TIAR_HUMAN
ID TIAR_HUMAN Reviewed; 375 AA.
AC Q01085; A8K3T0; A8K4L9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Nucleolysin TIAR;
DE AltName: Full=TIA-1-related protein;
GN Name=TIAL1;
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] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1326761; DOI=10.1073/pnas.89.18.8681;
RA Kawakami A., Tian Q., Duan X., Streuli M., Schlossman S.F., Anderson P.;
RT "Identification and functional characterization of a TIA-1-related
RT nucleolysin.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8681-8685(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung;
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 [3]
RP FUNCTION, AND DOMAIN.
RX PubMed=8576255; DOI=10.1074/jbc.271.5.2783;
RA Dember L.M., Kim N.D., Liu K.Q., Anderson P.;
RT "Individual RNA recognition motifs of TIA-1 and TIAR have different RNA
RT binding specificities.";
RL J. Biol. Chem. 271:2783-2788(1996).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10613902; DOI=10.1083/jcb.147.7.1431;
RA Kedersha N.L., Gupta M., Li W., Miller I., Anderson P.;
RT "RNA-binding proteins TIA-1 and TIAR link the phosphorylation of eIF-2
RT alpha to the assembly of mammalian stress granules.";
RL J. Cell Biol. 147:1431-1442(1999).
RN [5]
RP INTERACTION WITH FASTK.
RX PubMed=17135269; DOI=10.1074/jbc.c600198200;
RA Izquierdo J.M., Valcarcel J.;
RT "Fas-activated serine/threonine kinase (FAST K) synergizes with TIA-1/TIAR
RT proteins to regulate Fas alternative splicing.";
RL J. Biol. Chem. 282:1539-1543(2007).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17488725; DOI=10.1074/jbc.m700688200;
RA Izquierdo J.M., Valcarcel J.;
RT "Two isoforms of the T-cell intracellular antigen 1 (TIA-1) splicing factor
RT display distinct splicing regulation activities. Control of TIA-1 isoform
RT ratio by TIA-1-related protein.";
RL J. Biol. Chem. 282:19410-19417(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [9]
RP PHOSPHORYLATION BY MAPK14.
RX PubMed=20932473; DOI=10.1016/j.molcel.2010.09.018;
RA Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S., van Vugt M.A.,
RA Wang X., Linding R., Ong S.E., Weaver D., Carr S.A., Yaffe M.B.;
RT "DNA damage activates a spatially distinct late cytoplasmic cell-cycle
RT checkpoint network controlled by MK2-mediated RNA stabilization.";
RL Mol. Cell 40:34-49(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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 [12]
RP STRUCTURE BY NMR OF 1-282.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA binding domains of nucleolysin TIAR.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: RNA-binding protein involved in alternative pre-RNA splicing
CC and in cytoplasmic stress granules formation (PubMed:1326761,
CC PubMed:8576255, PubMed:17488725, PubMed:10613902). Shows a preference
CC for uridine-rich RNAs (PubMed:8576255). Activates splicing of
CC alternative exons with weak 5' splice sites followed by a U-rich
CC stretch on its own pre-mRNA and on TIA1 mRNA (By similarity). Promotes
CC the inclusion of TIA1 exon 5 to give rise to the long isoform (isoform
CC a) of TIA1 (PubMed:17488725). Acts downstream of the stress-induced
CC phosphorylation of EIF2S1/EIF2A to promote the recruitment of
CC untranslated mRNAs to cytoplasmic stress granules (SG)
CC (PubMed:10613902). Possesses nucleolytic activity against cytotoxic
CC lymphocyte target cells (PubMed:1326761). May be involved in apoptosis
CC (PubMed:1326761). {ECO:0000250|UniProtKB:P70318,
CC ECO:0000269|PubMed:10613902, ECO:0000269|PubMed:1326761,
CC ECO:0000269|PubMed:17488725, ECO:0000269|PubMed:8576255}.
CC -!- SUBUNIT: Interacts with FASTK. {ECO:0000269|PubMed:17135269}.
