Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P54939

- TLN1_CHICK

UniProt

P54939 - TLN1_CHICK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Talin-1

Gene

TLN1

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

  1. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. cell adhesion Source: InterPro
  2. cytoskeletal anchoring at plasma membrane Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Talin-1
Gene namesi
Name:TLN1
Synonyms:TLN
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell surface By similarity. Cell junctionfocal adhesion By similarity
Note: Colocalizes with LAYN at the membrane ruffles.

GO - Cellular componenti

  1. actin cytoskeleton Source: InterPro
  2. cytosol Source: HGNC
  3. focal adhesion Source: HGNC
  4. plasma membrane Source: UniProtKB-KW
  5. ruffle Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25412541Talin-1PRO_0000219430Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi1486 – 14861O-linked (GlcNAc)1 PublicationCAR_000155
Glycosylationi1889 – 18891O-linked (GlcNAc)1 PublicationCAR_000156

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP54939.
PRIDEiP54939.

PTM databases

UniCarbKBiP54939.

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

WithEntry#Exp.IntActNotes
ITGB3P051062EBI-1035421,EBI-702847From a different organism.

Protein-protein interaction databases

DIPiDIP-35571N.
IntActiP54939. 3 interactions.
STRINGi9031.ENSGALP00000038501.

Structurei

Secondary structure

1
2541
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi201 – 2055Combined sources
Helixi209 – 22416Combined sources
Beta strandi226 – 2283Combined sources
Helixi232 – 24716Combined sources
Turni252 – 2543Combined sources
Turni257 – 2593Combined sources
Helixi262 – 2643Combined sources
Helixi268 – 2703Combined sources
Helixi276 – 28510Combined sources
Turni286 – 2883Combined sources
Helixi291 – 30414Combined sources
Turni306 – 3094Combined sources
Beta strandi311 – 3177Combined sources
Beta strandi320 – 3223Combined sources
Beta strandi326 – 3327Combined sources
Beta strandi334 – 3418Combined sources
Turni342 – 3443Combined sources
Beta strandi347 – 3526Combined sources
Helixi353 – 3553Combined sources
Beta strandi358 – 3614Combined sources
Beta strandi363 – 3697Combined sources
Helixi371 – 3733Combined sources
Beta strandi374 – 3763Combined sources
Beta strandi378 – 3814Combined sources
Helixi385 – 3939Combined sources
Helixi823 – 84119Combined sources
Helixi855 – 87319Combined sources
Turni1945 – 19473Combined sources
Helixi1948 – 196619Combined sources
Helixi2345 – 236117Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MIXX-ray1.75A196-400[»]
1MIZX-ray1.90B200-400[»]
1MK7X-ray2.20B/D209-400[»]
1MK9X-ray2.80B/D/F/H209-400[»]
1RKCX-ray2.70B1944-1969[»]
1U6HX-ray2.38B849-879[»]
1XWJX-ray2.60B1944-1969[»]
1ZVZX-ray1.80B820-844[»]
1ZW2X-ray2.10B2344-2368[»]
2H7DNMR-A309-405[»]
2H7ENMR-A309-405[»]
2HRJNMR-A189-309[»]
2K00NMR-A309-400[»]
ProteinModelPortaliP54939.
SMRiP54939. Positions 196-400, 486-889, 1837-1972, 2295-2481, 2494-2527.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54939.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 403318FERMPROSITE-ProRule annotationAdd
BLAST
Domaini2292 – 2531240I/LWEQPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni280 – 435156Interaction with LAYNAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi672 – 68110Poly-Ala
Compositional biasi1335 – 13406Poly-Ala

Sequence similaritiesi

Contains 1 FERM domain.PROSITE-ProRule annotation
Contains 1 I/LWEQ domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG324465.
HOVERGENiHBG023870.
InParanoidiP54939.
KOiK06271.
PhylomeDBiP54939.

