TLN2_HUMAN
ID TLN2_HUMAN Reviewed; 2542 AA.
AC Q9Y4G6; A6NLB8;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 4.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Talin-2;
GN Name=TLN2; Synonyms=KIAA0320;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PIP5K1C, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Brain, and Skeletal muscle;
RX PubMed=12422219; DOI=10.1038/nature01147;
RA Di Paolo G., Pellegrini L., Letinic K., Cestra G., Zoncu R., Voronov S.,
RA Chang S., Guo J., Wenk M.R., De Camilli P.;
RT "Recruitment and regulation of phosphatidylinositol phosphate kinase type 1
RT gamma by the FERM domain of talin.";
RL Nature 420:85-89(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11527381; DOI=10.1006/bbrc.2001.5497;
RA Monkley S.J., Pritchard C.A., Critchley D.R.;
RT "Analysis of the mammalian talin2 gene TLN2.";
RL Biochem. Biophys. Res. Commun. 286:880-885(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 610-2542.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1843, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
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., Buerckstuemmer T.,
RA 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1843, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1843, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1023 AND THR-1843, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP VARIANT LEU-339, AND SUBCELLULAR LOCATION.
RX PubMed=27223613; DOI=10.1371/journal.pone.0155180;
RA Deng H., Deng S., Xu H., Deng H.X., Chen Y., Yuan L., Deng X., Yang S.,
RA Guan L., Zhang J., Yuan H., Guo Y.;
RT "Exome Sequencing of a Pedigree Reveals S339L Mutation in the TLN2 Gene as
RT a Cause of Fifth Finger Camptodactyly.";
RL PLoS ONE 11:E0155180-E0155180(2016).
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:0000269|PubMed:12422219}.
CC -!- INTERACTION:
CC Q9Y4G6; P00519: ABL1; NbExp=3; IntAct=EBI-1220811, EBI-375543;
CC Q9Y4G6; P05107: ITGB2; NbExp=5; IntAct=EBI-1220811, EBI-300173;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27223613}. Cell
CC junction, focal adhesion {ECO:0000269|PubMed:12422219}. Synapse
CC {ECO:0000269|PubMed:12422219}. Cell membrane; Peripheral membrane
CC protein; Cytoplasmic side {ECO:0000269|PubMed:12422219}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:12422219}. Note=Focal adhesion plaques
CC and synapses (PubMed:12422219). {ECO:0000269|PubMed:12422219}.
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DR EMBL; AF402000; AAM73764.1; -; mRNA.
DR EMBL; AC068233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC100839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB002318; BAA20778.2; -; mRNA.
DR CCDS; CCDS32261.1; -.
DR RefSeq; NP_055874.2; NM_015059.2.
DR RefSeq; XP_016878157.1; XM_017022668.1.
DR PDB; 6U4K; X-ray; 2.56 A; A=1-403.
DR PDBsum; 6U4K; -.
DR AlphaFoldDB; Q9Y4G6; -.
DR SMR; Q9Y4G6; -.
DR BioGRID; 123717; 42.
DR DIP; DIP-17039N; -.
DR IntAct; Q9Y4G6; 22.
DR MINT; Q9Y4G6; -.
DR STRING; 9606.ENSP00000453508; -.
DR GlyGen; Q9Y4G6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y4G6; -.
DR PhosphoSitePlus; Q9Y4G6; -.
DR BioMuta; TLN2; -.
DR DMDM; 229463036; -.
DR EPD; Q9Y4G6; -.
DR jPOST; Q9Y4G6; -.
DR MassIVE; Q9Y4G6; -.
DR MaxQB; Q9Y4G6; -.
DR PaxDb; Q9Y4G6; -.
DR PeptideAtlas; Q9Y4G6; -.
DR PRIDE; Q9Y4G6; -.
DR ProteomicsDB; 86203; -.
DR Antibodypedia; 25560; 198 antibodies from 23 providers.
DR DNASU; 83660; -.
DR Ensembl; ENST00000561311.5; ENSP00000453508.1; ENSG00000171914.17.
DR Ensembl; ENST00000636159.2; ENSP00000490662.2; ENSG00000171914.17.
DR GeneID; 83660; -.
DR KEGG; hsa:83660; -.
DR MANE-Select; ENST00000636159.2; ENSP00000490662.2; NM_015059.3; NP_055874.2.
DR UCSC; uc002alb.5; human.
DR CTD; 83660; -.
DR DisGeNET; 83660; -.
DR GeneCards; TLN2; -.
DR HGNC; HGNC:15447; TLN2.
DR HPA; ENSG00000171914; Tissue enhanced (kidney).
DR MIM; 607349; gene.
