TDRD1_HUMAN
ID TDRD1_HUMAN Reviewed; 1180 AA.
AC Q9BXT4; A6NEN3; A6NMN2; B3KVI4; B4E2L5; D3DRC2; Q4G0Y8; Q6P518; Q9H7B3;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Tudor domain-containing protein 1;
DE AltName: Full=Cancer/testis antigen 41.1;
DE Short=CT41.1;
GN Name=TDRD1;
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 [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 444-1177 (ISOFORM 1).
RC TISSUE=Testis, and Trachea;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1176 (ISOFORM 1).
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 308-1180 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11279525; DOI=10.1038/86927;
RA Wang P.J., McCarrey J.R., Yang F., Page D.C.;
RT "An abundance of X-linked genes expressed in spermatogonia.";
RL Nat. Genet. 27:422-426(2001).
RN [6]
RP TISSUE SPECIFICITY, AND IDENTIFICATION AS A CANCER/TESTIS ANTIGEN.
RX PubMed=12704671; DOI=10.1002/ijc.11104;
RA Loriot A., Boon T., De Smet C.;
RT "Five new human cancer-germline genes identified among 12 genes expressed
RT in spermatogonia.";
RL Int. J. Cancer 105:371-376(2003).
CC -!- FUNCTION: Plays a central role during spermatogenesis by participating
CC in the repression transposable elements and preventing their
CC mobilization, which is essential for the germline integrity. Acts via
CC the piRNA metabolic process, which mediates the repression of
CC transposable elements during meiosis by forming complexes composed of
CC piRNAs and Piwi proteins and governs the methylation and subsequent
CC repression of transposons. Required for the localization of Piwi
CC proteins to the meiotic nuage. Involved in the piRNA metabolic process
CC by ensuring the entry of correct transcripts into the normal piRNA pool
CC and limiting the entry of cellular transcripts into the piRNA pathway.
CC May act by allowing the recruitment of piRNA biogenesis or loading
CC factors that ensure the correct entry of transcripts and piRNAs into
CC Piwi proteins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a mRNP complex, at least composed of TDRD1, TDRD6,
CC TDRD7 and DDX4. Interacts with MAEL. Interacts with PIWIL1, PIWIL2 and
CC PIWIL4 (when methylated on arginine residues). Interacts with TDRD12
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BXT4-2; Q12800: TFCP2; NbExp=3; IntAct=EBI-10301451, EBI-717422;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Component of the
CC meiotic nuage, also named P granule, a germ-cell-specific organelle
CC required to repress transposon activity during meiosis. Also present in
CC chromatoid body (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BXT4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BXT4-2; Sequence=VSP_035481, VSP_035482;
CC Name=3;
CC IsoId=Q9BXT4-3; Sequence=VSP_036670;
CC Name=4;
CC IsoId=Q9BXT4-4; Sequence=VSP_036667, VSP_036668, VSP_035481,
CC VSP_036669;
CC -!- TISSUE SPECIFICITY: Testis and ovary specific. Also expressed in
CC several cancers. {ECO:0000269|PubMed:12704671}.
CC -!- DOMAIN: Tudor domains 2 and 3 have higher affinity for arginine-
CC methylated peptides, tudor domain 1 is a poor binder due to an impaired
CC aromatic cage. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TDRD1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35010.1; Type=Miscellaneous discrepancy; Note=Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAK31985.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK31985.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence.; Evidence={ECO:0000305};
CC Sequence=BAB14982.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14982.1; Type=Miscellaneous discrepancy; Note=Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AC022023; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122916; BAG53796.1; -; mRNA.
DR EMBL; AK304331; BAG65177.1; -; mRNA.
DR EMBL; CH471066; EAW49479.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49480.1; -; Genomic_DNA.
DR EMBL; BC035010; AAH35010.1; ALT_SEQ; mRNA.
DR EMBL; BC063133; AAH63133.1; -; mRNA.
DR EMBL; AF285606; AAK31985.1; ALT_SEQ; mRNA.
DR EMBL; AK024735; BAB14982.1; ALT_SEQ; mRNA.
DR CCDS; CCDS7588.1; -. [Q9BXT4-3]
DR RefSeq; NP_942090.1; NM_198795.1. [Q9BXT4-3]
DR RefSeq; XP_005270035.1; XM_005269978.2. [Q9BXT4-3]
DR RefSeq; XP_011538261.1; XM_011539959.2. [Q9BXT4-3]
DR RefSeq; XP_011538262.1; XM_011539960.2. [Q9BXT4-3]
DR RefSeq; XP_011538263.1; XM_011539961.2. [Q9BXT4-3]
DR RefSeq; XP_011538264.1; XM_011539962.1. [Q9BXT4-3]
DR RefSeq; XP_011538265.1; XM_011539963.1. [Q9BXT4-1]
DR PDB; 5M9N; X-ray; 1.95 A; A/B=460-679.
