TSN_HUMAN
ID TSN_HUMAN Reviewed; 228 AA.
AC Q15631; B7Z3X8; Q5U0K7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Translin;
DE EC=3.1.-.-;
DE AltName: Full=Component 3 of promoter of RISC;
DE Short=C3PO;
GN Name=TSN;
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).
RX PubMed=7663511; DOI=10.1038/ng0695-167;
RA Aoki K., Suzuki K., Sugano T., Tasaka T., Nakahara K., Kuge O., Omori A.,
RA Kasai M.;
RT "A novel gene, Translin, encodes a recombination hotspot binding protein
RT associated with chromosomal translocations.";
RL Nat. Genet. 10:167-174(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thalamus;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-215.
RX PubMed=9244443; DOI=10.1006/geno.1997.4796;
RA Aoki K., Inazawa J., Takahashi T., Nakahara K., Kasai M.;
RT "Genomic structure and chromosomal localization of the gene encoding
RT translin, a recombination hotspot binding protein.";
RL Genomics 43:237-241(1997).
RN [7]
RP FUNCTION.
RX PubMed=9111049; DOI=10.1074/jbc.272.17.11402;
RA Kasai M., Matsuzaki T., Katayanagi K., Omori A., Maziarz R.T.,
RA Strominger J.L., Aoki K., Suzuki K.;
RT "The translin ring specifically recognizes DNA ends at recombination hot
RT spots in the human genome.";
RL J. Biol. Chem. 272:11402-11407(1997).
RN [8]
RP DNA/RNA-BINDING REGION.
RX PubMed=10025964; DOI=10.1016/s0014-5793(99)00010-1;
RA Aoki K., Suzuki K., Ishida R., Kasai M.;
RT "The DNA binding activity of Translin is mediated by a basic region in the
RT ring-shaped structure conserved in evolution.";
RL FEBS Lett. 443:363-366(1999).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TSNAX.
RX PubMed=11801738; DOI=10.1242/jcs.115.1.207;
RA Erdemir T., Bilican B., Oncel D., Goding C.R., Yavuzer U.;
RT "DNA damage-dependent interaction of the nuclear matrix protein C1D with
RT Translin-associated factor X (TRAX).";
RL J. Cell Sci. 115:207-216(2002).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-187 AND LYS-199, AND
RP IDENTIFICATION BY MASS 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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
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 [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 X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TSNAX, FUNCTION IN
RP RISC ACTIVATION, AND SUBUNIT.
RX PubMed=21552258; DOI=10.1038/nsmb.2032;
RA Ye X., Huang N., Liu Y., Paroo Z., Huerta C., Li P., Chen S., Liu Q.,
RA Zhang H.;
RT "Structure of C3PO and mechanism of human RISC activation.";
RL Nat. Struct. Mol. Biol. 18:650-657(2011).
CC -!- FUNCTION: DNA-binding protein that specifically recognizes consensus
CC sequences at the breakpoint junctions in chromosomal translocations,
CC mostly involving immunoglobulin (Ig)/T-cell receptor gene segments.
CC Seems to recognize single-stranded DNA ends generated by staggered
CC breaks occurring at recombination hot spots.
CC -!- FUNCTION: Exhibits both single-stranded and double-stranded
CC endoribonuclease activity. May act as an activator of RNA-induced
CC silencing complex (RISC) by facilitating endonucleolytic cleavage of
CC the siRNA passenger strand.
CC -!- SUBUNIT: Ring-shaped heterooctamer of six TSN and two TSNAX subunits,
CC DNA/RNA binding occurs inside the ring. {ECO:0000269|PubMed:21552258}.
