ID TLN1_HUMAN Reviewed; 2541 AA.
AC Q9Y490; A6NMY0; Q86YD0; Q9NZQ2; Q9UHH8; Q9UPX3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 3.
DT 29-MAY-2013, entry version 136.
DE RecName: Full=Talin-1;
GN Name=TLN1; Synonyms=KIAA1027, TLN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-1227.
RA Mao L., Fan Y.H.;
RT "Complete cDNA sequence of human talin.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=10610730; DOI=10.1006/geno.1999.6019;
RA Ben-Yosef T., Francomano C.A.;
RT "Characterization of the human talin (TLN) gene: genomic structure,
RT chromosomal localization, and expression pattern.";
RL Genomics 62:316-319(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TRP-1919.
RC TISSUE=Embryonic carcinoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 8-15; 34-82; 99-106; 119-131; 138-146; 148-156;
RP 165-178; 182-194; 197-234; 257-268; 307-316; 344-358; 428-438;
RP 442-454; 593-634; 674-685; 722-741; 766-824; 828-854; 862-869;
RP 876-910; 923-943; 958-999; 1026-1035; 1076-1086; 1097-1122; 1130-1184;
RP 1191-1198; 1208-1214; 1223-1269; 1274-1306; 1321-1340; 1362-1368;
RP 1402-1431; 1531-1541; 1560-1646; 1674-1780; 1863-1917; 1961-1973;
RP 2007-2016; 2025-2057; 2064-2085; 2090-2099; 2105-2115; 2120-2130;
RP 2134-2141; 2145-2154; 2169-2177; 2198-2209; 2221-2233; 2267-2274;
RP 2276-2321; 2322-2329; 2334-2361; 2369-2398; 2430-2443; 2456-2472;
RP 2477-2491; 2494-2510 AND 2512-2519, AND MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [9]
RP INTERACTION WITH NRAP.
RX PubMed=10320340; DOI=10.1021/bi982395t;
RA Luo G., Herrera A.H., Horowits R.;
RT "Molecular interactions of N-RAP, a nebulin-related protein of
RT striated muscle myotendon junctions and intercalated disks.";
RL Biochemistry 38:6135-6143(1999).
RN [10]
RP INTERACTION WITH PIP5K1C.
RX PubMed=12422220; DOI=10.1038/nature01082;
RA Ling K., Doughman R.L., Firestone A.J., Bunce M.W., Anderson R.A.;
RT "Type I gamma phosphatidylinositol phosphate kinase targets and
RT regulates focal adhesions.";
RL Nature 420:89-93(2002).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [12]
RP INTERACTION WITH SYNM.
RX PubMed=18342854; DOI=10.1016/j.yexcr.2008.01.034;
RA Sun N., Critchley D.R., Paulin D., Li Z., Robson R.M.;
RT "Identification of a repeated domain within mammalian alpha-synemin
RT that interacts directly with talin.";
RL Exp. Cell Res. 314:1839-1849(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2031 AND LYS-2115, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 607-631 IN COMPLEX WITH VCL.
RX PubMed=15070891; DOI=10.1074/jbc.M403076200;
RA Izard T., Vonrhein C.;
RT "Structural basis for amplifying vinculin activation by talin.";
RL J. Biol. Chem. 279:27667-27678(2004).
CC -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC structures to the plasma membrane. High molecular weight
CC cytoskeletal protein concentrated at regions of cell-substratum
CC contact and, in lymphocytes, at cell-cell contacts (By
CC similarity).
CC -!- SUBUNIT: Binds with high affinity to VCL and with low affinity to
CC integrins. Interacts with APBB1IP; this inhibits VCL binding.
CC Interacts with PTK2/FAK1 (By similarity). Interacts with PIP5K1C
CC and NRAP. Interacts with LAYN. Interacts with SYNM.
CC -!- INTERACTION:
CC P05556:ITGB1; NbExp=2; IntAct=EBI-2462036, EBI-703066;
CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane; Peripheral
CC membrane protein; Cytoplasmic side (By similarity). Cytoplasm,
CC cytoskeleton (By similarity). Note=Colocalizes with LAYN at the
CC membrane ruffles (By similarity).
CC -!- SIMILARITY: Contains 1 FERM domain.
CC -!- SIMILARITY: Contains 1 I/LWEQ domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA82979.2; Type=Erroneous initiation;
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DR EMBL; AF078828; AAD13152.1; -; mRNA.
DR EMBL; AF177198; AAF23322.1; -; mRNA.
DR EMBL; AF178534; AAF27330.1; -; Genomic_DNA.
DR EMBL; AF178081; AAF27330.1; JOINED; Genomic_DNA.
DR EMBL; AB028950; BAA82979.2; ALT_INIT; mRNA.
DR EMBL; AL133410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58352.1; -; Genomic_DNA.
