UniProtKB - P54939 (TLN1_CHICK)
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Protein
Talin-1
Gene
TLN1
Organism
Gallus gallus (Chicken)
Status
Functioni
Probably involved in connections of major cytoskeletal structures to the plasma membrane. Talin is a high molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts.
GO - Molecular functioni
- actin filament binding Source: InterPro
- structural constituent of cytoskeleton Source: InterPro
GO - Biological processi
- cell adhesion Source: InterPro
- cytoskeletal anchoring at plasma membrane Source: InterPro
Names & Taxonomyi
| Protein namesi | Recommended name: Talin-1 |
| Gene namesi | Name:TLN1 Synonyms:TLN |
| Organismi | Gallus gallus (Chicken) |
| Taxonomic identifieri | 9031 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archelosauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galloanserae › Galliformes › Phasianidae › Phasianinae › Gallus |
| Proteomesi |
|
Subcellular locationi
- Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side
- Cytoplasm › cytoskeleton
- Cell surface By similarity
- Cell junction › focal adhesion By similarity
Note: Colocalizes with LAYN at the membrane ruffles.
GO - Cellular componenti
- cell surface Source: UniProtKB-SubCell
- cytoskeleton Source: UniProtKB-SubCell
- cytosol Source: HGNC
- focal adhesion Source: HGNC
- ruffle Source: HGNC
- ruffle membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, MembranePTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| ChainiPRO_0000219430 | 1 – 2541 | Talin-1Add BLAST | 2541 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| GlycosylationiCAR_000155 | 1486 | O-linked (GlcNAc) threonine1 Publication | 1 | |
| GlycosylationiCAR_000156 | 1889 | O-linked (GlcNAc) threonine1 Publication | 1 |
Post-translational modificationi
Phosphorylated.By similarity
Keywords - PTMi
Glycoprotein, PhosphoproteinProteomic databases
| PaxDbi | P54939. |
| PRIDEi | P54939. |
PTM databases
| UniCarbKBi | P54939. |
Interactioni
Subunit structurei
Interacts with PIP5K1C and NRAP (By similarity). Binds with high affinity to vinculin and with low affinity to integrins. Interacts with APBB1IP; this inhibits VCL binding. May interact with F-actin. Interacts with LAYN.By similarity4 Publications
Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ITGB3 | P05106 | 2 | EBI-1035421,EBI-702847 | From Homo sapiens. |
GO - Molecular functioni
- actin filament binding Source: InterPro
Protein-protein interaction databases
| DIPi | DIP-35571N. |
| IntActi | P54939. 3 interactors. |
| STRINGi | 9031.ENSGALP00000038501. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Helixi | 201 – 205 | Combined sources | 5 | |
| Helixi | 209 – 224 | Combined sources | 16 | |
| Beta strandi | 226 – 228 | Combined sources | 3 | |
| Helixi | 232 – 247 | Combined sources | 16 | |
| Turni | 252 – 254 | Combined sources | 3 | |
| Turni | 257 – 259 | Combined sources | 3 | |
| Helixi | 262 – 264 | Combined sources | 3 | |
| Helixi | 268 – 270 | Combined sources | 3 | |
| Helixi | 276 – 285 | Combined sources | 10 | |
| Turni | 286 – 288 | Combined sources | 3 | |
| Helixi | 291 – 304 | Combined sources | 14 | |
| Turni | 306 – 309 | Combined sources | 4 | |
| Beta strandi | 311 – 317 | Combined sources | 7 | |
| Beta strandi | 320 – 322 | Combined sources | 3 | |
| Beta strandi | 326 – 332 | Combined sources | 7 | |
| Beta strandi | 334 – 341 | Combined sources | 8 | |
| Turni | 342 – 344 | Combined sources | 3 | |