CC -!- INTERACTION:
CC Q01085; Q9HCE1: MOV10; NbExp=2; IntAct=EBI-2820828, EBI-1055820;
CC Q01085-2; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-11064654, EBI-357530;
CC Q01085-2; P19801: AOC1; NbExp=3; IntAct=EBI-11064654, EBI-12826295;
CC Q01085-2; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-11064654, EBI-953896;
CC Q01085-2; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-11064654, EBI-12809220;
CC Q01085-2; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-11064654, EBI-1383687;
CC Q01085-2; Q9BZC1-2: CELF4; NbExp=3; IntAct=EBI-11064654, EBI-12818201;
CC Q01085-2; Q15038: DAZAP2; NbExp=5; IntAct=EBI-11064654, EBI-724310;
CC Q01085-2; Q92567-2: FAM168A; NbExp=5; IntAct=EBI-11064654, EBI-11978259;
CC Q01085-2; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-11064654, EBI-12193763;
CC Q01085-2; Q96AE4-2: FUBP1; NbExp=3; IntAct=EBI-11064654, EBI-12121668;
CC Q01085-2; Q7Z429: GRINA; NbExp=3; IntAct=EBI-11064654, EBI-2832909;
CC Q01085-2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-11064654, EBI-6509505;
CC Q01085-2; Q13351: KLF1; NbExp=3; IntAct=EBI-11064654, EBI-8284732;
CC Q01085-2; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-11064654, EBI-10261141;
CC Q01085-2; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-11064654, EBI-716006;
CC Q01085-2; Q8NDC0: MAPK1IP1L; NbExp=3; IntAct=EBI-11064654, EBI-741424;
CC Q01085-2; Q5VZF2-2: MBNL2; NbExp=3; IntAct=EBI-11064654, EBI-13307411;
CC Q01085-2; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-11064654, EBI-740924;
CC Q01085-2; P86480: PRR20D; NbExp=3; IntAct=EBI-11064654, EBI-12754095;
CC Q01085-2; Q96PU8: QKI; NbExp=3; IntAct=EBI-11064654, EBI-945792;
CC Q01085-2; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-11064654, EBI-11987469;
CC Q01085-2; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-11064654, EBI-12275818;
CC Q01085-2; P09012: SNRPA; NbExp=3; IntAct=EBI-11064654, EBI-607085;
CC Q01085-2; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-11064654, EBI-2559305;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10613902}. Cytoplasm
CC {ECO:0000250|UniProtKB:P70318}. Cytolytic granule
CC {ECO:0000269|PubMed:1326761}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:10613902, ECO:0000269|PubMed:18691976}.
CC Note=Nuclear import seems to be coupled to RNA polymerase II
CC transcription and may be dependent on RNA-binding (By similarity).
CC Accumulates in cytoplasmic stress granules (SG) following cellular
CC damage (PubMed:10613902). {ECO:0000250|UniProtKB:P70318,
CC ECO:0000269|PubMed:10613902}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q01085-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q01085-2; Sequence=VSP_043700;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, lung and
CC skeletal muscle. {ECO:0000269|PubMed:17488725}.
CC -!- DOMAIN: The RRM 2 domain is required for the binding to target RNA, and
CC the RRM 1 and RRM 3 domains seem to contribute to the affinity of the
CC interaction with RNA. {ECO:0000269|PubMed:8576255}.
CC -!- DOMAIN: The RRM2 domain and the C-terminal residues 290-339 contribute
CC to nuclear localization. {ECO:0000250|UniProtKB:P70318}.
CC -!- DOMAIN: The RRM3 domain mediates nuclear export and cytoplasmic
CC localization in a manner dependent on RNA- binding.
CC {ECO:0000250|UniProtKB:P70318}.
CC -!- PTM: Phosphorylated by MAPK14 following DNA damage, releasing TIAR from
CC GADD45A mRNA. {ECO:0000269|PubMed:20932473}.
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DR EMBL; M96954; AAA36384.1; -; mRNA.
DR EMBL; AK290695; BAF83384.1; -; mRNA.
DR EMBL; AK290984; BAF83673.1; -; mRNA.
DR CCDS; CCDS31295.1; -. [Q01085-2]
DR CCDS; CCDS7613.1; -. [Q01085-1]
DR PIR; A46174; A46174.
DR RefSeq; NP_001029097.1; NM_001033925.1. [Q01085-2]
DR RefSeq; NP_003243.1; NM_003252.3. [Q01085-1]
DR PDB; 1X4G; NMR; -; A=187-282.
DR PDB; 2CQI; NMR; -; A=1-90.
DR PDB; 2DH7; NMR; -; A=89-180.
DR PDBsum; 1X4G; -.
DR PDBsum; 2CQI; -.
DR PDBsum; 2DH7; -.
DR AlphaFoldDB; Q01085; -.
DR SMR; Q01085; -.
DR BioGRID; 112929; 138.
DR DIP; DIP-42425N; -.
DR IntAct; Q01085; 68.
DR MINT; Q01085; -.
DR STRING; 9606.ENSP00000358089; -.
DR GlyGen; Q01085; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q01085; -.
DR PhosphoSitePlus; Q01085; -.
DR SwissPalm; Q01085; -.
DR BioMuta; TIAL1; -.
DR DMDM; 267131; -.
DR EPD; Q01085; -.
DR jPOST; Q01085; -.
DR MassIVE; Q01085; -.
DR MaxQB; Q01085; -.
DR PaxDb; Q01085; -.
DR PeptideAtlas; Q01085; -.
DR PRIDE; Q01085; -.
DR ProteomicsDB; 57913; -. [Q01085-1]
DR ProteomicsDB; 57914; -. [Q01085-2]
DR Antibodypedia; 18838; 153 antibodies from 29 providers.