DR EMBL; BC042923; AAH42923.1; -; mRNA.
DR IPI; IPI00298994; -.
DR RefSeq; NP_006280.3; NM_006289.3.
DR UniGene; Hs.471014; -.
DR PDB; 1SYQ; X-ray; 2.42 A; B=607-631.
DR PDB; 4DJ9; X-ray; 2.25 A; B=2075-2103.
DR PDBsum; 1SYQ; -.
DR PDBsum; 4DJ9; -.
DR ProteinModelPortal; Q9Y490; -.
DR IntAct; Q9Y490; 4.
DR MINT; MINT-5002070; -.
DR STRING; 9606.ENSP00000316029; -.
DR PhosphoSite; Q9Y490; -.
DR DMDM; 81175200; -.
DR OGP; Q9Y490; -.
DR PaxDb; Q9Y490; -.
DR PRIDE; Q9Y490; -.
DR Ensembl; ENST00000314888; ENSP00000316029; ENSG00000137076.
DR GeneID; 7094; -.
DR KEGG; hsa:7094; -.
DR UCSC; uc003zxt.2; human.
DR CTD; 7094; -.
DR GeneCards; GC09M035687; -.
DR HGNC; HGNC:11845; TLN1.
DR HPA; CAB002006; -.
DR HPA; HPA004748; -.
DR MIM; 186745; gene.
DR neXtProt; NX_Q9Y490; -.
DR PharmGKB; PA36547; -.
DR eggNOG; NOG324465; -.
DR HOGENOM; HOG000006734; -.
DR HOVERGEN; HBG023870; -.
DR InParanoid; Q9Y490; -.
DR KO; K06271; -.
DR OMA; ELGHGCA; -.
DR OrthoDB; EOG48PMJ8; -.
DR Pathway_Interaction_DB; amb2_neutrophils_pathway; amb2 Integrin signaling.
DR Pathway_Interaction_DB; avb3_integrin_pathway; Integrins in angiogenesis.
DR Pathway_Interaction_DB; a4b1_paxdep_pathway; Paxillin-dependent events mediated by a4b1.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17044; Muscle contraction.
DR Reactome; REACT_604; Hemostasis.
DR ChiTaRS; TLN1; human.
DR EvolutionaryTrace; Q9Y490; -.
DR GenomeRNAi; 7094; -.
DR NextBio; 27751; -.
DR ArrayExpress; Q9Y490; -.
DR Bgee; Q9Y490; -.
DR CleanEx; HS_TLN1; -.
DR Genevestigator; Q9Y490; -.
DR GermOnline; ENSG00000137076; Homo sapiens.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR GO; GO:0005911; C:cell-cell junction; IC:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; NAS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001726; C:ruffle; ISS:HGNC.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; NAS:UniProtKB.
DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0007043; P:cell-cell junction assembly; TAS:UniProtKB.
DR GO; GO:0007044; P:cell-substrate junction assembly; IEA:Compara.
DR GO; GO:0006928; P:cellular component movement; NAS:UniProtKB.
DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Compara.
DR GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; NAS:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; TAS:Reactome.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
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; IPR015710; Talin-1.
DR InterPro; IPR015224; Talin_cent.
DR InterPro; IPR015009; Vinculin-bd_dom.
DR InterPro; IPR006077; Vinculin/catenin.
DR PANTHER; PTHR19981:SF7; PTHR19981:SF7; 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 SMART; SM00307; ILWEQ; 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; 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; Acetylation; Cell membrane; Cell projection;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Membrane; Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 2541 Talin-1.
FT /FTId=PRO_0000219428.
FT DOMAIN 86 403 FERM.
FT DOMAIN 2293 2533 I/LWEQ.
FT REGION 280 435 Interaction with LAYN (By similarity).
FT REGION 1327 1948 Interaction with SYNM.
FT MOD_RES 425 425 Phosphoserine.
FT MOD_RES 1116 1116 Phosphotyrosine (By similarity).
FT MOD_RES 2031 2031 N6-acetyllysine.
FT MOD_RES 2040 2040 Phosphoserine.
FT MOD_RES 2115 2115 N6-acetyllysine.
FT MOD_RES 2273 2273 Phosphoserine (By similarity).
FT VARIANT 1227 1227 S -> L (in dbSNP:rs2295795).
FT /FTId=VAR_023751.
FT VARIANT 1919 1919 R -> W (in dbSNP:rs17854239).
FT /FTId=VAR_023752.
FT VARIANT 1984 1984 A -> T (in dbSNP:rs35642290).
FT /FTId=VAR_055538.
FT CONFLICT 824 824 R -> G (in Ref. 1; AAD13152 and 2;
FT AAF23322).
FT CONFLICT 1549 1549 A -> P (in Ref. 1; AAD13152 and 2;
FT AAF23322).
FT CONFLICT 1604 1604 K -> Q (in Ref. 1; AAD13152 and 2;
FT AAF23322).
