ID   TLN_OSCPE               Reviewed;        2531 AA.
AC   A0A3G2LGI8;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Talin {ECO:0000303|PubMed:29880641};
GN   Name=TLN {ECO:0000305};
OS   Oscarella pearsei (Sponge).
OC   Eukaryota; Metazoa; Porifera; Homoscleromorpha; Homosclerophorida;
OC   Oscarellidae; Oscarella.
OX   NCBI_TaxID=1940113;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH VIN1.
RX   PubMed=29880641; DOI=10.1074/jbc.ra117.001325;
RA   Miller P.W., Pokutta S., Mitchell J.M., Chodaparambil J.V., Clarke D.N.,
RA   Nelson W.J., Weis W.I., Nichols S.A.;
RT   "Analysis of a vinculin homolog in a sponge (phylum Porifera) reveals that
RT   vertebrate-like cell adhesions emerged early in animal evolution.";
RL   J. Biol. Chem. 293:11674-11686(2018).
CC   -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC       structures to the plasma membrane. {ECO:0000305|PubMed:29880641}.
CC   -!- SUBUNIT: Interacts with VIN1 (vinculin); the interaction facilitates
CC       VIN1 binding to F-actin. {ECO:0000269|PubMed:29880641}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P0CE95}. Cytoplasm, cell cortex
CC       {ECO:0000250|UniProtKB:P0CE95}.
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DR   EMBL; MG852029; AYN71349.1; -; mRNA.
DR   AlphaFoldDB; A0A3G2LGI8; -.
DR   SMR; A0A3G2LGI8; -.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IEA:InterPro.
DR   GO; GO:0001726; C:ruffle; IEA:InterPro.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
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   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; IPR002404; IRS_PTB.
DR   InterPro; IPR011993; PH-like_dom_sf.
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   Pfam; PF16511; FERM_f0; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF01608; I_LWEQ; 1.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF09141; Talin_middle; 1.
DR   Pfam; PF08913; VBS; 1.
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; 6.
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   Cytoplasm; Cytoskeleton.
FT   CHAIN           1..2531
FT                   /note="Talin"
FT                   /id="PRO_0000451757"
FT   DOMAIN          87..401
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   DOMAIN          2287..2526
FT                   /note="I/LWEQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00292"
FT   REGION          598..621
FT                   /note="Interaction with VIN1"
FT                   /evidence="ECO:0000269|PubMed:29880641"
FT   REGION          2466..2485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2468..2482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2531 AA;  266048 MW;  42B92B532041C8C3 CRC64;
     MASLALRINI VDQNNVKTMQ FEPSMIVYDA CKMIRERIGE KPAAGQGYGL FLANEDPKRG
     VWLESGRTLD FYLLKPGDLL EYKNKMRPLR VRMMDESLKT VLVDDSFTVD QLVKTVCDRI
