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P54939

- TLN1_CHICK

UniProt

P54939 - TLN1_CHICK

Protein

Talin-1

Gene

TLN1

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (08 Nov 2005)
      Previous versions | rss
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    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

    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

    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 – 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.
    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.
    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: October 1, 2014
    This is version 97 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