CC -!- INTERACTION:
CC Q15631; Q92997: DVL3; NbExp=3; IntAct=EBI-1044160, EBI-739789;
CC Q15631; Q14161: GIT2; NbExp=2; IntAct=EBI-1044160, EBI-1046878;
CC Q15631; Q9H8Y8: GORASP2; NbExp=6; IntAct=EBI-1044160, EBI-739467;
CC Q15631; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-1044160, EBI-739832;
CC Q15631; Q15014: MORF4L2; NbExp=3; IntAct=EBI-1044160, EBI-399257;
CC Q15631; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-1044160, EBI-741158;
CC Q15631; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-1044160, EBI-79165;
CC Q15631; O00560: SDCBP; NbExp=3; IntAct=EBI-1044160, EBI-727004;
CC Q15631; Q15631: TSN; NbExp=4; IntAct=EBI-1044160, EBI-1044160;
CC Q15631; Q99598: TSNAX; NbExp=14; IntAct=EBI-1044160, EBI-742638;
CC Q15631; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-1044160, EBI-10180829;
CC Q15631; P61086: UBE2K; NbExp=3; IntAct=EBI-1044160, EBI-473850;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11801738}. Nucleus
CC {ECO:0000269|PubMed:11801738}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15631-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15631-2; Sequence=VSP_044937, VSP_044938;
CC -!- SIMILARITY: Belongs to the translin family. {ECO:0000305}.
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DR EMBL; X78627; CAA55341.1; -; mRNA.
DR EMBL; BT019490; AAV38297.1; -; mRNA.
DR EMBL; BT019491; AAV38298.1; -; mRNA.
DR EMBL; AK296469; BAH12364.1; -; mRNA.
DR EMBL; AC018737; AAY14831.1; -; Genomic_DNA.
DR EMBL; BC002359; AAH02359.1; -; mRNA.
DR EMBL; Y12563; CAA73150.1; -; Genomic_DNA.
DR EMBL; Y12564; CAA73150.1; JOINED; Genomic_DNA.
DR EMBL; Y12565; CAA73150.1; JOINED; Genomic_DNA.
DR EMBL; Y12566; CAA73150.1; JOINED; Genomic_DNA.
DR EMBL; Y12567; CAA73150.1; JOINED; Genomic_DNA.
DR CCDS; CCDS33284.1; -. [Q15631-1]
DR CCDS; CCDS58723.1; -. [Q15631-2]
DR PIR; S51738; S51738.
DR RefSeq; NP_001248330.1; NM_001261401.1. [Q15631-2]
DR RefSeq; NP_004613.1; NM_004622.2. [Q15631-1]
DR PDB; 1J1J; X-ray; 2.20 A; A/B/C/D=1-228.
DR PDB; 3PJA; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I=1-228.
DR PDB; 3QB5; X-ray; 2.95 A; A/B/C=1-228.
DR PDB; 4WYV; X-ray; 3.00 A; A/B/C/D/E/F/G/H=1-228.
DR PDBsum; 1J1J; -.
DR PDBsum; 3PJA; -.
DR PDBsum; 3QB5; -.
DR PDBsum; 4WYV; -.
DR AlphaFoldDB; Q15631; -.
DR SMR; Q15631; -.
DR BioGRID; 113098; 56.
DR ComplexPortal; CPX-890; C3PO endoribonuclease complex.
DR DIP; DIP-42216N; -.
DR IntAct; Q15631; 22.
DR MINT; Q15631; -.
DR STRING; 9606.ENSP00000374332; -.
DR GlyGen; Q15631; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15631; -.
DR PhosphoSitePlus; Q15631; -.
DR BioMuta; TSN; -.
DR DMDM; 6136060; -.
DR EPD; Q15631; -.
DR jPOST; Q15631; -.
DR MassIVE; Q15631; -.
DR MaxQB; Q15631; -.
DR PaxDb; Q15631; -.
DR PeptideAtlas; Q15631; -.
DR PRIDE; Q15631; -.
DR ProteomicsDB; 60665; -. [Q15631-1]
DR ProteomicsDB; 6554; -.
DR TopDownProteomics; Q15631-1; -. [Q15631-1]
DR Antibodypedia; 33410; 234 antibodies from 34 providers.
DR DNASU; 7247; -.
DR Ensembl; ENST00000389682.8; ENSP00000374332.3; ENSG00000211460.12. [Q15631-1]
DR Ensembl; ENST00000536142.5; ENSP00000437728.1; ENSG00000211460.12. [Q15631-2]
DR GeneID; 7247; -.
DR KEGG; hsa:7247; -.
DR MANE-Select; ENST00000389682.8; ENSP00000374332.3; NM_004622.3; NP_004613.1.
DR UCSC; uc002tnl.4; human. [Q15631-1]
DR CTD; 7247; -.
