TES_HUMAN
ID TES_HUMAN Reviewed; 421 AA.
AC Q9UGI8; A4D0U6; Q9GZQ1; Q9HAJ9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Testin;
DE AltName: Full=TESS;
GN Name=TES;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RX PubMed=10950921; DOI=10.1006/geno.2000.6272;
RA Tatarelli C., Linnenbach A., Mimori K., Croce C.M.;
RT "Characterization of the human TESTIN gene localized in the FRA7G region at
RT 7q31.2.";
RL Genomics 68:1-12(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11420696; DOI=10.1038/sj.onc.1204433;
RA Tobias E.S., Hurlstone A.F.L., MacKenzie E., McFarlane R., Black D.M.;
RT "The TES gene at 7q31.1 is methylated in tumours and encodes a novel
RT growth-suppressing LIM domain protein.";
RL Oncogene 20:2844-2853(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Prostate;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF CYS-391, AND
RP INTERACTION WITH ENAH; ZYX; VASP; ACTIN FIBERS; ALPHA-ACTININ AND PXN.
RX PubMed=12695497; DOI=10.1083/jcb.200211015;
RA Garvalov B.K., Higgins T.E., Sutherland J.D., Zettl M., Scaplehorn N.,
RA Koecher T., Piddini E., Griffiths G., Way M.;
RT "The conformational state of Tes regulates its zyxin-dependent recruitment
RT to focal adhesions.";
RL J. Cell Biol. 161:33-39(2003).
RN [8]
RP FUNCTION, INTERACTION WITH ZYX; GRIP1; ENAH AND TALIN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=12571287; DOI=10.1242/jcs.00278;
RA Coutts A.S., MacKenzie E., Griffith E., Black D.M.;
RT "TES is a novel focal adhesion protein with a role in cell spreading.";
RL J. Cell Sci. 116:897-906(2003).
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 INTERACTION WITH ALKBH4.
RX PubMed=23145062; DOI=10.1371/journal.pone.0049045;
RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A.,
RA Falnes P.O.;
RT "Human ALKBH4 interacts with proteins associated with transcription.";
RL PLoS ONE 7:E49045-E49045(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 357-421 IN COMPLEX WITH ZINC IONS
RP AND ENAH.
RX PubMed=18158903; DOI=10.1016/j.molcel.2007.10.033;
RA Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J.,
RA McDonald N.Q., Way M.;
RT "Tes, a specific Mena interacting partner, breaks the rules for EVH1
RT binding.";
RL Mol. Cell 28:1071-1082(2007).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 296-421 IN COMPLEX WITH ZINC
RP IONS; ENAH AND ACTL7A, MUTAGENESIS OF CYS-328, AND SUBUNIT.
RX PubMed=21278383; DOI=10.1074/jbc.m110.171264;
RA Boeda B., Knowles P.P., Briggs D.C., Murray-Rust J., Soriano E.,
RA Garvalov B.K., McDonald N.Q., Way M.;
RT "Molecular recognition of the Tes LIM2-3 domains by the actin-related
RT protein Arp7A.";
RL J. Biol. Chem. 286:11543-11554(2011).
CC -!- FUNCTION: Scaffold protein that may play a role in cell adhesion, cell
CC spreading and in the reorganization of the actin cytoskeleton. Plays a
CC role in the regulation of cell proliferation. May act as a tumor
CC suppressor. Inhibits tumor cell growth. {ECO:0000269|PubMed:11420696,
CC ECO:0000269|PubMed:12571287, ECO:0000269|PubMed:12695497}.
CC -!- SUBUNIT: Interacts via LIM domain 1 with ZYX. Interacts (via LIM domain
CC 3) with ENAH and VASP. Interacts with ALKBH4, talin, actin, alpha-
CC actinin, GRIP1 and PXN. Interacts (via LIM domain 2) with ACTL7A (via
CC N-terminus). Heterodimer with ACTL7A; the heterodimer interacts with
CC ENAH to form a heterotrimer. {ECO:0000269|PubMed:12571287,
CC ECO:0000269|PubMed:12695497, ECO:0000269|PubMed:18158903,
CC ECO:0000269|PubMed:21278383, ECO:0000269|PubMed:23145062}.