DR PDBsum; 5M9N; -.
DR AlphaFoldDB; Q9BXT4; -.
DR SMR; Q9BXT4; -.
DR BioGRID; 121098; 6.
DR IntAct; Q9BXT4; 4.
DR MINT; Q9BXT4; -.
DR STRING; 9606.ENSP00000251864; -.
DR GlyGen; Q9BXT4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BXT4; -.
DR PhosphoSitePlus; Q9BXT4; -.
DR BioMuta; TDRD1; -.
DR DMDM; 206729901; -.
DR EPD; Q9BXT4; -.
DR jPOST; Q9BXT4; -.
DR MassIVE; Q9BXT4; -.
DR MaxQB; Q9BXT4; -.
DR PaxDb; Q9BXT4; -.
DR PeptideAtlas; Q9BXT4; -.
DR PRIDE; Q9BXT4; -.
DR ProteomicsDB; 79503; -. [Q9BXT4-1]
DR ProteomicsDB; 79504; -. [Q9BXT4-2]
DR ProteomicsDB; 79505; -. [Q9BXT4-3]
DR ProteomicsDB; 79506; -. [Q9BXT4-4]
DR Antibodypedia; 31923; 137 antibodies from 24 providers.
DR DNASU; 56165; -.
DR Ensembl; ENST00000251864.6; ENSP00000251864.2; ENSG00000095627.9. [Q9BXT4-3]
DR GeneID; 56165; -.
DR KEGG; hsa:56165; -.
DR UCSC; uc001lbg.1; human. [Q9BXT4-1]
DR CTD; 56165; -.
DR DisGeNET; 56165; -.
DR GeneCards; TDRD1; -.
DR HGNC; HGNC:11712; TDRD1.
DR HPA; ENSG00000095627; Tissue enriched (testis).
DR MIM; 605796; gene.
DR neXtProt; NX_Q9BXT4; -.
DR OpenTargets; ENSG00000095627; -.
DR PharmGKB; PA36430; -.
DR VEuPathDB; HostDB:ENSG00000095627; -.
DR eggNOG; KOG2039; Eukaryota.
DR GeneTree; ENSGT00940000158754; -.
DR InParanoid; Q9BXT4; -.
DR OMA; EYCSAQK; -.
DR PhylomeDB; Q9BXT4; -.
DR TreeFam; TF343710; -.
DR PathwayCommons; Q9BXT4; -.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR SignaLink; Q9BXT4; -.
DR SIGNOR; Q9BXT4; -.
DR BioGRID-ORCS; 56165; 10 hits in 1036 CRISPR screens.
DR ChiTaRS; TDRD1; human.
DR GenomeRNAi; 56165; -.
DR Pharos; Q9BXT4; Tbio.
DR PRO; PR:Q9BXT4; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9BXT4; protein.
DR Bgee; ENSG00000095627; Expressed in secondary oocyte and 75 other tissues.
DR ExpressionAtlas; Q9BXT4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0043186; C:P granule; ISS:UniProtKB.
DR GO; GO:0071546; C:pi-body; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043046; P:DNA methylation involved in gamete generation; ISS:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; ISS:UniProtKB.
DR GO; GO:0007281; P:germ cell development; ISS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030719; P:P granule organization; IBA:GO_Central.
DR GO; GO:0034587; P:piRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR CDD; cd04508; TUDOR; 4.
DR Gene3D; 2.40.50.90; -; 5.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF00567; TUDOR; 4.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00333; TUDOR; 4.
DR PROSITE; PS50304; TUDOR; 4.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW Differentiation; Meiosis; Metal-binding; Reference proteome; Repeat;
KW RNA-mediated gene silencing; Spermatogenesis; Zinc; Zinc-finger.
