ID   G3V852_RAT              Unreviewed;      2541 AA.
AC   G3V852;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=Talin 1 {ECO:0000313|Ensembl:ENSRNOP00000022401.5};
GN   Name=Tln1 {ECO:0000313|Ensembl:ENSRNOP00000022401.5,
GN   ECO:0000313|RGD:1306247};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000022401.5, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000022401.5, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000022401.5,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:16641100}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [3] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [4] {ECO:0000313|Ensembl:ENSRNOP00000022401.5}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000022401.5};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; NP_001034114.2; NM_001039025.2.
DR   AlphaFoldDB; G3V852; -.
DR   SMR; G3V852; -.
DR   STRING; 10116.ENSRNOP00000022401; -.
DR   PhosphoSitePlus; G3V852; -.
DR   PaxDb; 10116-ENSRNOP00000022401; -.
DR   Ensembl; ENSRNOT00000022400.6; ENSRNOP00000022401.5; ENSRNOG00000016630.7.
DR   GeneID; 313494; -.
DR   KEGG; rno:313494; -.
DR   AGR; RGD:1306247; -.
DR   CTD; 7094; -.
DR   RGD; 1306247; Tln1.
DR   eggNOG; KOG4261; Eukaryota.
DR   GeneTree; ENSGT00940000157006; -.
DR   HOGENOM; CLU_000364_1_1_1; -.
DR   OrthoDB; 25353at2759; -.
DR   TreeFam; TF314677; -.
DR   Reactome; R-RNO-114608; Platelet degranulation.
DR   Reactome; R-RNO-354192; Integrin signaling.
DR   Reactome; R-RNO-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR   Reactome; R-RNO-372708; p130Cas linkage to MAPK signaling for integrins.
DR   Reactome; R-RNO-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR   Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR   Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000016630; Expressed in spleen and 19 other cell types or tissues.
DR   GO; GO:0005912; C:adherens junction; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0001726; C:ruffle; IEA:InterPro.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005178; F:integrin binding; IPI:RGD.
DR   GO; GO:0030274; F:LIM domain binding; ISO:RGD.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISO:RGD.
DR   GO; GO:0001786; F:phosphatidylserine binding; ISO:RGD.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0017166; F:vinculin binding; ISO:RGD.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007044; P:cell-substrate junction assembly; ISO:RGD.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:RGD.
DR   GO; GO:0033622; P:integrin activation; ISO:RGD.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd10569; FERM_C_Talin; 1.
DR   CDD; cd17171; FERM_F0_TLN1; 1.
DR   CDD; cd17173; FERM_F1_TLN1; 1.
DR   CDD; cd12150; talin-RS; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 5.
DR   Gene3D; 1.20.1410.10; I/LWEQ domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.20.1420.10; Talin, central domain; 7.
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; IPR037438; Talin1/2-RS.
DR   InterPro; IPR015224; Talin_cent.
DR   InterPro; IPR036476; Talin_cent_sf.
DR   InterPro; IPR049108; Talin_R4.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR015009; Vinculin-bd_dom.
DR   PANTHER; PTHR19981; TALIN; 1.
DR   PANTHER; PTHR19981:SF7; TALIN-1; 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; PF21692; Talin_R4; 2.
DR   Pfam; PF08913; VBS; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00307; ILWEQ; 1.
DR   SMART; SM01244; IRS; 1.
DR   SUPFAM; SSF109880; A middle domain of Talin 1; 1.
DR   SUPFAM; SSF47220; alpha-catenin/vinculin-like; 5.
