TLN1_CHICK
ID TLN1_CHICK Reviewed; 2541 AA.
AC P54939; Q8AWI0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Talin-1;
GN Name=TLN1; Synonyms=TLN;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH F-ACTIN AND VCL.
RX PubMed=8937989; DOI=10.1242/jcs.109.11.2715;
RA Hemmings L., Rees D.J.G., Ohanian V., Bolton S.J., Gilmore A.P., Patel B.,
RA Priddle H., Trevithick J.E., Hynes R.O., Critchley D.R.;
RT "Talin contains three actin-binding sites each of which is adjacent to a
RT vinculin-binding site.";
RL J. Cell Sci. 109:2715-2726(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1469-1487 AND 1882-1898, AND GLYCOSYLATION AT THR-1486
RP AND THR-1889.
RC TISSUE=Gizzard;
RX PubMed=1629228; DOI=10.1016/s0021-9258(19)49729-9;
RA Hagmann J., Grob M., Burger M.M.;
RT "The cytoskeletal protein talin is O-glycosylated.";
RL J. Biol. Chem. 267:14424-14428(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 196-400 IN COMPLEX WITH ITGB3.
RX PubMed=12535520; DOI=10.1016/s1097-2765(02)00823-7;
RA Garcia-Alvarez B., de Pereda J.M., Calderwood D.A., Ulmer T.S.,
RA Critchley D., Campbell I.D., Ginsberg M.H., Liddington R.C.;
RT "Structural determinants of integrin recognition by talin.";
RL Mol. Cell 11:49-58(2003).
RN [4]
RP INTERACTION WITH VCL.
RX PubMed=20610383; DOI=10.1074/jbc.m109.095455;
RA Gingras A.R., Bate N., Goult B.T., Patel B., Kopp P.M., Emsley J.,
RA Barsukov I.L., Roberts G.C., Critchley D.R.;
RT "Central region of talin has a unique fold that binds vinculin and actin.";
RL J. Biol. Chem. 285:29577-29587(2010).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1944-1969 IN COMPLEX WITH VCL.
RX PubMed=14702644; DOI=10.1038/nature02281;
RA Izard T., Evans G., Borgon R.A., Rush C.L., Bricogne G., Bois P.R.J.;
RT "Vinculin activation by talin through helical bundle conversion.";
RL Nature 427:171-175(2004).
RN [6]
RP INTERACTION WITH LAYN.
RX PubMed=9786953; DOI=10.1083/jcb.143.2.429;
RA Borowsky M.L., Hynes R.O.;
RT "Layilin, a novel talin-binding transmembrane protein homologous with C-
RT type lectins, is localized in membrane ruffles.";
RL J. Cell Biol. 143:429-442(1998).
CC -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC structures to the plasma membrane. Talin is a high molecular weight
CC cytoskeletal protein concentrated at regions of cell-substratum contact
CC and, in lymphocytes, at cell-cell contacts.
CC -!- SUBUNIT: Interacts with PIP5K1C and NRAP (By similarity). Binds with
CC high affinity to vinculin VCL and with low affinity to integrins
CC (PubMed:14702644, PubMed:12535520, PubMed:8937989, PubMed:20610383).
CC Interacts with APBB1IP; this inhibits VCL binding (By similarity).
CC Interacts with F-actin (PubMed:8937989). Interacts with LAYN
CC (PubMed:9786953). Interacts with THSD1. {ECO:0000250|UniProtKB:P26039,
CC ECO:0000250|UniProtKB:Q9Y490, ECO:0000269|PubMed:12535520,
CC ECO:0000269|PubMed:14702644, ECO:0000269|PubMed:20610383,
CC ECO:0000269|PubMed:8937989, ECO:0000269|PubMed:9786953}.
