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P54939 (TLN1_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Talin-1
Gene names
Name:TLN1
Synonyms:TLN
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length2541 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.1 Ref.5

Subcellular location

Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton. Note: Colocalizes with LAYN at the membrane ruffles.

Post-translational modification

Phosphorylated By similarity.

Sequence similarities

Contains 1 FERM domain.

Contains 1 I/LWEQ domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ITGB3P051062EBI-1035421,EBI-702847From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25412541Talin-1
PRO_0000219430

Regions

Domain86 – 403318FERM
Domain2292 – 2531240I/LWEQ
Region280 – 435156Interaction with LAYN
Compositional bias672 – 68110Poly-Ala
Compositional bias1335 – 13406Poly-Ala

Amino acid modifications

Glycosylation14861O-linked (GlcNAc) Ref.2
CAR_000155
Glycosylation18891O-linked (GlcNAc) Ref.2
CAR_000156

Secondary structure

1 ...................................................... 2541
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54939 [UniParc].

Last modified November 8, 2005. Version 2.
Checksum: 5A94C290C624699E

FASTA2,541271,842
        10         20         30         40         50         60 
MVALSLKISI GNVVKTMQFE PSTMVYDACR MIRERVPEAQ MGQPNDFGLF LSDEDPKKGI 

        70         80         90        100        110        120 
WLEAGKALDY YMLRNGDTME YKKKQRPLKI RMLDGTVKTV MVDDSKTVTD MLTTICARIG 

       130        140        150        160        170        180 
ITNYDEYSLV REIMEEKKEE VTGTLKKDKT LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL 

       190        200        210        220        230        240 
REQGIDDNET LLLRRKFFYS DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG 

       250        260        270        280        290        300 
YQCQIQFGPH NEQKHKPGFL ELKDFLPKEY IKQKGERKIF MAHKNCGNMS EIEAKVRYVK 

       310        320        330        340        350        360 
LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE WSLTNIKRWA 

       370        380        390        400        410        420 
ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL KKKKSKDHFG LEGDEESTML 

       430        440        450        460        470        480 
EDSVSPKKST VLQQQFNRVG KAELGSVALP AIMRTGAGGP ENFQVGTMPQ AQMQITSGQM 

       490        500        510        520        530        540 
HRGHMPPLTS AQQALTGTIN SSMQAVNAAQ ATLDDFETLP PLGQDAASKA WRKNKMDESK 

       550        560        570        580        590        600 
HEIHSQADAI TAGTASVVNL TAGDPADTDY TAVGCAVTTI SSNLTEMSKG VKLLAALMED 

       610        620        630        640        650        660 
EGGNGRQLLQ AAKNLASAVS DLLKTAQPAS AEPRQNLLQA AGLVGQTSGE LLQQIGESDT 

       670        680        690        700        710        720 
DPRFQDMLMQ LAKAVASAAA ALVLKAKNVA QKTEDSALQT QVIAAATQCA LSTSQLVACT 

       730        740        750        760        770        780 
KVVAPTISSP VCQEQLIEAG KLVAKSAEGC VEASKAATND DQLLKQVGVA ATAVTQALND 

       790        800        810        820        830        840 
LLQHIKQHAT GGQPIGRYDQ ATDTILNVTE NIFSSMGDAG EMVRQARILA QATSDLVNAI 

       850        860        870        880        890        900 
KADAEGETDL ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA 

       910        920        930        940        950        960 
TNAAAQNAIK KKLVHKLEHA AKQAAASATQ TIAAAQHAAA SNKNPAAQQQ LVQSCKVVAD 

       970        980        990       1000       1010       1020 
QIPMLVQGVR GSQSQPDSPS AQLALIAASQ NFLQPGGKMV AAAKATVPTI TDQASAMQLS 

      1030       1040       1050       1060       1070       1080 
QCAKNLAAAL AELRTAAQKA QEACGPLEID SALGLVQSLE RDLKEAKAAA RDGKLKPLPG 

      1090       1100       1110       1120       1130       1140 
ETMEKCAQDL GNSTKAVTSA IAHLLGEVAQ GNENYTGIAA REVAQALRSL SQAARGVAAN 

      1150       1160       1170       1180       1190       1200 
SSDPQAQNAM LECASDVMDK ANNLIEEARK AVAKPGDPDS QQRLVQVAKA VSQALNRCVN 

      1210       1220       1230       1240       1250       1260 
CLPGQRDVDA AIRMVGEASK RLLSDSFPPS NKTFQEAQSQ LNRAAAGLNQ SANELVQASR 

      1270       1280       1290       1300       1310       1320 
GTPQDLAKSS GKFGQDFNEF LQAGVEMASL SPTKEDQAQV VSNLKSISMS SSKLLLAAKA 

      1330       1340       1350       1360       1370       1380 
LSADPTSPNL KSQLAAAARA VTDSINQLIT MCTQQAPGQK ECDNALRELE TVKELLENPT 

      1390       1400       1410       1420       1430       1440 
QTVNDMSYFS CLDSVMENSK VLGESMAGIS QNAKNSKLPE FGESISAASK ALCGLTEAAA 

      1450       1460       1470       1480       1490       1500 
QAAYLVGVSD PNSQAGQQGL VDPTQFARAN QAIQMACQNL VDPACTQSQV LSAATIVAKH 

      1510       1520       1530       1540       1550       1560 
TSALCNTCRL ASSRTANPVA KRQFVQPAKE VANSTANLVK TIKALDGAFN EENRERCRAA 