DR   SUPFAM; SSF109885; I/LWEQ domain; 4.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   COILED          1024..1077
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2463..2528
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   2541 AA;  269672 MW;  755E0BB7E7FBE5DF CRC64;
     MVALSLRISI GNVVKTMQFE PSTMVYDACR MIRERIPEAL AGPPSDFGLF LSDDDPKKGI
     WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI MVDDSKTVTD MLMTICARIG
     ITNHDEYSLV RELMEEKKDE GTGTLRKDKT LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL
     REQGVEEHET LLLRRKFFYS DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG
     FQCQIQFGPH NEQKHKAGFL DLKDFLPKEY VKQKGERKIF QAHKNCGQMS EIEAKVRYVK
     LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE WSLTNIKRWA
     ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL KKKKSKDHFG LEGDEESTML
     EDSVSPKKST VLQQQYNRVG KAEHGSVALP AIMRSGASGP ENFQVGSMPP AQQQVTSGQM
     HRGHMPPLTS AQQALTGTIN SSMQAVQAAQ AALDDFDALP PLGQDAASKA WRKNKMDESK
     HEIHSQVDAI TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED
     EGGNGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE LLQQIGESDT
     DPHFQDILMQ LAKAVASAAA ALVLKAKSVA QRTEDSGLQT QVIAAATQCA LSTSQLVACT
     KVVAPTISSP VCQEQLVEAG RLVAKAVEGC VSASQAATED GQLLRGVGAA ATAVTQALNE
     LLQHVKAHAT GAGPAGRYDQ ATDTILTVTE NIFSSMGDAG EMVRQARILA QATSDLVNAI
     KADAEGESDL ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA
     TNAAAQNAIK KKLVQRLEHA AKQAAASATQ TIAAAQHAAS APKASAGPQP LLVQSCKAVA
     EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM VAAAKASVPT IQDQASAMQL
     SQCAKNLGTA LAELRTAAQK AQEACGPLEM DSALSVVQNL EKDLQEIKAA AREGKLKPLP
     GETMEKCTQD LGNSTKAVSS AIAKLLGEIA QGNENYAGIA ARDVAGGLRS LAQAARGVAA
     LTTDPAVQAI VLDTASDALD KASSLIEEAK KASGHPGDPE SQQRLAQVAK AVTQALNRCV
     SCLPGQRDVD NALRAVGDAS KRLLSDSLPP STGTFQEAQS RLNEAAAGLN QAATELVQAS
     RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ VVSNLKGISM SSSKLLLAAK
     ALSTDPAAPN LKSQLAAAAR AVTDSINQLI TMCTQQAPGQ KECDNALRQL ETVRELLENP
     VQPINDMSYF GCLDSVMENS KVLGEAMTGI SQNAKNGNLP EFGDAIATAS KALCGFTEAA
     AQAAYLVGVS DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK
     HTSALCNSCR LASARTANPT AKRQFVQSAK EVANSTANLV KTIKALDGAF TEENRAQCRA
     ATAPLLEAVD NLSAFASNPE FSSVPAQISP EGRAAMEPIV ISAKTMLESA GGLIQTARAL
     AVNPRDPPRW SVLAGHSRTV SDSIKKLITS MRDKAPGQLE CETAIAALNS CLRDLDQASL
     AAVSQQLAPR EGISQEALHT QMLTAVQEIS HLIEPLASAA RAEASQLGHK VSQMAQYFEP
     LTLAAVGAAS KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV
     QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGEPEGSF VDYQTTMVRT
     AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASQA KPAAVAAENE EIGAHIKHRV
     QELGHGCSAL VTKAGALQCS PSDVYTKKEL IECARRVSEK VSHVLAALQA GNRGTQACIT
     AASAVSGIIA DLDTTIMFAT AGTLNREGAE TFADHREGIL KTAKVLVEDT KVLVQNAAGS
     QEKLAQAAQS SVATITRLAD VVKLGAASLG AEDPETQVVL INAVKDVAKA LGDLISATKA
     AAGKVGDDPA VWQLKNSAKV MVTNVTSLLK TVKAVEDEAT KGTRALEATT EHIRQELAVF
     CSPEPPAKTS TPEDFIRMTK GITMATAKAV AAGNSCRQED VIATANLSRR AIADMLRACK
     EAAFHPEVAP DVRLRALHFG RECANGYLEL LDHVLLTLQK PNPELKQQLT GHSKRVAGSV
     TELIQAAEAM KGTEWVDPED PTVIAENELL GAAAAIEAAA KKLEQLKPRA KPKEADESLN
     FEEQILEAAK SIAAATSALV KAASAAQREL VAQGKVGAIP ANALDDGQWS QGLISAARMV
     AAATNNLCEA ANAAVQGHAS QEKLISSAKQ VAASTAQLLV ACKVKADQDS EAMKRLQAAG
     NAVKRASDNL VKAAQKAAAF EDQENETVVV KEKMVGGIAQ IIAAQEEMLR KERELEEARK
     KLAQIRQQQY KFLPSELRDE H
//