CC -!- INTERACTION:
CC Q9UGI8; Q9Y615: ACTL7A; NbExp=9; IntAct=EBI-2561654, EBI-10825302;
CC Q9UGI8; Q8N8S7: ENAH; NbExp=2; IntAct=EBI-2561654, EBI-2834410;
CC Q9UGI8; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2561654, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion.
CC Note=Detected along actin stress fibers.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UGI8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UGI8-2; Sequence=VSP_003122;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11420696}.
CC -!- DOMAIN: The N-terminal and the C-terminal halves of the protein can
CC associate with each other, thereby hindering interactions with ZYX.
CC {ECO:0000269|PubMed:12695497}.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
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DR EMBL; AF260225; AAG17635.1; -; Genomic_DNA.
DR EMBL; AF260225; AAG17636.1; -; Genomic_DNA.
DR EMBL; AF245356; AAG17612.1; -; mRNA.
DR EMBL; AF245357; AAG17613.1; -; mRNA.
DR EMBL; AJ250865; CAB65119.1; -; mRNA.
DR EMBL; AK021575; BAB13846.1; -; mRNA.
DR EMBL; AK291802; BAF84491.1; -; mRNA.
DR EMBL; AC073130; AAQ93367.1; -; Genomic_DNA.
DR EMBL; CH236947; EAL24365.1; -; Genomic_DNA.
DR EMBL; BC001451; AAH01451.1; -; mRNA.
DR CCDS; CCDS5763.1; -. [Q9UGI8-1]
DR CCDS; CCDS5764.1; -. [Q9UGI8-2]
DR RefSeq; NP_056456.1; NM_015641.3. [Q9UGI8-1]
DR RefSeq; NP_690042.1; NM_152829.2. [Q9UGI8-2]
DR PDB; 2IYB; X-ray; 2.35 A; E/F/G/H=357-421.
DR PDB; 2XQN; X-ray; 2.62 A; T=296-421.
DR PDBsum; 2IYB; -.
DR PDBsum; 2XQN; -.
DR AlphaFoldDB; Q9UGI8; -.
DR SMR; Q9UGI8; -.
DR BioGRID; 117572; 313.
DR IntAct; Q9UGI8; 58.
DR MINT; Q9UGI8; -.
DR STRING; 9606.ENSP00000350937; -.
DR GlyGen; Q9UGI8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UGI8; -.
DR MetOSite; Q9UGI8; -.
DR PhosphoSitePlus; Q9UGI8; -.
DR BioMuta; TES; -.
DR DMDM; 17380320; -.
DR EPD; Q9UGI8; -.
DR jPOST; Q9UGI8; -.
DR MassIVE; Q9UGI8; -.
DR MaxQB; Q9UGI8; -.
DR PaxDb; Q9UGI8; -.
DR PeptideAtlas; Q9UGI8; -.
DR PRIDE; Q9UGI8; -.
DR ProteomicsDB; 84218; -. [Q9UGI8-1]
DR ProteomicsDB; 84219; -. [Q9UGI8-2]
DR Antibodypedia; 2972; 192 antibodies from 26 providers.
DR DNASU; 26136; -.
DR Ensembl; ENST00000358204.9; ENSP00000350937.4; ENSG00000135269.18. [Q9UGI8-1]
DR Ensembl; ENST00000393481.6; ENSP00000377121.2; ENSG00000135269.18. [Q9UGI8-2]
DR GeneID; 26136; -.
DR KEGG; hsa:26136; -.
DR MANE-Select; ENST00000358204.9; ENSP00000350937.4; NM_015641.4; NP_056456.1.
DR UCSC; uc003vho.3; human. [Q9UGI8-1]
DR CTD; 26136; -.
DR DisGeNET; 26136; -.
DR GeneCards; TES; -.
DR HGNC; HGNC:14620; TES.
DR HPA; ENSG00000135269; Tissue enhanced (seminal).
DR MIM; 606085; gene.
DR neXtProt; NX_Q9UGI8; -.
DR OpenTargets; ENSG00000135269; -.
