GenomeNet

Database: UniProt
Entry: Q71LX4
LinkDB: Q71LX4
Original site: Q71LX4 
ID   TLN2_MOUSE              Reviewed;        2375 AA.
AC   Q71LX4; E9QM49; Q8BWK0;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   26-NOV-2014, entry version 100.
DE   RecName: Full=Talin-2;
GN   Name=Tln2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-135.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 30-2375.
RC   TISSUE=Kidney;
RA   Dubois A., Albiges-Rizo C., Block M., Faessler R.;
RT   "Expression of the newly identified Mus musculus talin 2 gene.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1666, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: As a major component of focal adhesion plaques that
CC       links integrin to the actin cytoskeleton, may play an important
CC       role in cell adhesion. Recruits PIP5K1C to focal adhesion plaques
CC       and strongly activates its kinase activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts directly with PIP5K1C. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
CC       Cell junction, synapse {ECO:0000250}. Cell membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Focal
CC       adhesion plaques and synapses. {ECO:0000250}.
CC   -!- SIMILARITY: Contains 1 FERM domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00084}.
CC   -!- SIMILARITY: Contains 1 I/LWEQ domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00292}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ05019.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=BAC34927.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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DR   EMBL; AC107740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC107755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC173343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF467081; AAQ05019.1; ALT_INIT; mRNA.
DR   EMBL; AK052301; BAC34927.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001074711.2; NM_001081242.2.
DR   UniGene; Mm.33645; -.
DR   PDB; 3G9W; X-ray; 2.16 A; A/B=198-408.
DR   PDBsum; 3G9W; -.
DR   ProteinModelPortal; Q71LX4; -.
DR   SMR; Q71LX4; 1-408, 489-915, 917-1047, 1209-1360, 1362-1794, 1887-2203, 2208-2375.
DR   DIP; DIP-53098N; -.
DR   IntAct; Q71LX4; 1.
DR   MINT; MINT-4997511; -.
DR   MaxQB; Q71LX4; -.
DR   PaxDb; Q71LX4; -.
DR   PRIDE; Q71LX4; -.
DR   GeneID; 70549; -.
DR   KEGG; mmu:70549; -.
DR   CTD; 83660; -.
DR   MGI; MGI:1917799; Tln2.
DR   eggNOG; NOG324465; -.
DR   HOGENOM; HOG000006734; -.
DR   HOVERGEN; HBG023870; -.
DR   InParanoid; Q71LX4; -.
DR   KO; K06271; -.
DR   ChiTaRS; Tln2; mouse.
DR   EvolutionaryTrace; Q71LX4; -.
DR   NextBio; 331831; -.
DR   PRO; PR:Q71LX4; -.
DR   CleanEx; MM_TLN2; -.
DR   Genevestigator; Q71LX4; -.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005916; C:fascia adherens; IDA:MGI.
DR   GO; GO:0005925; C:focal adhesion; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001726; C:ruffle; IEA:InterPro.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; IEA:InterPro.
DR   Gene3D; 1.20.1410.10; -; 4.
DR   Gene3D; 1.20.1420.10; -; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR002558; ILWEQ_dom.
DR   InterPro; IPR002404; Insln_rcpt_S1.
DR   InterPro; IPR011993; PH_like_dom.
DR   InterPro; IPR015711; Talin-2.
DR   InterPro; IPR015224; Talin_cent.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   InterPro; IPR015009; Vinculin-bd_dom.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   PANTHER; PTHR19981:SF15; PTHR19981:SF15; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF01608; I_LWEQ; 1.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF09141; Talin_middle; 1.
DR   Pfam; PF08913; VBS; 2.
DR   ProDom; PD011820; ILWEQ; 1.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF109880; SSF109880; 1.
DR   SUPFAM; SSF109885; SSF109885; 5.
DR   SUPFAM; SSF47031; SSF47031; 1.
DR   SUPFAM; SSF47220; SSF47220; 4.
DR   SUPFAM; SSF54236; SSF54236; 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; Complete proteome;
KW   Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Reference proteome;
KW   Synapse.
FT   CHAIN         1   2375       Talin-2.
FT                                /FTId=PRO_0000219432.
FT   DOMAIN       88    406       FERM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00084}.
FT   DOMAIN     2205   2375       I/LWEQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00292}.
FT   REGION      312    406       Interaction with PIP5K1C. {ECO:0000250}.
FT   COMPBIAS    862    943       Ala-rich.
FT   MOD_RES    1666   1666       Phosphotyrosine.