DR neXtProt; NX_Q9Y4G6; -.
DR OpenTargets; ENSG00000171914; -.
DR PharmGKB; PA37958; -.
DR VEuPathDB; HostDB:ENSG00000171914; -.
DR eggNOG; KOG4261; Eukaryota.
DR GeneTree; ENSGT00940000154699; -.
DR HOGENOM; CLU_000364_1_1_1; -.
DR InParanoid; Q9Y4G6; -.
DR OMA; NMVKHSK; -.
DR PhylomeDB; Q9Y4G6; -.
DR TreeFam; TF314677; -.
DR PathwayCommons; Q9Y4G6; -.
DR SignaLink; Q9Y4G6; -.
DR BioGRID-ORCS; 83660; 11 hits in 1071 CRISPR screens.
DR ChiTaRS; TLN2; human.
DR GeneWiki; TLN2; -.
DR GenomeRNAi; 83660; -.
DR Pharos; Q9Y4G6; Tbio.
DR PRO; PR:Q9Y4G6; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9Y4G6; protein.
DR Bgee; ENSG00000171914; Expressed in sural nerve and 178 other tissues.
DR ExpressionAtlas; Q9Y4G6; baseline and differential.
DR Genevisible; Q9Y4G6; HS.
DR GO; GO:0015629; C:actin cytoskeleton; NAS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IEA:InterPro.
DR GO; GO:0045202; C:synapse; NAS:UniProtKB.
DR GO; GO:0003779; F:actin binding; NAS:UniProtKB.
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:0005198; F:structural molecule activity; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; TAS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd12150; talin-RS; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
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; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR015009; Vinculin-bd_dom.
DR Pfam; PF16511; FERM_f0; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF01608; I_LWEQ; 2.
DR Pfam; PF09141; Talin_middle; 1.
DR Pfam; PF08913; VBS; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF109880; SSF109880; 1.
DR SUPFAM; SSF109885; SSF109885; 4.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF47220; SSF47220; 5.
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; Cytoplasm; Cytoskeleton;
KW Disease variant; Membrane; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..2542
FT /note="Talin-2"
FT /id="PRO_0000219431"
FT DOMAIN 88..406
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 2294..2533
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:0000250|UniProtKB:Q71LX4"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX4"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX4"
FT MOD_RES 1023
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1665
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX4"
FT MOD_RES 1843
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VARIANT 339
FT /note="S -> L (found in patients with fifth finger
FT camptodactyly syndrome; unknown pathological significance;
FT dbSNP:rs1343670062)"
FT /evidence="ECO:0000269|PubMed:27223613"
FT /id="VAR_076545"
FT VARIANT 340
FT /note="V -> A (in dbSNP:rs11634784)"
FT /id="VAR_055313"
FT VARIANT 1148
FT /note="A -> S (in dbSNP:rs2280279)"
FT /id="VAR_014432"
FT VARIANT 1148
FT /note="A -> T (in dbSNP:rs2280279)"
FT /id="VAR_059136"
FT VARIANT 1877
FT /note="V -> I (in dbSNP:rs7182971)"
FT /id="VAR_055314"
FT VARIANT 2144
FT /note="T -> I (in dbSNP:rs11633796)"
FT /id="VAR_055315"
FT VARIANT 2266
FT /note="F -> L (in dbSNP:rs3816988)"
FT /id="VAR_014433"
FT CONFLICT 285
FT /note="E -> A (in Ref. 1; AAM73764)"
FT /evidence="ECO:0000305"
FT CONFLICT 1269