FT CONFLICT 1701 1701 Q -> E (in Ref. 1; AAD13152 and 2;
FT AAF23322).
FT CONFLICT 1718 1718 N -> H (in Ref. 1; AAD13152 and 2;
FT AAF23322).
FT CONFLICT 1966 1966 A -> R (in Ref. 1; AAD13152).
FT CONFLICT 2256 2256 Missing (in Ref. 2; AAF27330).
FT HELIX 608 625
FT HELIX 2079 2098
SQ SEQUENCE 2541 AA; 269767 MW; E21575E9199BBC5C CRC64;
MVALSLKISI GNVVKTMQFE PSTMVYDACR IIRERIPEAP AGPPSDFGLF LSDDDPKKGI
WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI MVDDSKTVTD MLMTICARIG
ITNHDEYSLV RELMEEKKEE ITGTLRKDKT LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL
REQGVEEHET LLLRRKFFYS DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG
FQCQIQFGPH NEQKHKAGFL DLKDFLPKEY VKQKGERKIF QAHKNCGQMS EIEAKVRYVK
LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE WNLTNIKRWA
ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL KKKKSKDHFG LEGDEESTML
EDSVSPKKST VLQQQYNRVG KVEHGSVALP AIMRSGASGP ENFQVGSMPP AQQQITSGQM
HRGHMPPLTS AQQALTGTIN SSMQAVQAAQ ATLDDFDTLP PLGQDAASKA WRKNKMDESK
HEIHSQVDAI TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED
EGGSGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE LLQQIGESDT
DPHFQDALMQ 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 TPKASAGPQP LLVQSCKAVA
EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM VAAAKASVPT IQDQASAMQL
SQCAKNLGTA LAELRTAAQK AQEACGPLEM DSALSVVQNL EKDLQEVKAA ARDGKLKPLP
GETMEKCTQD LGNSTKAVSS AIAQLLGEVA QGNENYAGIA ARDVAGGLRS LAQAARGVAA
LTSDPAVQAI VLDTASDVLD KASSLIEEAK KAAGHPGDPE SQQRLAQVAK AVTQALNRCV
SCLPGQRDVD NALRAVGDAS KRLLSDSLPP STGTFQEAQS RLNEAAAGLN QAATELVQAS
RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ VVSNLKGISM SSSKLLLAAK
ALSTDPAAPN LKSQLAAAAR AVTDSINQLI TMCTQQAPGQ KECDNALREL ETVRELLENP
VQPINDMSYF GCLDSVMENS KVLGEAMTGI SQNAKNGNLP EFGDAISTAS KALCGFTEAA
AQAAYLVGVS DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK
HTSALCNSCR LASARTTNPT AKRQFVQSAK EVANSTANLV KTIKALDGAF TEENRAQCRA
ATAPLLEAVD NLSAFASNPE FSSIPAQISP EGRAAMEPIV ISAKTMLESA GGLIQTARAL
AVNPRDPPSW SVLAGHSRTV SDSIKKLITS MRDKAPGQLE CETAIAALNS CLRDLDQASL
AAVSQQLAPR EGISQEALHT QMLTAVQEIS HLIEPLANAA RAEASQLGHK VSQMAQYFEP
LTLAAVGAAS KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV
QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGEPEGSF VDYQTTMVRT
AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASEA KPAAVAAENE EIGSHIKHRV
QELGHGCAAL VTKAGALQCS PSDAYTKKEL IECARRVSEK VSHVLAALQA GNRGTQACIT
AASAVSGIIA DLDTTIMFAT AGTLNREGTE TFADHREGIL KTAKVLVEDT KVLVQNAAGS
QEKLAQAAQS SVATITRLAD VVKLGAASLG AEDPETQVVL INAVKDVAKA LGDLISATKA
AAGKVGDDPA VWQLKNSAKV MVTNVTSLLK TVKAVEDEAT KGTRALEATT EHIRQELAVF
CSPEPPAKTS TPEDFIRMTK GITMATAKAV AAGNSCRQED VIATANLSRR AIADMLRACK
EAAYHPEVAP DVRLRALHYG RECANGYLEL LDHVLLTLQK PSPELKQQLT GHSKRVAGSV
TELIQAAEAM KGTEWVDPED PTVIAENELL GAAAAIEAAA KKLEQLKPRA KPKEADESLN
FEEQILEAAK SIAAATSALV KAASAAQREL VAQGKVGAIP ANALDDGQWS QGLISAARMV
AAATNNLCEA ANAAVQGHAS QEKLISSAKQ VAASTAQLLV ACKVKADQDS EAMKRLQAAG
NAVKRASDNL VKAAQKAAAF EEQENETVVV KEKMVGGIAQ IIAAQEEMLR KERELEEARK
KLAQIRQQQY KFLPSELRDE H
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