P54939

SS
Gene name
TLN1 (TLN)
Protein name
Talin-1
Names
Species
Gallus gallus (Chicken)
KEGG Pathway
gga:395194
EC number
Protein Class

Descriptions

Talin-1, a FERM domain-containing protein, forms a direct link with integrin adhesion receptors and the actin cytoskeleton and plays an important role in regulating integrin-mediated signaling. Talin function is autoinhibited by intramolecular interactions between the integrin-binding F3 domain within the FERM domain and autoinhibitory domain (R9) within the C-terminal rod domain (Talin rod). Both the small GTPase Rap1 and PIP2 activate talin and promote integrin-mediated cell adhesion.

Autoinhibitory domains (AIDs)

1654-1821 (R9 fragment of talin rod) SS

Target domain

314-403 (Talin head, FERM F3 subdomain)

Relief mechanism

Ligand binding, Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

14 structures for P54939

Entry ID Method Resolution Chain Position Source
1MIX X-ray 175 A A 196-400 PDB
1MIZ X-ray 190 A B 200-400 PDB
1MK7 X-ray 220 A B/D 209-400 PDB
1MK9 X-ray 280 A B/D/F/H 209-400 PDB
1RKC X-ray 270 A B 1944-1969 PDB
1U6H X-ray 238 A B 849-879 PDB
1XWJ X-ray 260 A B 1944-1969 PDB
1ZVZ X-ray 180 A B 820-844 PDB
1ZW2 X-ray 210 A B 2344-2368 PDB
2H7D NMR - A 309-405 PDB
2H7E NMR - A 309-405 PDB
2HRJ NMR - A 189-309 PDB
2K00 NMR - A 309-400 PDB
AF-P54939-F1 Predicted AlphaFoldDB

No variants for P54939

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P54939

No associated diseases with P54939

18 regional properties for P54939

Type Name Position InterPro Accession
domain FERM domain 86 - 403 IPR000299
domain IRS-type PTB domain 313 - 400 IPR002404
domain I/LWEQ domain 2292 - 2531 IPR002558
domain Vinculin-binding site-containing domain 1848 - 1972 IPR015009
domain Talin, central 491 - 652 IPR015224
domain FERM, N-terminal 90 - 130 IPR018979
conserved_site FERM conserved site 173 - 201 IPR019747-1
conserved_site FERM conserved site 283 - 312 IPR019747-2
domain FERM central domain 203 - 313 IPR019748
domain Band 4.1 domain 82 - 313 IPR019749
domain Talin, N-terminal F0 domain 4 - 83 IPR032425
domain Talin-1/2, rod-segment 1653 - 1825 IPR037438
domain Talin, R4 domain 916 - 1040 IPR049108
domain Talin 1-like, rod-segment domain 1209 - 1353 IPR054060-1
domain Talin 1-like, rod-segment domain 1656 - 1821 IPR054060-2
domain Talin 1-like, rod-segment domain 1974 - 2138 IPR054060-3
domain Talin, IBS2B domain 1045 - 1205 IPR054082-1
domain Talin, IBS2B domain 2141 - 2289 IPR054082-2

Functions

Description
EC Number
Subcellular Localization
  • Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side
  • Cytoplasm, cytoskeleton
  • Cell surface
  • Cell junction, focal adhesion
  • Colocalizes with LAYN at the membrane ruffles
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
cell surface The external part of the cell wall and/or plasma membrane.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
focal adhesion A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ).
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
ruffle Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork.
ruffle membrane The portion of the plasma membrane surrounding a ruffle.

3 GO annotations of molecular function

Name Definition
actin filament binding Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
integrin binding Binding to an integrin.
structural constituent of cytoskeleton The action of a molecule that contributes to the structural integrity of a cytoskeletal structure.

2 GO annotations of biological process

Name Definition
cell-cell adhesion The attachment of one cell to another cell via adhesion molecules.
platelet aggregation The adhesion of one platelet to one or more other platelets via adhesion molecules.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9Y4G6 TLN2 Talin-2 Homo sapiens (Human) SS
Q9Y490 TLN1 Talin-1 Homo sapiens (Human) EV
Q71LX4 Tln2 Talin-2 Mus musculus (Mouse) SS
P26039 Tln1 Talin-1 Mus musculus (Mouse) EV
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