     GITNNEEFSL VCEDEEATPK KAAPPQIRNQ KKMDELKKKL HTEDDVNWLS HDKTLRSQGI
     SESQVLLLRK KFFFSDQNVD RNDPVQLNQL YAQARDAIVD GTHPCTYEEA INLAALQCQI
     VLGNHDSGKH KPGYITEELG SYLPREYVKA KGVERRVFTE HAKFTGLSQL NAKFRYIQVV
     RSLKTYGVTF FLVKEKMKGK NKLAPRLLGI TRESIMRVDE KTKEVMKTWP LTTVRRWAAS
     PNSFTLDFGD YSESYYSVQT TEGEQISRLI AGYIDIILKK KRATDRKVPE VEDETTLTED
     LVLPARATQV SYVTSTSDRG EEGQVAHPGV LRAAGESGAL FVPGDFLEGS HIQRQAAQTP
     GYSPAQQALQ SSIAKGLGCA DVAINELEAP TQLPPLGSDP QSLKWKQNTL DVSRQNVGSQ
     LAAMTAAAAQ MVGLTGADPA DIDYTAVGAA VTTLSSNLTE LSKGVRMIAA LQGNSHDGEK
     LLEAARGLAG AVRHLLKSAE PSENQNRKDL LDAAAALGIS GTQLMALMGD PDVTQEVQDA
     LLSKAKAVAV ATSGLVQNAK MVAGKCPDST LQSSVITATK GTATATSQLV ACTKIVASTI
     TNPLCQEQLI NSAKQVAGAV EGTVSSAQNA CSDDDALREL GMSATKVTDA LQDLLRYIRD
     IEAGGLRGGK YEEQIEMILA ATERLINSLG NAQETVKSAK TVAMATSQMV SGVKDEASGL
     SDEDAKRRLL AAARGLADAT AKMVDAAKVS ARDPSNVEAQ AALKAATEDL RAAVNAAANN
     ALKKKLIKKL EVAAKHTAAA ATQCIAAAQG AGPTNRNQSS QQQLLGNCKT VADHIGRLVQ
     AVRASMANPE SPSSQLGLIN ASQAMIQPCG KMIAASKAAV PTIGDQAAAL QLANFAKQTA
     TCLAELRTAA GKAAEACGSL EIESAIDVVR QLEADLLSVQ RTAASGKFLP LPGETAESCA
     LELGATSKTV GASMAQLLTA AAQGNENYTG IAARDTANAL KVLSGSVRGV AAATDDRSAQ
     EQIIVTAIQV MAHSRRLIEE AKKAIASPTN PENQSRLAQA AKAVSQALNQ VINCLPGQRD
     VDAAIKDIAA ASVALTTGQF PSAGGQSFQD VQTSLSVSSA ALNVSASELV ANSRGTHMQL
     AQSSQKFAGK YKTMLHSGLM LAGLSKEKAA RSKIVGYLRS VSMSSSKLLL AAKALSADPN
     APNVKNNLAA AARGVTDAIN ALVTVCTASA PGQKECDNAL RKIQTVGGML ANPVEPVNDN
     SYFVCLDAVM ENSKILGEAM GDITKHAKGE RHDEFGSAVS TAASAVCTLT ESAAQAAYLV
     AISDSSSTAA ISGLVDTSQF ARAQQAIREA CEQLLNPSSA QQQVLSSATV IAKHTSGLCN
     ACKIASGKTK NPVAKRKFVQ SAKDVATSTA NLVKSIKALA GTLNDGNRGD CAKTTKPLLE
     AIDDLVEFAS AAEFASVPAQ ISPEARSAQA PILVAGNNML IASSSLISSA KNLAVNPRDA
     ATWQLLASHS KAVSDAIRRL VAAVKDKSPG QAECDQAIEL LNMAINEVDQ ATLAAISSKL
     TPSSQSTLQG FHTQMMGGVS EISDLIEPVA LAAKGDAEKL GHMVTNVVSY FVPLSKAAVG
     AASKTTNPDR QMAVLEQTKT LAESALQLMY AAKESGGNPA AAAAGAHANI NEAAGNMTEA
     VKDLKGTLEM AASEAGLTAG MVDTIHKAAG TLDDPIHGEV SKSFGEYQES MVHSAKIIIL
     KAQDMVGRAG TSPGELGVIS KDATTSYCAL ATDCRGALAT ADDDVTGARL KAACQQLGDA
     LGDLIQCAGS VQSNPTDAIG RKELSDCAKK VGSKVNFVLA ALQAGAKGTQ ACINAVADVS
     GIVGDLDTSV MFATAGVLNP DREGDTFGEH REDILKTAKT LVEDTKTLVS GAAASQEQLA
     KAAVDAVGTI TRLADHVKKG AAALTSEDQE AQVLLLNAVR DVASSLGALI TATKNASGKS
     VQDPAMEHLR TCAKAMVSNV SSLLKTVKSV EDEAARGARA LESAIDAINA QLEELLSPNE
     PGRDASPEDI IRVTKGVTLA TAKAVAAGNS GRQDDVTASA NLGRKAIIDM MLTTKAAALK
     AESEDSKIRS ITAAKECTAA FRSLLELVHS ILMKPSHDKK QKLTAYSKEV ATCVSEVVQA
     AEVLKGTDWV DPSDPNIIAE NELLNAAASI EAAAKKLALL KPREKKHEAD ETLSFDEQIL
     EAARAIAAAT GALIKSATTA QRELVAQGRL RPGVPGSDDS QWAEGLVSAA RMVAAATQSL
     CEAANSAVQG VSSEEKLIAS AKAVAASTAQ LLLACQVKAD ADSENFKRLH KAGGAVKRAA
     ENLVTAAKRS SEEGDDEEVS GGGQERFVGG IAREIEAQEA ILRKERELDE AKRQLKKIRH
     DKYKRHGQDE P