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)

Target domain

317-406 (Talin head, FERM F3 subdomain)

Relief mechanism

Ligand binding, Partner binding

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

2 structures for Q71LX4

Entry ID Method Resolution Chain Position Source
3G9W X-ray 216 A A/B 198-408 PDB
AF-Q71LX4-F1 Predicted AlphaFoldDB

No variants for Q71LX4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q71LX4

No associated diseases with Q71LX4

6 regional properties for Q71LX4

Type Name Position InterPro Accession
domain Protein kinase domain 56 - 307 IPR000719
domain Kinase associated domain 1 (KA1) 704 - 753 IPR001772
active_site Serine/threonine-protein kinase, active site 174 - 186 IPR008271
domain Ubiquitin-associated domain 326 - 365 IPR015940
binding_site Protein kinase, ATP binding site 62 - 85 IPR017441
domain Serine/threonine-protein kinase MARK 1-4, catalytic domain 55 - 307 IPR049508

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cell junction, focal adhesion
  • Synapse
  • Cell membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Cytoplasm, cytoskeleton
  • Focal adhesion plaques and synapses
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.
fascia adherens A cell-cell junction that contains the transmembrane protein N-cadherin, which interacts with identical molecules from neighbouring cells to form a tight mechanical intercellular link; forms a large portion of the intercalated disc, the structure at which myofibrils terminate in cardiomyocytes.
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.
synapse The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.

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.

