TTC4_HUMAN
ID TTC4_HUMAN Reviewed; 387 AA.
AC O95801; Q53Y95; Q5TA96; Q9H3I2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Tetratricopeptide repeat protein 4;
DE Short=TPR repeat protein 4;
GN Name=TTC4; ORFNames=My044;
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].
RC TISSUE=Brain;
RX PubMed=9933562; DOI=10.1006/geno.1998.5633;
RA Su G., Roberts T., Cowell J.K.;
RT "TTC4, a novel human gene containing the tetratricopeptide repeat and
RT mapping to the region of chromosome 1p31 that is frequently deleted in
RT sporadic breast cancer.";
RL Genomics 55:157-163(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-47.
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Zheng Z.H.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-47.
RC TISSUE=Testis;
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 MRNA], AND VARIANT THR-47.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-47.
RC TISSUE=Cervix;
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 [9]
RP FUNCTION, INTERACTION WITH HSPA8; HSP90AB1 AND CDC6, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF VAL-42; ILE-67; GLU-77; LYS-152; ARG-156 AND ASN-217, AND
RP TISSUE SPECIFICITY.
RX PubMed=18320024; DOI=10.1371/journal.pone.0001737;
RA Crevel G., Bennett D., Cotterill S.;
RT "The human TPR protein TTC4 is a putative Hsp90 co-chaperone which
RT interacts with CDC6 and shows alterations in transformed cells.";
RL PLoS ONE 3:E0001737-E0001737(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND IDENTIFICATION BY
RP 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, AND
RP IDENTIFICATION BY 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 [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TBK1.
RX PubMed=29251827; DOI=10.1002/pmic.201700403;
RA Shang J., Xia T., Han Q.Q., Zhao X., Hu M.M., Shu H.B., Guo L.;
RT "Quantitative Proteomics Identified TTC4 as a TBK1 Interactor and a
RT Positive Regulator of SeV-Induced Innate Immunity.";
RL Proteomics 18:0-0(2018).
CC -!- FUNCTION: May act as a co-chaperone for HSP90AB1 (PubMed:18320024).
CC Promotes Sendai virus (SeV)-induced host cell innate immune responses
CC (PubMed:29251827). {ECO:0000269|PubMed:18320024,
CC ECO:0000269|PubMed:29251827}.
CC -!- SUBUNIT: Interacts (via TPR repeats) with HSP90AB1 (PubMed:18320024).
CC Interacts with HSPA8 and CDC6 (PubMed:18320024). Interacts with TBK1
CC (PubMed:29251827). Interacts with MSL1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8R3H9, ECO:0000269|PubMed:18320024,
CC ECO:0000269|PubMed:29251827}.
CC -!- INTERACTION:
CC O95801; P08238: HSP90AB1; NbExp=5; IntAct=EBI-1050890, EBI-352572;
CC O95801; Q92966: SNAPC3; NbExp=3; IntAct=EBI-1050890, EBI-1760638;
CC O95801; Q9UHD2: TBK1; NbExp=5; IntAct=EBI-1050890, EBI-356402;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18320024,
CC ECO:0000269|PubMed:29251827}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:18320024}. Cytoplasm {ECO:0000269|PubMed:29251827}.
CC Note=Predominantly nuclear in the G1 and S phases of cell cycle and is
CC evenly distributed between the nucleus and cytoplasm in the G2 phase
CC (By similarity). MSL1 can promote its nuclear localization (By
CC similarity). {ECO:0000250|UniProtKB:Q8R3H9}.
CC -!- TISSUE SPECIFICITY: Highly expressed in proliferating tissue and tumor
CC cell lines but not in normal cell lines. {ECO:0000269|PubMed:18320024}.
CC -!- SIMILARITY: Belongs to the TTC4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD19853.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF073887; AAD19853.1; ALT_FRAME; mRNA.
DR EMBL; AF063602; AAG43161.1; -; mRNA.
DR EMBL; AK292426; BAF85115.1; -; mRNA.
DR EMBL; BT006817; AAP35463.1; -; mRNA.
DR EMBL; AK222562; BAD96282.1; -; mRNA.
DR EMBL; AL139244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06671.1; -; Genomic_DNA.
DR EMBL; BC001276; AAH01276.1; -; mRNA.
DR CCDS; CCDS596.1; -.
DR RefSeq; NP_004614.3; NM_004623.4.
DR PDB; 6HFO; X-ray; 1.65 A; A=217-387.
DR PDBsum; 6HFO; -.
DR AlphaFoldDB; O95801; -.
DR SMR; O95801; -.
DR BioGRID; 113119; 94.
