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 24-JAN-2024, entry version 154. DE RecName: Full=Talin-2; GN Name=Tln2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT 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., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., 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., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., 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 BY RP 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). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428; SER-450 AND SER-624, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: As a major component of focal adhesion plaques that links CC integrin to the actin cytoskeleton, may play an important role in cell CC adhesion. Recruits PIP5K1C to focal adhesion plaques and strongly CC activates its kinase activity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts directly with PIP5K1C. CC {ECO:0000250|UniProtKB:Q9Y4G6}. CC -!- INTERACTION: CC Q71LX4; P05556-5: ITGB1; Xeno; NbExp=3; IntAct=EBI-2255655, EBI-7208579; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4G6}. Cell CC junction, focal adhesion {ECO:0000250|UniProtKB:Q9Y4G6}. Synapse CC {ECO:0000250|UniProtKB:Q9Y4G6}. Cell membrane CC {ECO:0000250|UniProtKB:Q9Y4G6}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q9Y4G6}; Cytoplasmic side CC {ECO:0000250|UniProtKB:Q9Y4G6}. Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:Q9Y4G6}. Note=Focal adhesion plaques and CC synapses. {ECO:0000250|UniProtKB:Q9Y4G6}. CC -!- SEQUENCE CAUTION: CC Sequence=AAQ05019.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC34927.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 3G9W; X-ray; 2.16 A; A/B=198-408. DR PDBsum; 3G9W; -. DR AlphaFoldDB; Q71LX4; -. DR SMR; Q71LX4; -. DR BioGRID; 214125; 9. DR DIP; DIP-53098N; -. DR IntAct; Q71LX4; 7. DR MINT; Q71LX4; -. DR STRING; 10090.ENSMUSP00000039633; -. DR GlyConnect; 2751; 1 N-Linked glycan (1 site). DR GlyCosmos; Q71LX4; 1 site, 1 glycan. DR GlyGen; Q71LX4; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q71LX4; -. DR PhosphoSitePlus; Q71LX4; -. DR SwissPalm; Q71LX4; -. DR EPD; Q71LX4; -. DR jPOST; Q71LX4; -. DR MaxQB; Q71LX4; -. DR PaxDb; 10090-ENSMUSP00000039633; -. DR PeptideAtlas; Q71LX4; -. DR ProteomicsDB; 260667; -. DR Pumba; Q71LX4; -. DR GeneID; 70549; -. DR KEGG; mmu:70549; -. DR AGR; MGI:1917799; -. DR CTD; 83660; -. DR MGI; MGI:1917799; Tln2. DR eggNOG; KOG4261; Eukaryota. DR InParanoid; Q71LX4; -. DR OrthoDB; 25353at2759; -. DR BioGRID-ORCS; 70549; 3 hits in 81 CRISPR screens. DR ChiTaRS; Tln2; mouse. DR EvolutionaryTrace; Q71LX4; -. DR PRO; PR:Q71LX4; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q71LX4; Protein. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005916; C:fascia adherens; IDA:MGI. DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0001726; C:ruffle; IEA:InterPro. DR GO; GO:0045202; C:synapse; IDA:MGI. DR GO; GO:0051015; F:actin filament binding; IEA:InterPro. DR GO; GO:0005178; F:integrin binding; IBA:GO_Central. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR CDD; cd14473; FERM_B-lobe; 1. DR CDD; cd10569; FERM_C_Talin; 1. DR CDD; cd17172; FERM_F0_TLN2; 1. DR CDD; cd17174; FERM_F1_TLN2; 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; IPR018979; FERM_N. 