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P54939

- TLN1_CHICK

UniProt

P54939 - TLN1_CHICK

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Protein

Talin-1

Gene
TLN1, TLN
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. protein binding Source: IntAct
  2. 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. cell surface Source: UniProtKB-SubCell
  3. cytosol Source: HGNC
  4. focal adhesion Source: HGNC
  5. ruffle Source: HGNC
  6. ruffle membrane Source: UniProtKB-SubCell
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.2 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 – 2055
Helixi209 – 22416
Beta strandi226 – 2283
Helixi232 – 24716
Turni252 – 2543
Turni257 – 2593
Helixi262 – 2643
Helixi268 – 2703
Helixi276 – 28510
Turni286 – 2883
Helixi291 – 30414
Turni306 – 3094
Beta strandi311 – 3177
Beta strandi320 – 3223
Beta strandi326 – 3327
Beta strandi334 – 3418
Turni342 – 3443
Beta strandi347 – 3526
Helixi353 – 3553
Beta strandi358 – 3614
Beta strandi363 – 3697
Helixi371 – 3733
Beta strandi374 – 3763
Beta strandi378 – 3814
Helixi385 – 3939
Helixi823 – 84119
Helixi855 – 87319
Turni1945 – 19473
Helixi1948 – 196619
Helixi2345 – 236117

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.

Miscellaneous databases

EvolutionaryTraceiP54939.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini86 – 403318FERMAdd
BLAST
Domaini2292 – 2531240I/LWEQAdd
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.
Contains 1 I/LWEQ domain.

Phylogenomic databases

eggNOGiNOG324465.
HOVERGENiHBG023870.
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

MVALSLKISI GNVVKTMQFE PSTMVYDACR MIRERVPEAQ MGQPNDFGLF     50
LSDEDPKKGI WLEAGKALDY YMLRNGDTME YKKKQRPLKI RMLDGTVKTV 100
MVDDSKTVTD MLTTICARIG ITNYDEYSLV REIMEEKKEE VTGTLKKDKT 150
LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL REQGIDDNET LLLRRKFFYS 200
DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG YQCQIQFGPH 250
NEQKHKPGFL ELKDFLPKEY IKQKGERKIF MAHKNCGNMS EIEAKVRYVK 300
LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE 350
WSLTNIKRWA ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL 400
KKKKSKDHFG LEGDEESTML EDSVSPKKST VLQQQFNRVG KAELGSVALP 450
AIMRTGAGGP ENFQVGTMPQ AQMQITSGQM HRGHMPPLTS AQQALTGTIN 500
SSMQAVNAAQ ATLDDFETLP PLGQDAASKA WRKNKMDESK HEIHSQADAI 550
TAGTASVVNL TAGDPADTDY TAVGCAVTTI SSNLTEMSKG VKLLAALMED 600
EGGNGRQLLQ AAKNLASAVS DLLKTAQPAS AEPRQNLLQA AGLVGQTSGE 650
LLQQIGESDT DPRFQDMLMQ LAKAVASAAA ALVLKAKNVA QKTEDSALQT 700
QVIAAATQCA LSTSQLVACT KVVAPTISSP VCQEQLIEAG KLVAKSAEGC 750
VEASKAATND DQLLKQVGVA ATAVTQALND LLQHIKQHAT GGQPIGRYDQ 800
ATDTILNVTE NIFSSMGDAG EMVRQARILA QATSDLVNAI KADAEGETDL 850
ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA 900
TNAAAQNAIK KKLVHKLEHA AKQAAASATQ TIAAAQHAAA SNKNPAAQQQ 950
LVQSCKVVAD QIPMLVQGVR GSQSQPDSPS AQLALIAASQ NFLQPGGKMV 1000
AAAKATVPTI TDQASAMQLS QCAKNLAAAL AELRTAAQKA QEACGPLEID 1050
SALGLVQSLE RDLKEAKAAA RDGKLKPLPG ETMEKCAQDL GNSTKAVTSA 1100
IAHLLGEVAQ GNENYTGIAA REVAQALRSL SQAARGVAAN SSDPQAQNAM 1150
LECASDVMDK ANNLIEEARK AVAKPGDPDS QQRLVQVAKA VSQALNRCVN 1200
CLPGQRDVDA AIRMVGEASK RLLSDSFPPS NKTFQEAQSQ LNRAAAGLNQ 1250
SANELVQASR GTPQDLAKSS GKFGQDFNEF LQAGVEMASL SPTKEDQAQV 1300
VSNLKSISMS SSKLLLAAKA LSADPTSPNL KSQLAAAARA VTDSINQLIT 1350
MCTQQAPGQK ECDNALRELE TVKELLENPT QTVNDMSYFS CLDSVMENSK 1400
VLGESMAGIS QNAKNSKLPE FGESISAASK ALCGLTEAAA QAAYLVGVSD 1450
PNSQAGQQGL VDPTQFARAN QAIQMACQNL VDPACTQSQV LSAATIVAKH 1500
TSALCNTCRL ASSRTANPVA KRQFVQPAKE VANSTANLVK TIKALDGAFN 1550
EENRERCRAA TAPLIEAVDN LTAFASNPEF ATVPAQISPE GRRAMEPIVT 1600
SAKTMLESSA GLIQTARSLA VNPKDPPQWS VLAGHSRTVS DSIKKLITNM 1650
RDKAPGQREC DEAIDVLNRC MREVDQASLA AISQQLAPRE GISQEALHNQ 1700
MITAVQEINN LIEPVASAAR AEASQLGHKV SQMAQYFEPL ILAAIGAASK 1750
TPNHQQQMNL LDQTKTLAES ALQMLYTAKE AGGNPKQAAH TQEALEEAVQ 1800
MMKEAVEDLT TTLNEAASAA GVVGGMVDSI TQAINQLDEG PMGEPEGTFV 1850
DYQTTMVKTA KAIAVTVQEM VTKSTTNPDE LGILANQLTN DYGQLAQQAK 1900
PAALTAENEE IGSHIKRRVQ ELGHGCAALV TKAGALQCSP SDAYTKKELI 1950
ESARKVSEKV SHVLAALQAG NRGTQACITA ASAVSGIIAD LDTTIMFATA 2000
GTLNRENSET FADHREGILK TAKALVEDTK VLVQNATASQ EKLAQAAQSS 2050
VSTITRLAEV VKLGAASLGS EDPETQVVLI NAVKDVAKAL GDLIGATKAA 2100
AGKAGDDPAV YQLKNSAKVM VTNVTSLLKT VKAVEDEATK GTRALEATIE 2150
HIRQELAVFS SPVPPAQVST PEDFIRMTKG ITMATAKAVA AGNSCRQEDV 2200
IATANLSRRA IADMLRACKE AAYHPEVSAD VRQRALRFGK ECADGYLELL 2250
EHVLVILQKP THELKQQLAG YSKRVASSVT ELIQAAEAMK GTEWVDPEDP 2300
TVIAENELLG AAAAIEAAAK KLEQLKPRAK PKQADESLDF EEQILEAAKS 2350
IAAATSALVK AASAAQRELV AQGKVGVIPA NAVDDGQWSQ GLISAARMVA 2400
AATNNLCEAA NAAVQGHASE EKLISSAKQV AASTAQLLVA CKVKADHDSE 2450
AMKRLQAAGN AVKRASDNLV KAAQKAAAFQ DHDETVVVKE KMVGGIAQII 2500
AAQEEMLRKE RELEEARKKL AMIRQQQYKF LPTELRDEEQ N 2541
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.
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: June 11, 2014
This is version 96 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

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