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   24-JAN-2024, entry version 210.
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; 48.
DR   DIP; DIP-17039N; -.
DR   IntAct; Q9Y4G6; 23.
DR   MINT; Q9Y4G6; -.
DR   STRING; 9606.ENSP00000453508; -.
DR   TCDB; 8.A.25.1.7; the ezrin/radixin/moesin (ezrin) family.
DR   GlyCosmos; Q9Y4G6; 1 site, 1 glycan.
DR   GlyGen; Q9Y4G6; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q9Y4G6; -.
DR   PhosphoSitePlus; Q9Y4G6; -.
DR   SwissPalm; Q9Y4G6; -.
DR   BioMuta; TLN2; -.
DR   DMDM; 229463036; -.
DR   EPD; Q9Y4G6; -.
DR   jPOST; Q9Y4G6; -.
DR   MassIVE; Q9Y4G6; -.
DR   MaxQB; Q9Y4G6; -.
DR   PaxDb; 9606-ENSP00000453508; -.
DR   PeptideAtlas; Q9Y4G6; -.
DR   ProteomicsDB; 86203; -.
DR   Pumba; Q9Y4G6; -.
DR   Antibodypedia; 25560; 208 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   AGR; HGNC:15447; -.
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   OrthoDB; 25353at2759; -.
DR   PhylomeDB; Q9Y4G6; -.
DR   TreeFam; TF314677; -.
DR   PathwayCommons; Q9Y4G6; -.
DR   SignaLink; Q9Y4G6; -.
DR   BioGRID-ORCS; 83660; 12 hits in 1147 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 180 other cell types or tissues.
DR   ExpressionAtlas; Q9Y4G6; baseline and differential.
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; 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; 5.
DR   SUPFAM; SSF109885; I/LWEQ domain; 4.
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.
DR   Genevisible; Q9Y4G6; HS.
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; uncertain 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
//