| Beta strandi | 347 – 352 | Combined sources | 6 | |
| Helixi | 353 – 355 | Combined sources | 3 | |
| Beta strandi | 358 – 361 | Combined sources | 4 | |
| Beta strandi | 363 – 369 | Combined sources | 7 | |
| Helixi | 371 – 373 | Combined sources | 3 | |
| Beta strandi | 374 – 376 | Combined sources | 3 | |
| Beta strandi | 378 – 381 | Combined sources | 4 | |
| Helixi | 385 – 393 | Combined sources | 9 | |
| Helixi | 823 – 841 | Combined sources | 19 | |
| Helixi | 855 – 873 | Combined sources | 19 | |
| Turni | 1945 – 1947 | Combined sources | 3 | |
| Helixi | 1948 – 1966 | Combined sources | 19 | |
| Helixi | 2345 – 2361 | Combined sources | 17 |
3D structure databases
| Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1MIX | X-ray | 1.75 | A | 196-400 | [»] | |
| 1MIZ | X-ray | 1.90 | B | 200-400 | [»] | |
| 1MK7 | X-ray | 2.20 | B/D | 209-400 | [»] | |
| 1MK9 | X-ray | 2.80 | B/D/F/H | 209-400 | [»] | |
| 1RKC | X-ray | 2.70 | B | 1944-1969 | [»] | |
| 1U6H | X-ray | 2.38 | B | 849-879 | [»] | |
| 1XWJ | X-ray | 2.60 | B | 1944-1969 | [»] | |
| 1ZVZ | X-ray | 1.80 | B | 820-844 | [»] | |
| 1ZW2 | X-ray | 2.10 | B | 2344-2368 | [»] | |
| 2H7D | NMR | - | A | 309-405 | [»] | |
| 2H7E | NMR | - | A | 309-405 | [»] | |
| 2HRJ | NMR | - | A | 189-309 | [»] | |
| 2K00 | NMR | - | A | 309-400 | [»] | |
| ProteinModelPortali | P54939. | |||||
| SMRi | P54939. | |||||
| ModBasei | Search... | |||||
| MobiDBi | Search... | |||||
Miscellaneous databases
| EvolutionaryTracei | P54939. |
Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Domaini | 86 – 403 | FERMPROSITE-ProRule annotationAdd BLAST | 318 | |
| Domaini | 2292 – 2531 | I/LWEQPROSITE-ProRule annotationAdd BLAST | 240 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Regioni | 280 – 435 | Interaction with LAYN1 PublicationAdd BLAST | 156 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Compositional biasi | 672 – 681 | Poly-Ala | 10 | |
| Compositional biasi | 1335 – 1340 | Poly-Ala | 6 |
Phylogenomic databases
| eggNOGi | KOG4261. Eukaryota. ENOG410XQ0V. LUCA. |
| HOVERGENi | HBG023870. |
| InParanoidi | P54939. |
| KOi | K06271. |
| PhylomeDBi | P54939. |
Family and domain databases
| CDDi | cd14473. FERM_B-lobe. 1 hit. |
| Gene3Di | 1.20.80.10. 1 hit. 2.30.29.30. 1 hit. |
| InterProi | View protein in InterPro IPR019749. Band_41_domain. IPR014352. FERM/acyl-CoA-bd_prot_3-hlx. IPR019748. FERM_central. IPR019747. FERM_CS. IPR000299. FERM_domain. IPR032425. FERM_f0. IPR018979. FERM_N. IPR002558. ILWEQ_dom. IPR011993. PH_dom-like. IPR015710. Talin-1. IPR015224. Talin_cent. IPR029071. Ubiquitin-rel_dom. IPR015009. Vinculin-bd_dom. IPR006077. Vinculin/catenin. |
| PANTHERi | PTHR19981:SF24. PTHR19981:SF24. 1 hit. |
| Pfami | View protein in Pfam PF16511. FERM_f0. 1 hit. PF00373. FERM_M. 1 hit. PF09379. FERM_N. 1 hit. PF01608. I_LWEQ. 1 hit. PF09141. Talin_middle. 1 hit. PF08913. VBS. 2 hits. |
| ProDomi | View protein in ProDom or Entries sharing at least one domain PD011820. ILWEQ. 1 hit. |
| SMARTi | View protein in SMART SM00295. B41. 1 hit. SM00307. ILWEQ. 1 hit. |
| SUPFAMi | SSF109880. SSF109880. 1 hit. SSF109885. SSF109885. 4 hits. SSF47031. SSF47031. 1 hit. SSF47220. SSF47220. 5 hits. SSF50729. SSF50729. 1 hit. SSF54236. SSF54236. 1 hit. |
| PROSITEi | View protein in PROSITE PS00660. FERM_1. 1 hit. PS00661. FERM_2. 1 hit. PS50057. FERM_3. 1 hit. PS50945. I_LWEQ. 1 hit. |
Sequencei
Sequence statusi: Complete.
