P26039 (TLN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Talin-1

Gene names

Name:	Tln1
Synonyms:	Tln

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	2541 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts.
Subunit structure	Binds with high affinity to VCL and with low affinity to integrins. Interacts with NRAP and LAYN. Interacts with SYNM By similarity. Interacts with PTK2/FAK1. Interacts with PIP5K1C. Ref.4
Subcellular location	Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasm › cytoskeleton By similarity. Note: Colocalizes with LAYN at the membrane ruffles By similarity.
Sequence similarities	Contains 1 FERM domain. Contains 1 I/LWEQ domain.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: InterPro cell-substrate junction assembly Inferred from mutant phenotype. Source: MGI cortical actin cytoskeleton organization Inferred from mutant phenotype. Source: MGI cytoskeletal anchoring at plasma membrane Inferred from electronic annotation. Source: InterPro
Cellular component	actin cytoskeleton Inferred from electronic annotation. Source: InterPro focal adhesion Inferred from direct assay. Source: MGI ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Inferred from electronic annotation. Source: InterPro insulin receptor binding Inferred from electronic annotation. Source: InterPro structural constituent of cytoskeleton Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ITGB3	P05106	3	EBI-1039593,EBI-702847	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2541

2541

Talin-1

PRO_0000219429

Regions

Domain

86 – 403

318

FERM

Domain

2293 – 2533

241

I/LWEQ

Region

280 – 435

156

Interaction with LAYN By similarity

Region

1327 – 1948

622

Interaction with SYNM By similarity

Amino acid modifications

Modified residue

26

1

Phosphotyrosine By similarity

Modified residue

70

1

Phosphotyrosine By similarity

Modified residue

167

1

Phosphothreonine By similarity

Modified residue

425

1

Phosphoserine By similarity

Modified residue

436

1

Phosphotyrosine By similarity

Modified residue

1116

1

Phosphotyrosine Ref.6

Modified residue

1945

1

Phosphotyrosine By similarity

Modified residue

2031

1

N6-acetyllysine By similarity

Modified residue

2040

1

Phosphoserine Ref.5 Ref.7

Modified residue

2115

1

N6-acetyllysine By similarity

Modified residue

2273

1

Phosphoserine Ref.8

Modified residue

2338

1

Phosphoserine By similarity

Modified residue

2530

1

Phosphotyrosine By similarity

Natural variations

Natural variant

1105

1

L → P.

Natural variant

2180

1

K → M.

Experimental info

Sequence conflict

673

1

K → N in CAA39588. Ref.1

Sequence conflict

1227

1

S → L in CAA39588. Ref.1

Secondary structure

1

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2541

Helix Strand Turn

Details...