FT                                {ECO:0000269|PubMed:18034455}.
FT   CONFLICT    102    102       V -> K (in Ref. 2; BAC34927).
FT                                {ECO:0000305}.
FT   CONFLICT    432    432       R -> Q (in Ref. 3; AAQ05019).
FT                                {ECO:0000305}.
FT   CONFLICT    447    447       E -> K (in Ref. 3; AAQ05019).
FT                                {ECO:0000305}.
FT   CONFLICT   1003   1003       M -> V (in Ref. 3; AAQ05019).
FT                                {ECO:0000305}.
FT   CONFLICT   1030   1030       L -> P (in Ref. 3; AAQ05019).
FT                                {ECO:0000305}.
FT   CONFLICT   1755   1755       M -> I (in Ref. 3; AAQ05019).
FT                                {ECO:0000305}.
FT   CONFLICT   1775   1775       A -> V (in Ref. 3; AAQ05019).
FT                                {ECO:0000305}.
FT   CONFLICT   1792   1792       V -> Q (in Ref. 3; AAQ05019).
FT                                {ECO:0000305}.
FT   CONFLICT   1795   1795       A -> S (in Ref. 3; AAQ05019).
FT                                {ECO:0000305}.
FT   CONFLICT   1816   1816       I -> V (in Ref. 3; AAQ05019).
FT                                {ECO:0000305}.
FT   CONFLICT   2047   2047       V -> A (in Ref. 3; AAQ05019).
FT                                {ECO:0000305}.
FT   HELIX       211    226       {ECO:0000244|PDB:3G9W}.
FT   HELIX       234    249       {ECO:0000244|PDB:3G9W}.
FT   TURN        254    256       {ECO:0000244|PDB:3G9W}.
FT   HELIX       264    266       {ECO:0000244|PDB:3G9W}.
FT   HELIX       270    272       {ECO:0000244|PDB:3G9W}.
FT   HELIX       278    288       {ECO:0000244|PDB:3G9W}.
FT   TURN        289    291       {ECO:0000244|PDB:3G9W}.
FT   HELIX       294    307       {ECO:0000244|PDB:3G9W}.
FT   TURN        309    312       {ECO:0000244|PDB:3G9W}.
FT   STRAND      314    321       {ECO:0000244|PDB:3G9W}.
FT   STRAND      328    335       {ECO:0000244|PDB:3G9W}.
FT   STRAND      337    343       {ECO:0000244|PDB:3G9W}.
FT   TURN        345    347       {ECO:0000244|PDB:3G9W}.
FT   STRAND      350    355       {ECO:0000244|PDB:3G9W}.
FT   HELIX       356    358       {ECO:0000244|PDB:3G9W}.
FT   STRAND      361    365       {ECO:0000244|PDB:3G9W}.
FT   STRAND      368    372       {ECO:0000244|PDB:3G9W}.
FT   HELIX       374    376       {ECO:0000244|PDB:3G9W}.
FT   STRAND      381    384       {ECO:0000244|PDB:3G9W}.
FT   HELIX       388    407       {ECO:0000244|PDB:3G9W}.
SQ   SEQUENCE   2375 AA;  253621 MW;  2264EEEC374476FC CRC64;
     MVALSLKICV RHCNVVKTMQ FEPSTAVYDA CRVIRERVPE AQTGQASDYG LFLSDEDPRK
     GIWLEAGRTL DYYMLRNGDI LEYKKKQRPQ KIRMLDGSVK TVMVDDSKTV GELLVTICSR