P54939-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MVALSLKISI GNVVKTMQFE PSTMVYDACR MIRERVPEAQ MGQPNDFGLF
60 70 80 90 100
LSDEDPKKGI WLEAGKALDY YMLRNGDTME YKKKQRPLKI RMLDGTVKTV
110 120 130 140 150
MVDDSKTVTD MLTTICARIG ITNYDEYSLV REIMEEKKEE VTGTLKKDKT
160 170 180 190 200
LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL REQGIDDNET LLLRRKFFYS
210 220 230 240 250
DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG YQCQIQFGPH
260 270 280 290 300
NEQKHKPGFL ELKDFLPKEY IKQKGERKIF MAHKNCGNMS EIEAKVRYVK
310 320 330 340 350
LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE
360 370 380 390 400
WSLTNIKRWA ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL
410 420 430 440 450
KKKKSKDHFG LEGDEESTML EDSVSPKKST VLQQQFNRVG KAELGSVALP
460 470 480 490 500
AIMRTGAGGP ENFQVGTMPQ AQMQITSGQM HRGHMPPLTS AQQALTGTIN
510 520 530 540 550
SSMQAVNAAQ ATLDDFETLP PLGQDAASKA WRKNKMDESK HEIHSQADAI
560 570 580 590 600
TAGTASVVNL TAGDPADTDY TAVGCAVTTI SSNLTEMSKG VKLLAALMED
610 620 630 640 650
EGGNGRQLLQ AAKNLASAVS DLLKTAQPAS AEPRQNLLQA AGLVGQTSGE
660 670 680 690 700
LLQQIGESDT DPRFQDMLMQ LAKAVASAAA ALVLKAKNVA QKTEDSALQT
710 720 730 740 750
QVIAAATQCA LSTSQLVACT KVVAPTISSP VCQEQLIEAG KLVAKSAEGC
760 770 780 790 800
VEASKAATND DQLLKQVGVA ATAVTQALND LLQHIKQHAT GGQPIGRYDQ
810 820 830 840 850
ATDTILNVTE NIFSSMGDAG EMVRQARILA QATSDLVNAI KADAEGETDL
860 870 880 890 900
ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA
910 920 930 940 950
TNAAAQNAIK KKLVHKLEHA AKQAAASATQ TIAAAQHAAA SNKNPAAQQQ
960 970 980 990 1000
LVQSCKVVAD QIPMLVQGVR GSQSQPDSPS AQLALIAASQ NFLQPGGKMV
1010 1020 1030 1040 1050
AAAKATVPTI TDQASAMQLS QCAKNLAAAL AELRTAAQKA QEACGPLEID
1060 1070 1080 1090 1100
SALGLVQSLE RDLKEAKAAA RDGKLKPLPG ETMEKCAQDL GNSTKAVTSA
1110 1120 1130 1140 1150
IAHLLGEVAQ GNENYTGIAA REVAQALRSL SQAARGVAAN SSDPQAQNAM
1160 1170 1180 1190 1200
LECASDVMDK ANNLIEEARK AVAKPGDPDS QQRLVQVAKA VSQALNRCVN
1210 1220 1230 1240 1250
CLPGQRDVDA AIRMVGEASK RLLSDSFPPS NKTFQEAQSQ LNRAAAGLNQ
1260 1270 1280 1290 1300
SANELVQASR GTPQDLAKSS GKFGQDFNEF LQAGVEMASL SPTKEDQAQV
1310 1320 1330 1340 1350
VSNLKSISMS SSKLLLAAKA LSADPTSPNL KSQLAAAARA VTDSINQLIT
1360 1370 1380 1390 1400
MCTQQAPGQK ECDNALRELE TVKELLENPT QTVNDMSYFS CLDSVMENSK
1410 1420 1430 1440 1450
VLGESMAGIS QNAKNSKLPE FGESISAASK ALCGLTEAAA QAAYLVGVSD
1460 1470 1480 1490 1500
PNSQAGQQGL VDPTQFARAN QAIQMACQNL VDPACTQSQV LSAATIVAKH
1510 1520 1530 1540 1550
TSALCNTCRL ASSRTANPVA KRQFVQPAKE VANSTANLVK TIKALDGAFN
1560 1570 1580 1590 1600