Helix

210 – 224

15

Beta strand

226 – 228

3

Helix

232 – 247

16

Turn

252 – 254

3

Helix

262 – 264

3

Helix

268 – 273

6

Helix

276 – 284

9

Turn

285 – 288

4

Helix

291 – 303

13

Turn

306 – 309

4

Beta strand

311 – 317

7

Beta strand

326 – 332

7

Beta strand

334 – 340

7

Turn

342 – 344

3

Beta strand

347 – 352

6

Helix

353 – 355

3

Beta strand

358 – 362

5

Beta strand

365 – 369

5

Beta strand

371 – 376

6

Beta strand

378 – 381

4

Helix

385 – 399

15

Helix

493 – 512

20

Helix

526 – 560

35

Beta strand

565 – 567

3

Helix

570 – 600

31

Helix

606 – 626

21

Helix

634 – 652

19

Helix

664 – 690

27

Beta strand

696 – 699

4

Helix

700 – 723

24

Turn

724 – 726

3

Helix

730 – 756

27

Helix

762 – 780

19

Helix

1631 – 1649

19

Helix

1847 – 1874

28

Turn

1875 – 1877

3

Helix

1882 – 1904

23

Helix

1910 – 1939

30

Helix

1944 – 1968

25

Helix

1969 – 1971

3

Helix

2301 – 2324

24

Beta strand

2332 – 2334

3

Helix

2341 – 2373

33

Helix

2380 – 2382

3

Helix

2383 – 2416

34

Helix

2421 – 2442

22

Turn

2443 – 2445

3

Helix

2451 – 2476

26

Helix

2497 – 2528

32

Sequences

	Sequence		Length	Mass (Da)
	P26039 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 78832388E2392B8E	FASTA	2,541	269,821
	10 20 30 40 50 60 MVALSLKISI GNVVKTMQFE PSTMVYDACR MIRERIPEAL AGPPNDFGLF LSDDDPKKGI 70 80 90 100 110 120 WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI MVDDSKTVTD MLMTICARIG 130 140 150 160 170 180 ITNHDEYSLV RELMEEKKDE GTGTLRKDKT LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL 190 200 210 220 230 240 REQGVEEHET LLLRRKFFYS DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG 250 260 270 280 290 300 FQCQIQFGPH NEQKHKAGFL DLKDFLPKEY VKQKGERKIF QAHKNCGQMS 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 VLQQQYNRVG KVEHGSVALP AIMRSGASGP ENFQVGSMPP AQQQITSGQM 490 500 510 520 530 540 HRGHMPPLTS AQQALTGTIN SSMQAVQAAQ ATLDDFETLP PLGQDAASKA WRKNKMDESK 550 560 570 580 590 600 HEIHSQVDAI TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED 610 620 630 640 650 660 EGGNGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE LLQQIGESDT 670 680 690 700 710 720 DPHFQDVLMQ LAKAVASAAA ALVLKAKSVA QRTEDSGLQT QVIAAATQCA LSTSQLVACT 730 740 750 760 770 780 KVVAPTISSP VCQEQLVEAG RLVAKAVEGC VSASQAATED GQLLRGVGAA ATAVTQALNE 790 800 810 820 830 840 LLQHVKAHAT GAGPAGRYDQ ATDTILTVTE NIFSSMGDAG EMVRQARILA QATSDLVNAI 850 860 870 880 890 900 KADAEGESDL ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA 910 920 930 940 950 960 TNAAAQNAIK KKLVQRLEHA AKQAAASATQ TIAAAQHAAS APKASAGPQP LLVQSCKAVA 970 980 990 1000 1010 1020 EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM VAAAKASVPT IQDQASAMQL 1030 1040 1050 1060 1070 1080 SQCAKNLGTA LAELRTAAQK AQEACGPLEM DSALSVVQNL EKDLQEIKAA ARDGKLKPLP 1090 1100 1110 1120 1130 1140 GETMEKCTQD LGNSTKAVSS AIAKLLGEIA QGNENYAGIA ARDVAGGLRS LAQAARGVAA 1150 1160 1170 1180 1190 1200 LTSDPAVQAI VLDTASDVLD KASSLIEEAK KASGHPGDPE SQQRLAQVAK AVTQALNRCV 1210 1220 1230 1240 1250 1260 SCLPGQRDVD NALRAVGDAS KRLLSDSLPP STGTFQEAQS RLNEAAAGLN QAATELVQAS 1270 1280 1290 1300 1310 1320 RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ VVSNLKGISM SSSKLLLAAK 1330 1340 1350 1360 1370 1380 ALSTDPASPN LKSQLAAAAR AVTDSINQLI TMCTQQAPGQ KECDNALRQL ETVRELLENP 1390 1400 1410 1420 1430 1440 VQPINDMSYF GCLDSVMENS KVLGEAMTGI SQNAKNGNLP EFGDAIATAS KALCGFTEAA 1450 1460 1470 1480 1490 1500 AQAAYLVGVS DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK 1510 1520 1530 1540 1550 1560 HTSALCNSCR LASARTANPT AKRQFVQSAK EVANSTANLV KTIKALDGDF TEENRAQCRA 1570 1580 1590 1600 1610 1620 ATAPLLEAVD NLSAFASNPE FSSVPAQISP EGRAAMEPIV ISAKTMLESA GGLIQTARAL 1630 