FT /note="L -> F (in Ref. 1; AAM73764)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:6U4K"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:6U4K"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:6U4K"
FT TURN 182..186
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 211..226
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 234..249
FT /evidence="ECO:0007829|PDB:6U4K"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:6U4K"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 294..307
FT /evidence="ECO:0007829|PDB:6U4K"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 314..322
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 325..335
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:6U4K"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 366..375
FT /evidence="ECO:0007829|PDB:6U4K"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:6U4K"
FT HELIX 388..399
FT /evidence="ECO:0007829|PDB:6U4K"
SQ SEQUENCE 2542 AA; 271613 MW; 802D50915F4FD4B0 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 KSTILQQQFN RTGKAEHGSV ALPAVMRSGS SGPETFNVGS MPSPQQQVMV
GQMHRGHMPP LTSAQQALMG TINTSMHAVQ QAQDDLSELD SLPPLGQDMA SRVWVQNKVD
ESKHEIHSQV DAITAGTASV VNLTAGDPAD TDYTAVGCAI TTISSNLTEM SKGVKLLAAL
MDDEVGSGED LLRAARTLAG AVSDLLKAVQ PTSGEPRQTV LTAAGSIGQA SGDLLRQIGE
NETDERFQDV LMSLAKAVAN AAAMLVLKAK NVAQVAEDTV LQNRVIAAAT QCALSTSQLV
ACAKVVSPTI SSPVCQEQLI EAGKLVDRSV ENCVRACQAA TTDSELLKQV SAAASVVSQA
LHDLLQHVRQ FASRGEPIGR YDQATDTIMC VTESIFSSMG DAGEMVRQAR VLAQATSDLV
NAMRSDAEAE IDMENSKKLL AAAKLLADST ARMVEAAKGA AANPENEDQQ QRLREAAEGL
RVATNAAAQN AIKKKIVNRL EVAAKQAAAA ATQTIAASQN AAVSNKNPAA QQQLVQSCKA
VADHIPQLVQ GVRGSQAQAE DLSAQLALII SSQNFLQPGS KMVSSAKAAV PTVSDQAAAM
QLSQCAKNLA TSLAELRTAS QKAHEACGPM EIDSALNTVQ TLKNELQDAK MAAVESQLKP
LPGETLEKCA QDLGSTSKAV GSSMAQLLTC AAQGNEHYTG VAARETAQAL KTLAQAARGV
AASTTDPAAA HAMLDSARDV MEGSAMLIQE AKQALIAPGD AERQQRLAQV AKAVSHSLNN
CVNCLPGQKD VDVALKSIGE SSKKLLVDSL PPSTKPFQEA QSELNQAAAD LNQSAGEVVH
ATRGQSGELA AASGKFSDDF DEFLDAGIEM AGQAQTKEDQ IQVIGNLKNI SMASSKLLLA
AKSLSVDPGA PNAKNLLAAA ARAVTESINQ LITLCTQQAP GQKECDNALR ELETVKGMLD
NPNEPVSDLS YFDCIESVME NSKVLGESMA GISQNAKTGD LPAFGECVGI ASKALCGLTE
AAAQAAYLVG ISDPNSQAGH QGLVDPIQFA RANQAIQMAC QNLVDPGSSP SQVLSAATIV
AKHTSALCNA CRIASSKTAN PVAKRHFVQS AKEVANSTAN LVKTIKALDG DFSEDNRNKC
RIATAPLIEA VENLTAFASN PEFVSIPAQI SSEGSQAQEP ILVSAKTMLE SSSYLIRTAR
SLAINPKDPP TWSVLAGHSH TVSDSIKSLI TSIRDKAPGQ RECDYSIDGI NRCIRDIEQA
SLAAVSQSLA TRDDISVEAL QEQLTSVVQE IGHLIDPIAT AARGEAAQLG HKVTQLASYF
EPLILAAVGV ASKILDHQQQ MTVLDQTKTL AESALQMLYA AKEGGGNPKA QHTHDAITEA
AQLMKEAVDD IMVTLNEAAS EVGLVGGMVD AIAEAMSKLD EGTPPEPKGT FVDYQTTVVK
YSKAIAVTAQ EMMTKSVTNP EELGGLASQM TSDYGHLAFQ GQMAAATAEP EEIGFQIRTR
VQDLGHGCIF LVQKAGALQV CPTDSYTKRE LIECARAVTE KVSLVLSALQ AGNKGTQACI
TAATAVSGII ADLDTTIMFA TAGTLNAENS ETFADHRENI LKTAKALVED TKLLVSGAAS
TPDKLAQAAQ SSAATITQLA EVVKLGAASL GSDDPETQVV LINAIKDVAK ALSDLISATK
GAASKPVDDP SMYQLKGAAK VMVTNVTSLL KTVKAVEDEA TRGTRALEAT IECIKQELTV
FQSKDVPEKT SSPEESIRMT KGITMATAKA VAAGNSCRQE DVIATANLSR KAVSDMLTAC
KQASFHPDVS DEVRTRALRF GTECTLGYLD LLEHVLVILQ KPTPEFKQQL AAFSKRVAGA
VTELIQAAEA MKGTEWVDPE DPTVIAETEL LGAAASIEAA AKKLEQLKPR AKPKQADETL
DFEEQILEAA KSIAAATSAL VKSASAAQRE LVAQGKVGSI PANAADDGQW SQGLISAARM
VAAATSSLCE AANASVQGHA SEEKLISSAK QVAASTAQLL VACKVKADQD SEAMRRLQAA
GNAVKRASDN LVRAAQKAAF GKADDDDVVV KTKFVGGIAQ IIAAQEEMLK KERELEEARK
KLAQIRQQQY KFLPTELRED EG