     IGITNYEEYS LIQETIEEKK EEGTGTLKKD RTLLRDERKM EKLKAKLHTD DDLNWLDHSR
     TFREQGVDEN ETLLLRRKFF YSDQNVDSRD PVQLNLLYVQ ARDDILNGSH PVSFEKACEF
     GGFQAQIQFG PHVEHKHKPG FLDLKEFLPK EYIKQRGAEK RIFQEHKNCG EMSEIEAKVK
     YVKLARSLRT YGVSFFLVKE KMKGKNKLVP RLLGITKDSV MRVDEKTKEV LQEWPLTTVK
     RWAASPKSFT LDFGEYQESY YSVQTTEGEQ ISQLIAGYID IILKKKQSKD RFGLEGDEES
     TMLEESVSPK KRSTILQQQF NRTGKAEHGS VALPAVMRSG SSGPETFNVG SMPSPQQQVM
     VGQMHRGHMP PLTSAQQALM GTINTSMHAV QQAQDDLSEL DSLPPLGQDM ASRVWVQNKV
     DESKHEIHSQ VDAITAGTAS VVNLTAGDPA DTDYTAVGCA ITTISSNLTE MSKGVKLLAA
     LMDDDVGSGE DLLRAARTLA GAVSDLLKAV QPTSGEPRQT VLTAAGSIGQ ASGDLLRQIG
     ENETDERFQD VLMSLAKAVA NAAAMLVLKA KNVAQVAEDT VLQNRVIAAA TQCALSTSQL
     VACAKVVSPT ISSPVCQEQL IEAGKLVDRS VENCVRACQA ATSDSELLKQ VSAAASVVSQ
     ALHDLLQHVR QFASRGEPIG RYDQATDTIM CVTESIFSSM GDAGEMVRQA RVLAQATSDL
     VNAMRSDAEA EIDMENSKKL LAAAKLLADS TARMVEAAKG AAANPENEDQ QQRLREAAEG
     LRVATNAAAQ NAIKKKIVNR LEVAAKQAAA AATQTIAASQ NAAISNKNPS AQQQLVQSCK
     AVADHIPQLV QGVRGSQAQA EDLSAQLALI ISSQNFLQPG SKMVSSAKAA VPTVSDQAAA
     MQLSQCAKNL ATSLAELRTA SQKAHEACGP MEIDSALNTV QTLKNELQDA KMAAAESQLK
     PLPGETLEKC AQDLGSTSKG VGSSMAQLLT CAAQGNEHYT GVAARETAQA LKTLAQAARG
     VAASTNDPEA AHAMLDSARD VMEGSAMLIQ EAKQALIAPG DTESQQRLAQ VAKAVSHSLN
     NCVNCLPGQK DVDVALKSIG EASKKLLVDS LPPSTKPFQE AQSELNQAAA DLNQSAGEVV
     HATRGQSGEL AAASGKFSDD FDEFLDAGIE MAGQAQTKED QMQVIGNLKN ISMASSKLLL
     AAKSLSVDPG APNAKNLLAA AARAVTESIN QLIMLCTQQA PGQKECDNAL RELETVKGML
     ENPNEPVSDL SYFDCIESVM ENSKVLGESM AGISQNAKTG DLPAFGECVG IASKALCGLT
     EAAAQAAYLV GISDPNSQAG HQGLVDPIQF ARANQAIQMA CQNLVDPGSS PSQVLSAATI
     VAKHTSALCN ACRIASSKTA NPVAKRHFVQ SAKEVANSTA NLVKTIKALD GDFSEDNRNK
     CRIATTPLIE AVENLTAFAS NPEFASIPAQ ISSEGSQAQE PILVSAKTML ESSSYLIRTA
     RSLAINPKDP PTWSVLAGHS HTVSDSIKSL ITSIRDKAPG QRECDYSIDG INRCIRDIEQ
     ASLAAVSQSL ATRDDISVEA LQEQLTSVVQ EIGHLIDPIA TAARGEAAQL GHKVTQLASY
     FEPLILAAVG VASKMLDHQQ QMTVLDQTKT LAESALQMLY AAKEGGGNPK AVHTAPEPKG
     TFVDYQTTVV KYSKAIAVTA QEMIGFQIRT RVQDLGHGCI FLVQKAGALQ VCPTDSYTKR
     ELIECARSVT EKVSLVLSAL QAGNKGTQAC ITAATAVSGI IADLDTTIMF ATAGTLNAEN
     GETFADHREN ILKTAKALVE DTKLLVSGAA STPDKLAQAA QSSAATITQL AEVVKLGAAS
     LGSNDPETQV VLINAIKDVA KALSDLIGAT KGAASKPADD PSMYQLKGAA KVMVTNVTSL
     LKTVKAVEDE ATRGTRALEA TIEYIKQELT VFQSKDIPEK TSSPEESIRM TKGITMATAK
     AVAAGNSCRQ EDVIATANLS RKAVSDMLIA CKQASFYPDV SEEVRTRALR YGTECTLGYL
     DLLEHVLVIL QKPTPELKHQ LAAFSKRVAG AVTELIQAAE AMKGTEWVDP EDPTVIAETE
     LLGAAASIEA AAKKLEQLKP RAKPKQADET LDFEEQILEA AKSIAAATSA LVKSASAAQR
     ELVAQGKVGS IPANAADDGQ WSQGLISAAR MVAAATSSLC EAANASVQGH ASEEKLISSA
     KQVAASTAQL LVACKVKADQ DSEAMKRLQA AGNAV
//
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