CC -!- INTERACTION:
CC P54939; P05106: ITGB3; Xeno; NbExp=2; IntAct=EBI-1035421, EBI-702847;
CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane; Peripheral
CC membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell
CC surface {ECO:0000250|UniProtKB:P26039}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:P26039}. Note=Colocalizes with LAYN at the
CC membrane ruffles.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:P26039,
CC ECO:0000250|UniProtKB:Q9Y490}.
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DR EMBL; AY150847; AAN75275.1; -; mRNA.
DR PIR; B42965; B42965.
DR PIR; D42965; D42965.
DR RefSeq; NP_989854.1; NM_204523.1.
DR PDB; 1MIX; X-ray; 1.75 A; A=196-400.
DR PDB; 1MIZ; X-ray; 1.90 A; B=200-400.
DR PDB; 1MK7; X-ray; 2.20 A; B/D=209-400.
DR PDB; 1MK9; X-ray; 2.80 A; B/D/F/H=209-400.
DR PDB; 1RKC; X-ray; 2.70 A; B=1944-1969.
DR PDB; 1U6H; X-ray; 2.38 A; B=849-879.
DR PDB; 1XWJ; X-ray; 2.60 A; B=1944-1969.
DR PDB; 1ZVZ; X-ray; 1.80 A; B=820-844.
DR PDB; 1ZW2; X-ray; 2.10 A; B=2344-2368.
DR PDB; 2H7D; NMR; -; A=309-405.
DR PDB; 2H7E; NMR; -; A=309-405.
DR PDB; 2HRJ; NMR; -; A=189-309.
DR PDB; 2K00; NMR; -; A=309-400.
DR PDBsum; 1MIX; -.
DR PDBsum; 1MIZ; -.
DR PDBsum; 1MK7; -.
DR PDBsum; 1MK9; -.
DR PDBsum; 1RKC; -.
DR PDBsum; 1U6H; -.
DR PDBsum; 1XWJ; -.
DR PDBsum; 1ZVZ; -.
DR PDBsum; 1ZW2; -.
DR PDBsum; 2H7D; -.
DR PDBsum; 2H7E; -.
DR PDBsum; 2HRJ; -.
DR PDBsum; 2K00; -.
DR AlphaFoldDB; P54939; -.
DR BMRB; P54939; -.
DR SMR; P54939; -.
DR DIP; DIP-35571N; -.
DR ELM; P54939; -.
DR IntAct; P54939; 4.
DR STRING; 9031.ENSGALP00000004013; -.
DR GlyConnect; 584; 1 O-Linked glycan (2 sites).
DR PaxDb; P54939; -.
DR PRIDE; P54939; -.
DR GeneID; 395194; -.
DR KEGG; gga:395194; -.
DR CTD; 7094; -.
DR VEuPathDB; HostDB:geneid_395194; -.
DR eggNOG; KOG4261; Eukaryota.
DR InParanoid; P54939; -.
DR OrthoDB; 9839at2759; -.
DR PhylomeDB; P54939; -.
DR EvolutionaryTrace; P54939; -.
DR PRO; PR:P54939; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:HGNC-UCL.
DR GO; GO:0005925; C:focal adhesion; IDA:HGNC-UCL.
DR GO; GO:0001726; C:ruffle; IDA:HGNC-UCL.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd12150; talin-RS; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR IDEAL; IID50213; -.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR032425; FERM_f0.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR030224; Sla2_fam.
DR InterPro; IPR037438; Talin1/2-RS.
DR InterPro; IPR015224; Talin_cent.
DR InterPro; IPR036476; Talin_cent_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR015009; Vinculin-bd_dom.
DR PANTHER; PTHR10407; PTHR10407; 1.
DR Pfam; PF16511; FERM_f0; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF01608; I_LWEQ; 1.
DR Pfam; PF09141; Talin_middle; 1.
DR Pfam; PF08913; VBS; 2.
DR SMART; SM00295; B41; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF109880; SSF109880; 1.