1640 1650 1660 1670 1680 AVNPRDPPRW SVLAGHSRTV SDSIKKLITS MRDKAPGQLE CETAIAALNS CLRDLDQASL 1690 1700 1710 1720 1730 1740 AAVSQQLAPR EGISQEALHT QMLTAVQEIS HLIEPLASAA RAEASQLGHK VSQMAQYFEP 1750 1760 1770 1780 1790 1800 LTLAAVGAAS KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV 1810 1820 1830 1840 1850 1860 QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGDPEGSF VDYQTTMVRT 1870 1880 1890 1900 1910 1920 AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASQA KPAAVAAENE EIGAHIKHRV 1930 1940 1950 1960 1970 1980 QELGHGCSAL VTKAGALQCS PSDVYTKKEL IECARRVSEK VSHVLAALQA GNRGTQACIT 1990 2000 2010 2020 2030 2040 AASAVSGIIA DLDTTIMFAT AGTLNREGAE TFADHREGIL KTAKVLVEDT KVLVQNAAGS 2050 2060 2070 2080 2090 2100 QEKLAQAAQS SVATITRLAD VVKLGAASLG AEDPETQVVL INAVKDVAKA LGDLISATKA 2110 2120 2130 2140 2150 2160 AAGKVGDDPA VWQLKNSAKV MVTNVTSLLK TVKAVEDEAT KGTRALEATT EHIRQELAVF 2170 2180 2190 2200 2210 2220 CSPEPPAKTS TPEDFIRMTK GITMATAKAV AAGNSCRQED VIATANLSRR AIADMLRACK 2230 2240 2250 2260 2270 2280 EAAFHPEVAP DVRLRALHYG RECANGYLEL LDHVLLTLQK PNPDLKQQLT GHSKRVAGSV 2290 2300 2310 2320 2330 2340 TELIQAAEAM KGTEWVDPED PTVIAENELL GAAAAIEAAA KKLEQLKPRA KPKEADESLN 2350 2360 2370 2380 2390 2400 FEEQILEAAK SIAAATSALV KAASAAQREL VAQGKVGAIP ANALDDGQWS QGLISAARMV 2410 2420 2430 2440 2450 2460 AAATNNLCEA ANAAVQGHAS QEKLISSAKQ VAASTAQLLV ACKVKADQDS EAMKRLQAAG 2470 2480 2490 2500 2510 2520 NAVKRASDNL VKAAQKAAAF EDQENETVVV KEKMVGGIAQ IIAAQEEMLR KERELEEARK 2530 2540 KLAQIRQQQY KFLPSELRDE H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and domain structure of talin." Rees D.J.G., Ades S.A., Singer S.J., Hynes R.O. Nature 347:685-689(1990) [PubMed: 2120593] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Fibroblast.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary gland.
[4]	"Interaction of focal adhesion kinase with cytoskeletal protein talin." Chen H.C., Appeddu P.A., Parsons J.T., Hildebrand J.D., Schaller M.D., Guan J.L. J. Biol. Chem. 270:16995-16999(1995) [PubMed: 7622520] [Abstract] Cited for: INTERACTION WITH PTK2/FAK1.
[5]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed: 18630941] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1116, MASS SPECTROMETRY. Tissue: Brain.
[7]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, MASS SPECTROMETRY. Tissue: Liver.
[8]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed: 19144319] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2273, MASS SPECTROMETRY. Tissue: Macrophage.
[9]	"Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle." Papagrigoriou E., Gingras A.R., Barsukov I.L., Bate N., Fillingham I.J., Patel B., Frank R., Ziegler W.H., Roberts G.C.K., Critchley D.R., Emsley J. EMBO J. 23:2942-2951(2004) [PubMed: 15272303] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 482-789 IN COMPLEX WITH VCL.
[10]	"Structural basis for phosphatidylinositol phosphate kinase type Igamma binding to talin at focal adhesions." de Pereda J.M., Wegener K.L., Santelli E., Bate N., Ginsberg M.H., Critchley D.R., Campbell I.D., Liddington R.C. J. Biol. Chem. 280:8381-8386(2005) [PubMed: 15623515] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 209-410 IN COMPLEX WITH PIP5K1C.
[11]	"A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head." Fillingham I., Gingras A.R., Papagrigoriou E., Patel B., Emsley J., Critchley D.R., Roberts G.C.K., Barsukov I.L. Structure 13:65-74(2005) [PubMed: 15642262] [Abstract] Cited for: STRUCTURE BY NMR OF 755-889.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X56123 mRNA. Translation: CAA39588.1.
AL732506 Genomic DNA. Translation: CAM17190.1.
BC018557 mRNA. Translation: AAH18557.1.
BC150810 mRNA. Translation: AAI50811.1.