DR DisGeNET; 7247; -.
DR GeneCards; TSN; -.
DR HGNC; HGNC:12379; TSN.
DR HPA; ENSG00000211460; Low tissue specificity.
DR MIM; 600575; gene.
DR neXtProt; NX_Q15631; -.
DR OpenTargets; ENSG00000211460; -.
DR PharmGKB; PA37047; -.
DR VEuPathDB; HostDB:ENSG00000211460; -.
DR eggNOG; KOG3067; Eukaryota.
DR GeneTree; ENSGT00940000153568; -.
DR HOGENOM; CLU_079179_0_0_1; -.
DR InParanoid; Q15631; -.
DR OMA; LHAGFQI; -.
DR OrthoDB; 1187354at2759; -.
DR PhylomeDB; Q15631; -.
DR TreeFam; TF323690; -.
DR PathwayCommons; Q15631; -.
DR Reactome; R-HSA-426486; Small interfering RNA (siRNA) biogenesis.
DR SignaLink; Q15631; -.
DR BioGRID-ORCS; 7247; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; TSN; human.
DR EvolutionaryTrace; Q15631; -.
DR GeneWiki; TSN_(gene); -.
DR GenomeRNAi; 7247; -.
DR Pharos; Q15631; Tbio.
DR PRO; PR:Q15631; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q15631; protein.
DR Bgee; ENSG00000211460; Expressed in secondary oocyte and 215 other tissues.
DR ExpressionAtlas; Q15631; baseline and differential.
DR Genevisible; Q15631; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:1902555; C:endoribonuclease complex; IPI:ComplexPortal.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
DR GO; GO:0030422; P:siRNA processing; IDA:ComplexPortal.
DR CDD; cd14819; Translin; 1.
DR DisProt; DP02701; -.
DR Gene3D; 1.20.58.190; -; 1.
DR Gene3D; 1.20.58.200; -; 1.
DR InterPro; IPR033956; Translin.
DR InterPro; IPR016069; Translin_C.
DR InterPro; IPR002848; Translin_fam.
DR InterPro; IPR016068; Translin_N.
DR InterPro; IPR036081; Translin_sf.
DR PANTHER; PTHR10741; PTHR10741; 1.
DR PANTHER; PTHR10741:SF2; PTHR10741:SF2; 1.
DR Pfam; PF01997; Translin; 1.
DR SUPFAM; SSF74784; SSF74784; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; DNA-binding;
KW Endonuclease; Hydrolase; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..228
FT /note="Translin"
FT /id="PRO_0000191683"
FT REGION 86..90
FT /note="DNA/RNA binding"
FT REGION 177..198
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255"
FT MOD_RES 187
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 199
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 127..148
FT /note="PDREKGFHLDVEDYLSGVLILA -> AVCQQRDCWRLLPTPPHLHLHQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044937"
FT VAR_SEQ 149..228
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044938"
FT HELIX 3..42
FT /evidence="ECO:0007829|PDB:1J1J"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:1J1J"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:1J1J"
FT HELIX 54..77
FT /evidence="ECO:0007829|PDB:1J1J"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1J1J"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1J1J"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1J1J"
FT HELIX 92..110
FT /evidence="ECO:0007829|PDB:1J1J"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:1J1J"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:1J1J"
FT HELIX 137..160
FT /evidence="ECO:0007829|PDB:1J1J"
FT HELIX 166..181
FT /evidence="ECO:0007829|PDB:1J1J"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:1J1J"
FT HELIX 198..213
FT /evidence="ECO:0007829|PDB:1J1J"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:1J1J"
SQ SEQUENCE 228 AA; 26183 MW; 3CAAF20BED7C4939 CRC64;
MSVSEIFVEL QGFLAAEQDI REEIRKVVQS LEQTAREILT LLQGVHQGAG FQDIPKRCLK
AREHFGTVKT HLTSLKTKFP AEQYYRFHEH WRFVLQRLVF LAAFVVYLET ETLVTREAVT
EILGIEPDRE KGFHLDVEDY LSGVLILASE LSRLSVNSVT AGDYSRPLHI STFINELDSG
FRLLNLKNDS LRKRYDGLKY DVKKVEEVVY DLSIRGFNKE TAAACVEK
