80 (2): 290–4. doi:10.1161/01.RES.80.2.290. PMID 9012751.
13. ^ Opitz CA, Kulke M, Leake MC, Neagoe C, Hinssen H, Hajjar RJ, Linke WA (oktobar 2003). "Damped elastic recoil of the titin spring in myofibrils of human myocardium". Proceedings of the National Academy of Sciences of the United States of America. 100 (22): 12688–93. doi:10.1073/pnas.2133733100. PMC 240679. PMID 14563922.
14. ^ Bang ML, Centner T, Fornoff F, Geach AJ, Gotthardt M, McNabb M, Witt CC, Labeit D, Gregorio CC, Granzier H, Labeit S (novembar 2001). "The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system". Circulation Research. 89 (11): 1065–72. doi:10.1161/hh2301.100981. PMID 11717165.