IPI

IPI00465786.

PIR

S11661.

RefSeq

NP_035732.2. NM_011602.5.

UniGene

Mm.208601.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SJ7	X-ray	2.50	A/B/C	482-655	[»]
1SJ8	X-ray	2.60	A	482-789	[»]
1T01	X-ray	2.06	B	605-628	[»]
1U89	NMR	-	A	755-889	[»]
1XWX	model	-	A	486-889	[»]
1Y19	X-ray	2.60	B/D/F/H/J/L	209-410	[»]
1ZW3	X-ray	3.30	B	1628-1652	[»]
2B0H	NMR	-	A	1843-1973	[»]
2G35	NMR	-	A	305-404	[»]
2JSW	NMR	-	A	2300-2482	[»]
2KBB	NMR	-	A	1655-1822	[»]
2KC1	NMR	-	A	1-85	[»]
2KC2	NMR	-	A	86-202	[»]
2KGX	NMR	-	A	1655-1822	[»]
			B	311-401	[»]
2KMA	NMR	-	A	1-202	[»]
2KVP	NMR	-	A	1815-1973	[»]
2L10	NMR	-	A	1206-1357	[»]
2QDQ	X-ray	2.20	A/B	2494-2541	[»]
2X0C	X-ray	2.00	A	1359-1659	[»]
3DYJ	X-ray	1.85	A/B	1974-2293	[»]
3IVF	X-ray	1.94	A	1-400	[»]
3S90	X-ray	1.97	C/D	1512-1546	[»]

ProteinModelPortal

P26039.

SMR

P26039. Positions 1-400, 485-889, 1206-1357, 1359-1973, 1975-2291, 2296-2482, 2496-2529.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-647N.

IntAct

P26039. 4 interactions.

MINT

MINT-258500.

STRING

P26039.

PTM databases

PhosphoSite

P26039.

Proteomic databases

PRIDE

P26039.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000030187; ENSMUSP00000030187; ENSMUSG00000028465.

GeneID

21894.

KEGG

mmu:21894.

Organism-specific databases

CTD

7094.

MGI

MGI:1099832. Tln1.

Phylogenomic databases

HOVERGEN

HBG023870.

InParanoid

P26039.

OrthoDB

EOG48PMJ8.

Gene expression databases

ArrayExpress

P26039.

Bgee

P26039.

CleanEx

MM_TLN1.

Genevestigator

P26039.

Family and domain databases

InterPro

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.
IPR002404. Insln_rcpt_S1.
IPR011993. PH_type.
IPR015711. Talin.
IPR015710. Talin-rel.
IPR015224. Talin_cent.
IPR015009. Vinculin-bd_dom.
IPR006077. Vinculin/catenin.
[Graphical view]

Gene3D

G3DSA:1.20.80.10. ACBP. 1 hit.
G3DSA:2.30.29.30. PH_type. 1 hit.
G3DSA:1.20.1420.10. Talin_cent. 1 hit.

KO

K06271.

PANTHER

PTHR19981:SF3. PTHR19981:SF3. 1 hit.
PTHR19981. Talin. 1 hit.

Pfam

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]

ProDom

PD011820. ILWEQ. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00295. B41. 1 hit.
SM00307. ILWEQ. 1 hit.
[Graphical view]

SUPFAM

SSF47031. FERM_3-hlx. 1 hit.
SSF109880. Talin_cent. 1 hit.
SSF47220. Vinculin/catenin. 5 hits.

PROSITE

PS00660. FERM_1. 1 hit.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. 1 hit.
PS50945. I_LWEQ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

301428.

SOURCE

Search...

Entry information

Entry name

TLN1_MOUSE

Accession

Primary (citable) accession number: P26039
Secondary accession number(s): A2AIM8, Q8VEF0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	July 27, 2011
Last modified:	January 25, 2012
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program