FT CHAIN 1..1180
FT /note="Tudor domain-containing protein 1"
FT /id="PRO_0000183161"
FT DOMAIN 312..372
FT /note="Tudor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 541..600
FT /note="Tudor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 762..821
FT /note="Tudor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT DOMAIN 990..1048
FT /note="Tudor 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT ZN_FING 170..206
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT VAR_SEQ 1..291
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036667"
FT VAR_SEQ 328..375
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036668"
FT VAR_SEQ 554..610
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035481"
FT VAR_SEQ 775..831
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035482"
FT VAR_SEQ 1059..1134
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036669"
FT VAR_SEQ 1180
FT /note="S -> KTASLGGKPL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036670"
FT VARIANT 864
FT /note="V -> L (in dbSNP:rs7914059)"
FT /id="VAR_057321"
FT VARIANT 1138
FT /note="Y -> C (in dbSNP:rs34112549)"
FT /id="VAR_057322"
FT CONFLICT 251
FT /note="M -> T (in Ref. 1; BAG53796)"
FT /evidence="ECO:0000305"
FT CONFLICT 1140
FT /note="M -> T (in Ref. 5; AAK31985)"
FT /evidence="ECO:0000305"
FT CONFLICT 1178
FT /note="L -> V (in Ref. 5; AAK31985)"
FT /evidence="ECO:0000305"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:5M9N"
FT STRAND 495..505
FT /evidence="ECO:0007829|PDB:5M9N"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:5M9N"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:5M9N"
FT HELIX 517..532
FT /evidence="ECO:0007829|PDB:5M9N"
FT STRAND 547..551
FT /evidence="ECO:0007829|PDB:5M9N"
FT TURN 553..555
FT /evidence="ECO:0007829|PDB:5M9N"
FT STRAND 558..568
FT /evidence="ECO:0007829|PDB:5M9N"
FT STRAND 571..576
FT /evidence="ECO:0007829|PDB:5M9N"
FT TURN 577..579
FT /evidence="ECO:0007829|PDB:5M9N"
FT STRAND 582..586
FT /evidence="ECO:0007829|PDB:5M9N"
FT HELIX 587..589
FT /evidence="ECO:0007829|PDB:5M9N"
FT HELIX 595..598
FT /evidence="ECO:0007829|PDB:5M9N"
FT STRAND 605..609
FT /evidence="ECO:0007829|PDB:5M9N"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:5M9N"
FT HELIX 621..631
FT /evidence="ECO:0007829|PDB:5M9N"
FT STRAND 636..643
FT /evidence="ECO:0007829|PDB:5M9N"
FT STRAND 645..654
FT /evidence="ECO:0007829|PDB:5M9N"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:5M9N"
FT HELIX 663..669
FT /evidence="ECO:0007829|PDB:5M9N"
FT STRAND 671..675
FT /evidence="ECO:0007829|PDB:5M9N"
SQ SEQUENCE 1180 AA; 132024 MW; 9B024C7D94F1D7E1 CRC64;
MSVKSPFNVM SRNNLEAPPC KMTEPFNFEK NENKLPPHES LRSPGTLPNH PNFRLKSSEN
GNKKNNFLLC EQTKQYLASQ EDNSVSSNPN GINGEVVGSK GDRKKLPAGN SVSPPSAESN
SPPKEVNIKP GNNVRPAKSK KLNKLVENSL SISNPGLFTS LGPPLRSTTC HRCGLFGSLR
CSQCKQTYYC STACQRRDWS AHSIVCRPVQ PNFHKLENKS SIETKDVEVN NKSDCPLGVT
KEIAIWAERI MFSDLRSLQL KKTMEIKGTV TEFKHPGDFY VQLYSSEVLE YMNQLSASLK
ETYANVHEKD YIPVKGEVCI AKYTVDQTWN RAIIQNVDVQ QKKAHVLYID YGNEEIIPLN
RIYHLNRNID LFPPCAIKCF VANVIPAEGN WSSDCIKATK PLLMEQYCSI KIVDILEEEV
VTFAVEVELP NSGKLLDHVL IEMGYGLKPS GQDSKKENAD QSDPEDVGKM TTENNIVVDK
SDLIPKVLTL NVGDEFCGVV AHIQTPEDFF CQQLQSGRKL AELQASLSKY CDQLPPRSDF
YPAIGDICCA QFSEDDQWYR ASVLAYASEE SVLVGYVDYG NFEILSLMRL CPIIPKLLEL
PMQAIKCVLA GVKPSLGIWT PEAICLMKKL VQNKIITVKV VDKLENSSLV ELIDKSETPH
VSVSKVLLDA GFAVGEQSMV TDKPSDVKET SVPLGVEGKV NPLEWTWVEL GVDQTVDVVV
CVIYSPGEFY CHVLKEDALK KLNDLNKSLA EHCQQKLPNG FKAEIGQPCC AFFAGDGSWY
RALVKEILPN GHVKVHFVDY GNIEEVTADE LRMISSTFLN LPFQGIRCQL ADIQSRNKHW
SEEAITRFQM CVAGIKLQAR VVEVTENGIG VELTDLSTCY PRIISDVLID EHLVLKSASP
HKDLPNDRLV NKHELQVHVQ GLQATSSAEQ WKTIELPVDK TIQANVLEII SPNLFYALPK
GMPENQEKLC MLTAELLEYC NAPKSRPPYR PRIGDACCAK YTSDDFWYRA VVLGTSDTDV
EVLYADYGNI ETLPLCRVQP ITSSHLALPF QIIRCSLEGL MELNGSSSQL IIMLLKNFML
NQNVMLSVKG ITKNVHTVSV EKCSENGTVD VADKLVTFGL AKNITPQRQS ALNTEKMYRM
NCCCTELQKQ VEKHEHILLF LLNNSTNQNK FIEMKKLLKS
