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 01-MAY-2013, entry version 86.
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-28 AND TYR-1666, AND
RP MASS SPECTROMETRY.
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 -!- SUBUNIT: Interacts directly with PIP5K1C (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion (By
CC similarity). Cell junction, synapse (By similarity). Cell
CC membrane; Peripheral membrane protein; Cytoplasmic side (By
CC similarity). Cytoplasm, cytoskeleton (By similarity). Note=Focal
CC adhesion plaques and synapses (By similarity).
CC -!- SIMILARITY: Contains 1 FERM domain.
CC -!- SIMILARITY: Contains 1 I/LWEQ domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ05019.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAC34927.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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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 IPI; IPI00975167; -.
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, 1209-1360, 1362-1794, 1887-2203, 2208-2375.
DR IntAct; Q71LX4; 1.
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 KO; K06271; -.
DR OrthoDB; EOG48PMJ8; -.
DR EvolutionaryTrace; Q71LX4; -.
DR NextBio; 331831; -.
DR CleanEx; MM_TLN2; -.
DR Genevestigator; Q71LX4; -.
DR GermOnline; ENSMUSG00000052698; Mus musculus.
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:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 1.20.1420.10; -; 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; IPR015009; Vinculin-bd_dom.
DR InterPro; IPR006077; Vinculin/catenin.
DR PANTHER; PTHR19981:SF3; PTHR19981:SF3; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF01608; I_LWEQ; 2.
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; SSF47031; FERM_3-hlx; 1.
DR SUPFAM; SSF109880; Talin_cent; 1.
DR SUPFAM; SSF47220; Vinculin/catenin; 6.
DR PROSITE; PS00660; FERM_1; FALSE_NEG.
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.
FT DOMAIN 2205 2375 I/LWEQ.
FT REGION 312 406 Interaction with PIP5K1C (By similarity).
FT COMPBIAS 862 943 Ala-rich.
FT MOD_RES 28 28 Phosphotyrosine.
FT MOD_RES 1666 1666 Phosphotyrosine.
FT CONFLICT 102 102 V -> K (in Ref. 2; BAC34927).
FT CONFLICT 432 432 R -> Q (in Ref. 3; AAQ05019).
FT CONFLICT 447 447 E -> K (in Ref. 3; AAQ05019).
FT CONFLICT 1003 1003 M -> V (in Ref. 3; AAQ05019).
FT CONFLICT 1030 1030 L -> P (in Ref. 3; AAQ05019).
FT CONFLICT 1755 1755 M -> I (in Ref. 3; AAQ05019).
FT CONFLICT 1775 1775 A -> V (in Ref. 3; AAQ05019).
FT CONFLICT 1792 1792 V -> Q (in Ref. 3; AAQ05019).
FT CONFLICT 1795 1795 A -> S (in Ref. 3; AAQ05019).
FT CONFLICT 1816 1816 I -> V (in Ref. 3; AAQ05019).
FT CONFLICT 2047 2047 V -> A (in Ref. 3; AAQ05019).
FT HELIX 211 226
FT HELIX 234 249
FT TURN 254 256
FT HELIX 264 266
FT HELIX 270 272
FT HELIX 278 288
FT TURN 289 291
FT HELIX 294 307
FT TURN 309 312
FT STRAND 314 321
FT STRAND 328 335
FT STRAND 337 343
FT TURN 345 347
FT STRAND 350 355
FT HELIX 356 358
FT STRAND 361 365
FT STRAND 368 372
FT HELIX 374 376
FT STRAND 381 384
FT HELIX 388 407
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
//