DR PharmGKB; PA37906; -.
DR VEuPathDB; HostDB:ENSG00000135269; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00940000155993; -.
DR HOGENOM; CLU_008937_1_1_1; -.
DR InParanoid; Q9UGI8; -.
DR OMA; NKLWHPA; -.
DR PhylomeDB; Q9UGI8; -.
DR TreeFam; TF313265; -.
DR PathwayCommons; Q9UGI8; -.
DR SignaLink; Q9UGI8; -.
DR BioGRID-ORCS; 26136; 10 hits in 1074 CRISPR screens.
DR ChiTaRS; TES; human.
DR EvolutionaryTrace; Q9UGI8; -.
DR GeneWiki; Testin; -.
DR GenomeRNAi; 26136; -.
DR Pharos; Q9UGI8; Tbio.
DR PRO; PR:Q9UGI8; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UGI8; protein.
DR Bgee; ENSG00000135269; Expressed in cauda epididymis and 185 other tissues.
DR ExpressionAtlas; Q9UGI8; baseline and differential.
DR Genevisible; Q9UGI8; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR CDD; cd09413; LIM1_Testin; 1.
DR CDD; cd09416; LIM2_Testin; 1.
DR CDD; cd09419; LIM3_Testin; 1.
DR CDD; cd09829; PET_testin; 1.
DR IDEAL; IID00684; -.
DR InterPro; IPR034958; LIM1_Testin.
DR InterPro; IPR034959; LIM2_Testin.
DR InterPro; IPR034960; LIM3_Testin.
DR InterPro; IPR010442; PET_domain.
DR InterPro; IPR033724; PET_testin.
DR InterPro; IPR027683; Testin.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24211:SF1; PTHR24211:SF1; 1.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF06297; PET; 1.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS51303; PET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cytoplasm; LIM domain;
KW Metal-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..421
FT /note="Testin"
FT /id="PRO_0000075906"
FT DOMAIN 92..199
FT /note="PET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT DOMAIN 234..297
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 299..359
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 362..421
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 133..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10950921,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_003122"
FT VARIANT 221
FT /note="A -> V (in dbSNP:rs2272193)"
FT /id="VAR_050170"
FT MUTAGEN 328
FT /note="C->A: Abolishes interaction with ACTL7A."
FT /evidence="ECO:0000269|PubMed:21278383"
FT MUTAGEN 391
FT /note="C->A: Abolishes localization at focal adhesions."
FT /evidence="ECO:0000269|PubMed:12695497"
FT CONFLICT 132
FT /note="K -> E (in Ref. 3; BAB13846)"
FT /evidence="ECO:0000305"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:2XQN"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:2XQN"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:2XQN"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:2XQN"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:2XQN"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:2XQN"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:2XQN"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:2XQN"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:2XQN"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:2IYB"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:2IYB"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:2IYB"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:2IYB"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:2IYB"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:2IYB"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:2IYB"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:2IYB"
FT HELIX 414..418
FT /evidence="ECO:0007829|PDB:2IYB"
SQ SEQUENCE 421 AA; 47996 MW; AB9FF6669C50D492 CRC64;
MDLENKVKKM GLGHEQGFGA PCLKCKEKCE GFELHFWRKI CRNCKCGQEE HDVLLSNEED
RKVGKLFEDT KYTTLIAKLK SDGIPMYKRN VMILTNPVAA KKNVSINTVT YEWAPPVQNQ
ALARQYMQML PKEKQPVAGS EGAQYRKKQL AKQLPAHDQD PSKCHELSPR EVKEMEQFVK
KYKSEALGVG DVKLPCEMDA QGPKQMNIPG GDRSTPAAVG AMEDKSAEHK RTQYSCYCCK
LSMKEGDPAI YAERAGYDKL WHPACFVCST CHELLVDMIY FWKNEKLYCG RHYCDSEKPR
CAGCDELIFS NEYTQAENQN WHLKHFCCFD CDSILAGEIY VMVNDKPVCK PCYVKNHAVV
CQGCHNAIDP EVQRVTYNNF SWHASTECFL CSCCSKCLIG QKFMPVEGMV FCSVECKKRM
S