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:SF34; TALIN-2; 1. DR Pfam; PF16511; FERM_f0; 1. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF09379; FERM_N; 1. DR Pfam; PF01608; I_LWEQ; 2. DR Pfam; PF09141; Talin_middle; 1. DR Pfam; PF21692; Talin_R4; 1. 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; 4. DR SUPFAM; SSF109885; I/LWEQ domain; 5. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF47031; Second domain of FERM; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 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; Cytoplasm; Cytoskeleton; KW Membrane; Phosphoprotein; Reference proteome; Synapse. FT CHAIN 1..2375 FT /note="Talin-2" FT /id="PRO_0000219432" FT DOMAIN 88..406 FT /note="FERM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084" FT DOMAIN 2205..2375 FT /note="I/LWEQ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00292" FT REGION 312..406 FT /note="Interaction with PIP5K1C" FT /evidence="ECO:0000250" FT MOD_RES 428 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 450 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 624 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1024 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9Y4G6" FT MOD_RES 1666 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18034455" FT CONFLICT 102 FT /note="V -> K (in Ref. 2; BAC34927)" FT /evidence="ECO:0000305" FT CONFLICT 432 FT /note="R -> Q (in Ref. 3; AAQ05019)" FT /evidence="ECO:0000305" FT CONFLICT 447 FT /note="E -> K (in Ref. 3; AAQ05019)" FT /evidence="ECO:0000305" FT CONFLICT 1003 FT /note="M -> V (in Ref. 3; AAQ05019)" FT /evidence="ECO:0000305" FT CONFLICT 1030 FT /note="L -> P (in Ref. 3; AAQ05019)" FT /evidence="ECO:0000305" FT CONFLICT 1755 FT /note="M -> I (in Ref. 3; AAQ05019)" FT /evidence="ECO:0000305" FT CONFLICT 1775 FT /note="A -> V (in Ref. 3; AAQ05019)" FT /evidence="ECO:0000305" FT CONFLICT 1792 FT /note="V -> Q (in Ref. 3; AAQ05019)" FT /evidence="ECO:0000305" FT CONFLICT 1795 FT /note="A -> S (in Ref. 3; AAQ05019)" FT /evidence="ECO:0000305" FT CONFLICT 1816 FT /note="I -> V (in Ref. 3; AAQ05019)" FT /evidence="ECO:0000305" FT CONFLICT 2047 FT /note="V -> A (in Ref. 3; AAQ05019)" FT /evidence="ECO:0000305" FT HELIX 211..226 FT /evidence="ECO:0007829|PDB:3G9W" FT HELIX 234..249 FT /evidence="ECO:0007829|PDB:3G9W" FT TURN 254..256 FT /evidence="ECO:0007829|PDB:3G9W" FT HELIX 264..266 FT /evidence="ECO:0007829|PDB:3G9W" FT HELIX 270..272 FT /evidence="ECO:0007829|PDB:3G9W" FT HELIX 278..288 FT /evidence="ECO:0007829|PDB:3G9W" FT TURN 289..291 FT /evidence="ECO:0007829|PDB:3G9W" FT HELIX 294..307 FT /evidence="ECO:0007829|PDB:3G9W" FT TURN 309..312 FT /evidence="ECO:0007829|PDB:3G9W" FT STRAND 314..321 FT /evidence="ECO:0007829|PDB:3G9W" FT STRAND 328..335 FT /evidence="ECO:0007829|PDB:3G9W" FT STRAND 337..343 FT /evidence="ECO:0007829|PDB:3G9W" FT TURN 345..347 FT /evidence="ECO:0007829|PDB:3G9W" FT STRAND 350..355 FT /evidence="ECO:0007829|PDB:3G9W" FT HELIX 356..358 FT /evidence="ECO:0007829|PDB:3G9W" FT STRAND 361..365 FT /evidence="ECO:0007829|PDB:3G9W" FT STRAND 368..372 FT /evidence="ECO:0007829|PDB:3G9W" FT HELIX 374..376 FT /evidence="ECO:0007829|PDB:3G9W" FT STRAND 381..384 FT /evidence="ECO:0007829|PDB:3G9W" FT HELIX 388..407 FT /evidence="ECO:0007829|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 //