1 GO annotations of biological process

Name Definition
cell-cell adhesion The attachment of one cell to another cell via adhesion molecules.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P54939 TLN1 Talin-1 Gallus gallus (Chicken) SS
Q9Y490 TLN1 Talin-1 Homo sapiens (Human) EV
Q9Y4G6 TLN2 Talin-2 Homo sapiens (Human) SS
P26039 Tln1 Talin-1 Mus musculus (Mouse) EV
10 20 30 40 50 60
MVALSLKICV RHCNVVKTMQ FEPSTAVYDA CRVIRERVPE AQTGQASDYG LFLSDEDPRK
70 80 90 100 110 120
GIWLEAGRTL DYYMLRNGDI LEYKKKQRPQ KIRMLDGSVK TVMVDDSKTV GELLVTICSR
130 140 150 160 170 180
IGITNYEEYS LIQETIEEKK EEGTGTLKKD RTLLRDERKM EKLKAKLHTD DDLNWLDHSR
190 200 210 220 230 240
TFREQGVDEN ETLLLRRKFF YSDQNVDSRD PVQLNLLYVQ ARDDILNGSH PVSFEKACEF
250 260 270 280 290 300
GGFQAQIQFG PHVEHKHKPG FLDLKEFLPK EYIKQRGAEK RIFQEHKNCG EMSEIEAKVK
310 320 330 340 350 360
YVKLARSLRT YGVSFFLVKE KMKGKNKLVP RLLGITKDSV MRVDEKTKEV LQEWPLTTVK
370 380 390 400 410 420
RWAASPKSFT LDFGEYQESY YSVQTTEGEQ ISQLIAGYID IILKKKQSKD RFGLEGDEES
430 440 450 460 470 480
TMLEESVSPK KRSTILQQQF NRTGKAEHGS VALPAVMRSG SSGPETFNVG SMPSPQQQVM
490 500 510 520 530 540
VGQMHRGHMP PLTSAQQALM GTINTSMHAV QQAQDDLSEL DSLPPLGQDM ASRVWVQNKV
550 560 570 580 590 600
DESKHEIHSQ VDAITAGTAS VVNLTAGDPA DTDYTAVGCA ITTISSNLTE MSKGVKLLAA
610 620 630 640 650 660
LMDDDVGSGE DLLRAARTLA GAVSDLLKAV QPTSGEPRQT VLTAAGSIGQ ASGDLLRQIG
670 680 690 700 710 720
ENETDERFQD VLMSLAKAVA NAAAMLVLKA KNVAQVAEDT VLQNRVIAAA TQCALSTSQL
730 740 750 760 770 780
VACAKVVSPT ISSPVCQEQL IEAGKLVDRS VENCVRACQA ATSDSELLKQ VSAAASVVSQ
790 800 810 820 830 840
ALHDLLQHVR QFASRGEPIG RYDQATDTIM CVTESIFSSM GDAGEMVRQA RVLAQATSDL
850 860 870 880 890 900
VNAMRSDAEA EIDMENSKKL LAAAKLLADS TARMVEAAKG AAANPENEDQ QQRLREAAEG
910 920 930 940 950 960
LRVATNAAAQ NAIKKKIVNR LEVAAKQAAA AATQTIAASQ NAAISNKNPS AQQQLVQSCK
970 980 990 1000 1010 1020
AVADHIPQLV QGVRGSQAQA EDLSAQLALI ISSQNFLQPG SKMVSSAKAA VPTVSDQAAA
1030 1040 1050 1060 1070 1080
MQLSQCAKNL ATSLAELRTA SQKAHEACGP MEIDSALNTV QTLKNELQDA KMAAAESQLK
1090 1100 1110 1120 1130 1140
PLPGETLEKC AQDLGSTSKG VGSSMAQLLT CAAQGNEHYT GVAARETAQA LKTLAQAARG
1150 1160 1170 1180 1190 1200
VAASTNDPEA AHAMLDSARD VMEGSAMLIQ EAKQALIAPG DTESQQRLAQ VAKAVSHSLN
1210 1220 1230 1240 1250 1260
NCVNCLPGQK DVDVALKSIG EASKKLLVDS LPPSTKPFQE AQSELNQAAA DLNQSAGEVV
1270 1280 1290 1300 1310 1320
HATRGQSGEL AAASGKFSDD FDEFLDAGIE MAGQAQTKED QMQVIGNLKN ISMASSKLLL
1330 1340 1350 1360 1370 1380
AAKSLSVDPG APNAKNLLAA AARAVTESIN QLIMLCTQQA PGQKECDNAL RELETVKGML
1390 1400 1410 1420 1430 1440
ENPNEPVSDL SYFDCIESVM ENSKVLGESM AGISQNAKTG DLPAFGECVG IASKALCGLT
1450 1460 1470 1480 1490 1500
EAAAQAAYLV GISDPNSQAG HQGLVDPIQF ARANQAIQMA CQNLVDPGSS PSQVLSAATI
1510 1520 1530 1540 1550 1560
VAKHTSALCN ACRIASSKTA NPVAKRHFVQ SAKEVANSTA NLVKTIKALD GDFSEDNRNK
1570 1580 1590 1600 1610 1620
CRIATTPLIE AVENLTAFAS NPEFASIPAQ ISSEGSQAQE PILVSAKTML ESSSYLIRTA
1630 1640 1650 1660 1670 1680
RSLAINPKDP PTWSVLAGHS HTVSDSIKSL ITSIRDKAPG QRECDYSIDG INRCIRDIEQ
1690 1700 1710 1720 1730 1740
ASLAAVSQSL ATRDDISVEA LQEQLTSVVQ EIGHLIDPIA TAARGEAAQL GHKVTQLASY
1750 1760 1770 1780 1790 1800
FEPLILAAVG VASKMLDHQQ QMTVLDQTKT LAESALQMLY AAKEGGGNPK AVHTAPEPKG
1810 1820 1830 1840 1850 1860
TFVDYQTTVV KYSKAIAVTA QEMIGFQIRT RVQDLGHGCI FLVQKAGALQ VCPTDSYTKR
1870 1880 1890 1900 1910 1920
ELIECARSVT EKVSLVLSAL QAGNKGTQAC ITAATAVSGI IADLDTTIMF ATAGTLNAEN
1930 1940 1950 1960 1970 1980
GETFADHREN ILKTAKALVE DTKLLVSGAA STPDKLAQAA QSSAATITQL AEVVKLGAAS
1990 2000 2010 2020 2030 2040
LGSNDPETQV VLINAIKDVA KALSDLIGAT KGAASKPADD PSMYQLKGAA KVMVTNVTSL
2050 2060 2070 2080 2090 2100
LKTVKAVEDE ATRGTRALEA TIEYIKQELT VFQSKDIPEK TSSPEESIRM TKGITMATAK
2110 2120 2130 2140 2150 2160
AVAAGNSCRQ EDVIATANLS RKAVSDMLIA CKQASFYPDV SEEVRTRALR YGTECTLGYL
2170 2180 2190 2200 2210 2220
DLLEHVLVIL QKPTPELKHQ LAAFSKRVAG AVTELIQAAE AMKGTEWVDP EDPTVIAETE
2230 2240 2250 2260 2270 2280
LLGAAASIEA AAKKLEQLKP RAKPKQADET LDFEEQILEA AKSIAAATSA LVKSASAAQR
2290 2300 2310 2320 2330 2340
ELVAQGKVGS IPANAADDGQ WSQGLISAAR MVAAATSSLC EAANASVQGH ASEEKLISSA
2350 2360 2370
KQVAASTAQL LVACKVKADQ DSEAMKRLQA AGNAV