DR SUPFAM; SSF109885; SSF109885; 4.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF47220; SSF47220; 5.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..2541
FT /note="Talin-1"
FT /id="PRO_0000219430"
FT DOMAIN 86..403
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 2292..2531
FT /note="I/LWEQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00292"
FT REGION 280..435
FT /note="Interaction with LAYN"
FT /evidence="ECO:0000269|PubMed:9786953"
FT REGION 1358..1658
FT /note="Interaction with VCL and F-actin"
FT /evidence="ECO:0000250|UniProtKB:P26039"
FT CARBOHYD 1486
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:1629228"
FT /id="CAR_000155"
FT CARBOHYD 1889
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:1629228"
FT /id="CAR_000156"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:1MIX"
FT HELIX 209..224
FT /evidence="ECO:0007829|PDB:1MIX"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1MIZ"
FT HELIX 232..247
FT /evidence="ECO:0007829|PDB:1MIX"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:1MIX"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:2HRJ"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1MIX"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:1MIX"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:1MIX"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:1MIX"
FT HELIX 291..304
FT /evidence="ECO:0007829|PDB:1MIX"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:1MIX"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:1MIX"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:2H7D"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:1MIX"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:1MIX"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:1MIX"
FT STRAND 347..352
FT /evidence="ECO:0007829|PDB:1MIX"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:1MIX"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:1MIX"
FT STRAND 363..369
FT /evidence="ECO:0007829|PDB:1MIX"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:1MIX"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:1MIX"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:1MIX"
FT HELIX 385..393
FT /evidence="ECO:0007829|PDB:1MIX"
FT HELIX 823..841
FT /evidence="ECO:0007829|PDB:1ZVZ"
FT HELIX 855..873
FT /evidence="ECO:0007829|PDB:1U6H"
FT TURN 1945..1947
FT /evidence="ECO:0007829|PDB:1RKC"
FT HELIX 1948..1966
FT /evidence="ECO:0007829|PDB:1XWJ"
FT HELIX 2345..2361
FT /evidence="ECO:0007829|PDB:1ZW2"
SQ SEQUENCE 2541 AA; 271842 MW; 5A94C290C624699E CRC64;
MVALSLKISI GNVVKTMQFE PSTMVYDACR MIRERVPEAQ MGQPNDFGLF LSDEDPKKGI
WLEAGKALDY YMLRNGDTME YKKKQRPLKI RMLDGTVKTV MVDDSKTVTD MLTTICARIG