      1570       1580       1590       1600       1610       1620 
TAPLIEAVDN LTAFASNPEF ATVPAQISPE GRRAMEPIVT SAKTMLESSA GLIQTARSLA 

      1630       1640       1650       1660       1670       1680 
VNPKDPPQWS VLAGHSRTVS DSIKKLITNM RDKAPGQREC DEAIDVLNRC MREVDQASLA 

      1690       1700       1710       1720       1730       1740 
AISQQLAPRE GISQEALHNQ MITAVQEINN LIEPVASAAR AEASQLGHKV SQMAQYFEPL 

      1750       1760       1770       1780       1790       1800 
ILAAIGAASK TPNHQQQMNL LDQTKTLAES ALQMLYTAKE AGGNPKQAAH TQEALEEAVQ 

      1810       1820       1830       1840       1850       1860 
MMKEAVEDLT TTLNEAASAA GVVGGMVDSI TQAINQLDEG PMGEPEGTFV DYQTTMVKTA 

      1870       1880       1890       1900       1910       1920 
KAIAVTVQEM VTKSTTNPDE LGILANQLTN DYGQLAQQAK PAALTAENEE IGSHIKRRVQ 

      1930       1940       1950       1960       1970       1980 
ELGHGCAALV TKAGALQCSP SDAYTKKELI ESARKVSEKV SHVLAALQAG NRGTQACITA 

      1990       2000       2010       2020       2030       2040 
ASAVSGIIAD LDTTIMFATA GTLNRENSET FADHREGILK TAKALVEDTK VLVQNATASQ 

      2050       2060       2070       2080       2090       2100 
EKLAQAAQSS VSTITRLAEV VKLGAASLGS EDPETQVVLI NAVKDVAKAL GDLIGATKAA 

      2110       2120       2130       2140       2150       2160 
AGKAGDDPAV YQLKNSAKVM VTNVTSLLKT VKAVEDEATK GTRALEATIE HIRQELAVFS 

      2170       2180       2190       2200       2210       2220 
SPVPPAQVST PEDFIRMTKG ITMATAKAVA AGNSCRQEDV IATANLSRRA IADMLRACKE 

      2230       2240       2250       2260       2270       2280 
AAYHPEVSAD VRQRALRFGK ECADGYLELL EHVLVILQKP THELKQQLAG YSKRVASSVT 

      2290       2300       2310       2320       2330       2340 
ELIQAAEAMK GTEWVDPEDP TVIAENELLG AAAAIEAAAK KLEQLKPRAK PKQADESLDF 

      2350       2360       2370       2380       2390       2400 
EEQILEAAKS IAAATSALVK AASAAQRELV AQGKVGVIPA NAVDDGQWSQ GLISAARMVA 

      2410       2420       2430       2440       2450       2460 
AATNNLCEAA NAAVQGHASE EKLISSAKQV AASTAQLLVA CKVKADHDSE AMKRLQAAGN 

      2470       2480       2490       2500       2510       2520 
AVKRASDNLV KAAQKAAAFQ DHDETVVVKE KMVGGIAQII AAQEEMLRKE RELEEARKKL 

      2530       2540 
AMIRQQQYKF LPTELRDEEQ N

« Hide

References

[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]"Structural determinants of integrin recognition by talin."
Garcia-Alvarez B., de Pereda J.M., Calderwood D.A., Ulmer T.S., Critchley D., Campbell I.D., Ginsberg M.H., Liddington R.C.
Mol. Cell 11:49-58(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY150847 mRNA. Translation: AAN75275.1.
IPIIPI00586709.
PIRB42965.
D42965.
RefSeqNP_989854.1. NM_204523.1.
UniGeneGga.4319.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP54939.
SMRP54939. Positions 196-400, 486-889, 1837-1972, 2295-2481, 2494-2527.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-35571N.
IntActP54939. 2 interactions.
STRING9031.ENSGALP00000038501.

PTM databases

GlycoSuiteDBP54939.

Proteomic databases

PaxDbP54939.
PRIDEP54939.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID395194.
KEGGgga:395194.

Organism-specific databases

CTD7094.

Phylogenomic databases

eggNOGNOG324465.
HOVERGENHBG023870.
KOK06271.

Family and domain databases

Gene3D1.20.1420.10. 1 hit.
1.20.80.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR019749. 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.
IPR015009. Vinculin-bd_dom.
IPR006077. Vinculin/catenin.
[Graphical view]
PANTHERPTHR19981:SF7. PTHR19981:SF7. 1 hit.
PfamPF00373. FERM_M. 1 hit.
PF09379. FERM_N. 1 hit.
PF01608. I_LWEQ. 2 hits.
PF02174. IRS. 1 hit.
PF09141. Talin_middle. 1 hit.
PF08913. VBS. 2 hits.
[Graphical view]
ProDomPD011820. ILWEQ. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00295. B41. 1 hit.
SM00307. ILWEQ. 1 hit.
[Graphical view]
SUPFAMSSF47031. FERM_3-hlx. 1 hit.
SSF109880. Talin_cent. 1 hit.
SSF47220. Vinculin/catenin. 6 hits.
PROSITEPS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
PS50945. I_LWEQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP54939.
NextBio20815284.

Entry information

Entry nameTLN1_CHICK
AccessionPrimary (citable) accession number: P54939
Secondary accession number(s): Q8AWI0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 8, 2005
Last modified: May 1, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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