EENRERCRAA TAPLIEAVDN LTAFASNPEF ATVPAQISPE GRRAMEPIVT
1610 1620 1630 1640 1650
SAKTMLESSA GLIQTARSLA VNPKDPPQWS VLAGHSRTVS DSIKKLITNM
1660 1670 1680 1690 1700
RDKAPGQREC DEAIDVLNRC MREVDQASLA AISQQLAPRE GISQEALHNQ
1710 1720 1730 1740 1750
MITAVQEINN LIEPVASAAR AEASQLGHKV SQMAQYFEPL ILAAIGAASK
1760 1770 1780 1790 1800
TPNHQQQMNL LDQTKTLAES ALQMLYTAKE AGGNPKQAAH TQEALEEAVQ
1810 1820 1830 1840 1850
MMKEAVEDLT TTLNEAASAA GVVGGMVDSI TQAINQLDEG PMGEPEGTFV
1860 1870 1880 1890 1900
DYQTTMVKTA KAIAVTVQEM VTKSTTNPDE LGILANQLTN DYGQLAQQAK
1910 1920 1930 1940 1950
PAALTAENEE IGSHIKRRVQ ELGHGCAALV TKAGALQCSP SDAYTKKELI
1960 1970 1980 1990 2000
ESARKVSEKV SHVLAALQAG NRGTQACITA ASAVSGIIAD LDTTIMFATA
2010 2020 2030 2040 2050
GTLNRENSET FADHREGILK TAKALVEDTK VLVQNATASQ EKLAQAAQSS
2060 2070 2080 2090 2100
VSTITRLAEV VKLGAASLGS EDPETQVVLI NAVKDVAKAL GDLIGATKAA
2110 2120 2130 2140 2150
AGKAGDDPAV YQLKNSAKVM VTNVTSLLKT VKAVEDEATK GTRALEATIE
2160 2170 2180 2190 2200
HIRQELAVFS SPVPPAQVST PEDFIRMTKG ITMATAKAVA AGNSCRQEDV
2210 2220 2230 2240 2250
IATANLSRRA IADMLRACKE AAYHPEVSAD VRQRALRFGK ECADGYLELL
2260 2270 2280 2290 2300
EHVLVILQKP THELKQQLAG YSKRVASSVT ELIQAAEAMK GTEWVDPEDP
2310 2320 2330 2340 2350
TVIAENELLG AAAAIEAAAK KLEQLKPRAK PKQADESLDF EEQILEAAKS
2360 2370 2380 2390 2400
IAAATSALVK AASAAQRELV AQGKVGVIPA NAVDDGQWSQ GLISAARMVA
2410 2420 2430 2440 2450
AATNNLCEAA NAAVQGHASE EKLISSAKQV AASTAQLLVA CKVKADHDSE
2460 2470 2480 2490 2500
AMKRLQAAGN AVKRASDNLV KAAQKAAAFQ DHDETVVVKE KMVGGIAQII
2510 2520 2530 2540
AAQEEMLRKE RELEEARKKL AMIRQQQYKF LPTELRDEEQ N
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY150847 mRNA. Translation: AAN75275.1. |
| PIRi | B42965. D42965. |
| RefSeqi | NP_989854.1. NM_204523.1. |
| UniGenei | Gga.4319. |
Genome annotation databases
| GeneIDi | 395194. |
| KEGGi | gga:395194. |
Similar proteinsi
Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:| 100% | UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry. |
| 90% | UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence). |
| 50% | UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster. |
Entry informationi
| Entry namei | TLN1_CHICK | |
| Accessioni | P54939Primary (citable) accession number: P54939 Secondary accession number(s): Q8AWI0 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
| Last sequence update: | November 8, 2005 | |
| Last modified: | June 7, 2017 | |
| This is version 114 of the entry and version 2 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references