Family and domain databases

Gene3Di1.20.1410.10. 2 hits.
1.20.1420.10. 1 hit.
1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR002558. ILWEQ_dom.
IPR002404. Insln_rcpt_S1.
IPR011993. PH_like_dom.
IPR015710. Talin-1.
IPR015224. Talin_cent.
IPR029071. Ubiquitin-rel_dom.
IPR015009. Vinculin-bd_dom.
IPR006077. Vinculin/catenin.
[Graphical view]
PANTHERiPTHR19981:SF7. PTHR19981:SF7. 1 hit.
PfamiPF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF01608. I_LWEQ. 1 hit.
PF02174. IRS. 1 hit.
PF09141. Talin_middle. 1 hit.
PF08913. VBS. 2 hits.
[Graphical view]
ProDomiPD011820. ILWEQ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00295. B41. 1 hit.
SM00307. ILWEQ. 1 hit.
[Graphical view]
SUPFAMiSSF109880. SSF109880. 1 hit.
SSF109885. SSF109885. 4 hits.
SSF47031. SSF47031. 1 hit.
SSF47220. SSF47220. 5 hits.
SSF54236. SSF54236. 1 hit.
PROSITEiPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
PS50945. I_LWEQ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P54939-1 [UniParc]FASTAAdd to Basket

« Hide

        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
Length:2,541
Mass (Da):271,842
Last modified:November 8, 2005 - v2
Checksum:i5A94C290C624699E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY150847 mRNA. Translation: AAN75275.1.
PIRiB42965.
D42965.
RefSeqiNP_989854.1. NM_204523.1.
UniGeneiGga.4319.

Genome annotation databases

GeneIDi395194.
KEGGigga:395194.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY150847 mRNA. Translation: AAN75275.1 .
PIRi B42965.
D42965.
RefSeqi NP_989854.1. NM_204523.1.
UniGenei Gga.4319.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 196-400, 486-889, 1837-1972, 2295-2481, 2494-2527.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35571N.
IntActi P54939. 3 interactions.
STRINGi 9031.ENSGALP00000038501.

PTM databases

UniCarbKBi P54939.

Proteomic databases

PaxDbi P54939.
PRIDEi P54939.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 395194.
KEGGi gga:395194.

Organism-specific databases

CTDi 7094.

Phylogenomic databases

eggNOGi NOG324465.
HOVERGENi HBG023870.
InParanoidi P54939.
KOi K06271.
PhylomeDBi P54939.

Miscellaneous databases

EvolutionaryTracei P54939.
NextBioi 20815284.
PROi P54939.

Family and domain databases

Gene3Di 1.20.1410.10. 2 hits.
1.20.1420.10. 1 hit.
1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProi IPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR019747. FERM_CS.
IPR000299. FERM_domain.
IPR018979. FERM_N.
IPR002558. ILWEQ_dom.
IPR002404. Insln_rcpt_S1.
IPR011993. PH_like_dom.
IPR015710. Talin-1.
IPR015224. Talin_cent.
IPR029071. Ubiquitin-rel_dom.
IPR015009. Vinculin-bd_dom.
IPR006077. Vinculin/catenin.
[Graphical view ]
PANTHERi PTHR19981:SF7. PTHR19981:SF7. 1 hit.
Pfami PF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF01608. I_LWEQ. 1 hit.
PF02174. IRS. 1 hit.
PF09141. Talin_middle. 1 hit.
PF08913. VBS. 2 hits.
[Graphical view ]
ProDomi PD011820. ILWEQ. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00295. B41. 1 hit.
SM00307. ILWEQ. 1 hit.
[Graphical view ]
SUPFAMi SSF109880. SSF109880. 1 hit.
SSF109885. SSF109885. 4 hits.
SSF47031. SSF47031. 1 hit.
SSF47220. SSF47220. 5 hits.
SSF54236. SSF54236. 1 hit.
PROSITEi PS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
PS50945. I_LWEQ. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Talin contains three actin-binding sites each of which is adjacent to a vinculin-binding site."
    Hemmings L., Rees D.J.G., Ohanian V., Bolton S.J., Gilmore A.P., Patel B., Priddle H., Trevithick J.E., Hynes R.O., Critchley D.R.
    J. Cell Sci. 109:2715-2726(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH F-ACTIN AND VCL.
  2. "The cytoskeletal protein talin is O-glycosylated."
    Hagmann J., Grob M., Burger M.M.
    J. Biol. Chem. 267:14424-14428(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1469-1487 AND 1882-1898, GLYCOSYLATION AT THR-1486 AND THR-1889.
    Tissue: Gizzard.
  3. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 196-400 IN COMPLEX WITH ITGB3.
  4. "Vinculin activation by talin through helical bundle conversion."
    Izard T., Evans G., Borgon R.A., Rush C.L., Bricogne G., Bois P.R.J.
    Nature 427:171-175(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1944-1969 IN COMPLEX WITH VCL.
  5. "Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles."
    Borowsky M.L., Hynes R.O.
    J. Cell Biol. 143:429-442(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LAYN.

Entry informationi

Entry nameiTLN1_CHICK
AccessioniPrimary (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: October 29, 2014
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3