ITNYDEYSLV REIMEEKKEE VTGTLKKDKT LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL
REQGIDDNET LLLRRKFFYS DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG
YQCQIQFGPH NEQKHKPGFL ELKDFLPKEY IKQKGERKIF MAHKNCGNMS EIEAKVRYVK
LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE WSLTNIKRWA
ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL KKKKSKDHFG LEGDEESTML
EDSVSPKKST VLQQQFNRVG KAELGSVALP AIMRTGAGGP ENFQVGTMPQ AQMQITSGQM
HRGHMPPLTS AQQALTGTIN SSMQAVNAAQ ATLDDFETLP PLGQDAASKA WRKNKMDESK
HEIHSQADAI TAGTASVVNL TAGDPADTDY TAVGCAVTTI SSNLTEMSKG VKLLAALMED
EGGNGRQLLQ AAKNLASAVS DLLKTAQPAS AEPRQNLLQA AGLVGQTSGE LLQQIGESDT
DPRFQDMLMQ LAKAVASAAA ALVLKAKNVA QKTEDSALQT QVIAAATQCA LSTSQLVACT
KVVAPTISSP VCQEQLIEAG KLVAKSAEGC VEASKAATND DQLLKQVGVA ATAVTQALND
LLQHIKQHAT GGQPIGRYDQ ATDTILNVTE NIFSSMGDAG EMVRQARILA QATSDLVNAI
KADAEGETDL ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA
TNAAAQNAIK KKLVHKLEHA AKQAAASATQ TIAAAQHAAA SNKNPAAQQQ LVQSCKVVAD
QIPMLVQGVR GSQSQPDSPS AQLALIAASQ NFLQPGGKMV AAAKATVPTI TDQASAMQLS
QCAKNLAAAL AELRTAAQKA QEACGPLEID SALGLVQSLE RDLKEAKAAA RDGKLKPLPG
ETMEKCAQDL GNSTKAVTSA IAHLLGEVAQ GNENYTGIAA REVAQALRSL SQAARGVAAN
SSDPQAQNAM LECASDVMDK ANNLIEEARK AVAKPGDPDS QQRLVQVAKA VSQALNRCVN
CLPGQRDVDA AIRMVGEASK RLLSDSFPPS NKTFQEAQSQ LNRAAAGLNQ SANELVQASR
GTPQDLAKSS GKFGQDFNEF LQAGVEMASL SPTKEDQAQV VSNLKSISMS SSKLLLAAKA
LSADPTSPNL KSQLAAAARA VTDSINQLIT MCTQQAPGQK ECDNALRELE TVKELLENPT
QTVNDMSYFS CLDSVMENSK VLGESMAGIS QNAKNSKLPE FGESISAASK ALCGLTEAAA
QAAYLVGVSD PNSQAGQQGL VDPTQFARAN QAIQMACQNL VDPACTQSQV LSAATIVAKH
TSALCNTCRL ASSRTANPVA KRQFVQPAKE VANSTANLVK TIKALDGAFN EENRERCRAA
TAPLIEAVDN LTAFASNPEF ATVPAQISPE GRRAMEPIVT SAKTMLESSA GLIQTARSLA
VNPKDPPQWS VLAGHSRTVS DSIKKLITNM RDKAPGQREC DEAIDVLNRC MREVDQASLA
AISQQLAPRE GISQEALHNQ MITAVQEINN LIEPVASAAR AEASQLGHKV SQMAQYFEPL
ILAAIGAASK TPNHQQQMNL LDQTKTLAES ALQMLYTAKE AGGNPKQAAH TQEALEEAVQ
MMKEAVEDLT TTLNEAASAA GVVGGMVDSI TQAINQLDEG PMGEPEGTFV DYQTTMVKTA
KAIAVTVQEM VTKSTTNPDE LGILANQLTN DYGQLAQQAK PAALTAENEE IGSHIKRRVQ
ELGHGCAALV TKAGALQCSP SDAYTKKELI ESARKVSEKV SHVLAALQAG NRGTQACITA
ASAVSGIIAD LDTTIMFATA GTLNRENSET FADHREGILK TAKALVEDTK VLVQNATASQ
EKLAQAAQSS VSTITRLAEV VKLGAASLGS EDPETQVVLI NAVKDVAKAL GDLIGATKAA
AGKAGDDPAV YQLKNSAKVM VTNVTSLLKT VKAVEDEATK GTRALEATIE HIRQELAVFS
SPVPPAQVST PEDFIRMTKG ITMATAKAVA AGNSCRQEDV IATANLSRRA IADMLRACKE
AAYHPEVSAD VRQRALRFGK ECADGYLELL EHVLVILQKP THELKQQLAG YSKRVASSVT
ELIQAAEAMK GTEWVDPEDP TVIAENELLG AAAAIEAAAK KLEQLKPRAK PKQADESLDF
EEQILEAAKS IAAATSALVK AASAAQRELV AQGKVGVIPA NAVDDGQWSQ GLISAARMVA
AATNNLCEAA NAAVQGHASE EKLISSAKQV AASTAQLLVA CKVKADHDSE AMKRLQAAGN
AVKRASDNLV KAAQKAAAFQ DHDETVVVKE KMVGGIAQII AAQEEMLRKE RELEEARKKL
AMIRQQQYKF LPTELRDEEQ N