DR DNASU; 7073; -.
DR Ensembl; ENST00000369093.6; ENSP00000358089.2; ENSG00000151923.18. [Q01085-2]
DR Ensembl; ENST00000436547.7; ENSP00000394902.2; ENSG00000151923.18. [Q01085-1]
DR GeneID; 7073; -.
DR KEGG; hsa:7073; -.
DR MANE-Select; ENST00000436547.7; ENSP00000394902.2; NM_003252.4; NP_003243.1.
DR UCSC; uc001lei.2; human. [Q01085-1]
DR CTD; 7073; -.
DR DisGeNET; 7073; -.
DR GeneCards; TIAL1; -.
DR HGNC; HGNC:11804; TIAL1.
DR HPA; ENSG00000151923; Low tissue specificity.
DR MIM; 603413; gene.
DR neXtProt; NX_Q01085; -.
DR OpenTargets; ENSG00000151923; -.
DR PharmGKB; PA36513; -.
DR VEuPathDB; HostDB:ENSG00000151923; -.
DR eggNOG; KOG0148; Eukaryota.
DR GeneTree; ENSGT00940000160482; -.
DR HOGENOM; CLU_025000_2_0_1; -.
DR InParanoid; Q01085; -.
DR OMA; TETRFQS; -.
DR PhylomeDB; Q01085; -.
DR TreeFam; TF312915; -.
DR PathwayCommons; Q01085; -.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR SignaLink; Q01085; -.
DR SIGNOR; Q01085; -.
DR BioGRID-ORCS; 7073; 58 hits in 1092 CRISPR screens.
DR ChiTaRS; TIAL1; human.
DR EvolutionaryTrace; Q01085; -.
DR GeneWiki; TIAL1; -.
DR GenomeRNAi; 7073; -.
DR Pharos; Q01085; Tbio.
DR PRO; PR:Q01085; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q01085; protein.
DR Bgee; ENSG00000151923; Expressed in right uterine tube and 206 other tissues.
DR ExpressionAtlas; Q01085; baseline and differential.
DR Genevisible; Q01085; HS.
DR GO; GO:0044194; C:cytolytic granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IEA:Ensembl.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:FlyBase.
DR GO; GO:0140517; F:protein-RNA adaptor activity; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR GO; GO:0007281; P:germ cell development; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:2000637; P:positive regulation of miRNA-mediated gene silencing; IGI:FlyBase.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0017145; P:stem cell division; IEA:Ensembl.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR CDD; cd12616; RRM1_TIAR; 1.
DR CDD; cd12617; RRM2_TIAR; 1.
DR CDD; cd12620; RRM3_TIAR; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR034492; TIAR_RRM1.
DR InterPro; IPR034494; TIAR_RRM2.
DR InterPro; IPR034496; TIAR_RRM3.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SMART; SM00361; RRM_1; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Cytoplasm;
KW Lysosome; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..375
FT /note="Nucleolysin TIAR"
FT /id="PRO_0000081978"
FT DOMAIN 9..85
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 97..175
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 205..277
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 345..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 43
FT /note="E -> EQPDSRRVNSSVGFSVLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043700"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:2CQI"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:2CQI"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:2CQI"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:2CQI"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:2CQI"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2CQI"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:2CQI"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:2DH7"
FT HELIX 110..116
FT /evidence="ECO:0007829|PDB:2DH7"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:2DH7"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:2DH7"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2DH7"
FT STRAND 136..147
FT /evidence="ECO:0007829|PDB:2DH7"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:2DH7"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:2DH7"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2DH7"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:1X4G"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:1X4G"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:1X4G"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:1X4G"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:1X4G"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:1X4G"
FT HELIX 250..260
FT /evidence="ECO:0007829|PDB:1X4G"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:1X4G"
SQ SEQUENCE 375 AA; 41591 MW; 2F8D1C7169A7817E CRC64;
MMEDDGQPRT LYVGNLSRDV TEVLILQLFS QIGPCKSCKM ITEHTSNDPY CFVEFYEHRD
AAAALAAMNG RKILGKEVKV NWATTPSSQK KDTSNHFHVF VGDLSPEITT EDIKSAFAPF
GKISDARVVK DMATGKSKGY GFVSFYNKLD AENAIVHMGG QWLGGRQIRT NWATRKPPAP
KSTQENNTKQ LRFEDVVNQS SPKNCTVYCG GIASGLTDQL MRQTFSPFGQ IMEIRVFPEK
GYSFVRFSTH ESAAHAIVSV NGTTIEGHVV KCYWGKESPD MTKNFQQVDY SQWGQWSQVY
GNPQQYGQYM ANGWQVPPYG VYGQPWNQQG FGVDQSPSAA WMGGFGAQPP QGQAPPPVIP
PPNQAGYGMA SYQTQ