DR IntAct; O95801; 34.
DR MINT; O95801; -.
DR STRING; 9606.ENSP00000360329; -.
DR GlyGen; O95801; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95801; -.
DR MetOSite; O95801; -.
DR PhosphoSitePlus; O95801; -.
DR BioMuta; TTC4; -.
DR EPD; O95801; -.
DR jPOST; O95801; -.
DR MassIVE; O95801; -.
DR MaxQB; O95801; -.
DR PaxDb; O95801; -.
DR PeptideAtlas; O95801; -.
DR PRIDE; O95801; -.
DR ProteomicsDB; 51058; -.
DR Antibodypedia; 34867; 78 antibodies from 20 providers.
DR DNASU; 7268; -.
DR Ensembl; ENST00000371281.4; ENSP00000360329.3; ENSG00000243725.7.
DR GeneID; 7268; -.
DR KEGG; hsa:7268; -.
DR MANE-Select; ENST00000371281.4; ENSP00000360329.3; NM_004623.5; NP_004614.3.
DR UCSC; uc001cxx.5; human.
DR CTD; 7268; -.
DR DisGeNET; 7268; -.
DR GeneCards; TTC4; -.
DR HGNC; HGNC:12394; TTC4.
DR HPA; ENSG00000243725; Low tissue specificity.
DR MIM; 606753; gene.
DR neXtProt; NX_O95801; -.
DR OpenTargets; ENSG00000243725; -.
DR PharmGKB; PA37059; -.
DR VEuPathDB; HostDB:ENSG00000243725; -.
DR eggNOG; KOG0551; Eukaryota.
DR GeneTree; ENSGT00510000049371; -.
DR HOGENOM; CLU_040446_2_0_1; -.
DR InParanoid; O95801; -.
DR OMA; HPMFEGL; -.
DR OrthoDB; 866891at2759; -.
DR PhylomeDB; O95801; -.
DR TreeFam; TF314657; -.
DR PathwayCommons; O95801; -.
DR SignaLink; O95801; -.
DR BioGRID-ORCS; 7268; 470 hits in 1081 CRISPR screens.
DR GeneWiki; TTC4; -.
DR GenomeRNAi; 7268; -.
DR Pharos; O95801; Tbio.
DR PRO; PR:O95801; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O95801; protein.
DR Bgee; ENSG00000243725; Expressed in gastrocnemius and 98 other tissues.
DR Genevisible; O95801; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR044059; Csn1/TTC4_wheel.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF18972; Wheel; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antiviral defense; Cytoplasm; Immunity;
KW Innate immunity; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat.
FT CHAIN 1..387
FT /note="Tetratricopeptide repeat protein 4"
FT /id="PRO_0000106379"
FT REPEAT 79..112
FT /note="TPR 1"
FT REPEAT 117..150
FT /note="TPR 2"
FT REPEAT 151..184
FT /note="TPR 3"
FT SITE 77
FT /note="Essential for interaction with CDC6"
FT /evidence="ECO:0000269|PubMed:18320024"
FT SITE 152
FT /note="Essential for interaction with HSPA8"
FT /evidence="ECO:0000269|PubMed:18320024"
FT SITE 156
FT /note="Essential for interaction with HSPA8"
FT /evidence="ECO:0000269|PubMed:18320024"
FT SITE 217
FT /note="Essential for interaction with CDC6"
FT /evidence="ECO:0000269|PubMed:18320024"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 47
FT /note="S -> T (in dbSNP:rs1147990)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4"
FT /id="VAR_031713"
FT MUTAGEN 42
FT /note="V->D: No effect on interaction with HSPA8, HSP90AB1
FT and CDC6."
FT /evidence="ECO:0000269|PubMed:18320024"
FT MUTAGEN 67
FT /note="I->M: No effect on interaction with HSPA8, HSP90AB1
FT and CDC6."
FT /evidence="ECO:0000269|PubMed:18320024"
FT MUTAGEN 77
FT /note="E->A: No effect on interaction with HSPA8 and
FT HSP90AB1. Loss of interaction with CDC6."
FT /evidence="ECO:0000269|PubMed:18320024"
FT MUTAGEN 152
FT /note="K->E: Loss of interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:18320024"
FT MUTAGEN 156
FT /note="R->E: Loss of interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:18320024"
FT MUTAGEN 217
FT /note="N->K: No effect on interaction with HSPA8 and
FT HSP90AB1. Loss of interaction with CDC6."
FT /evidence="ECO:0000269|PubMed:18320024"
FT CONFLICT 165
FT /note="K -> I (in Ref. 1; AAD19853)"
FT /evidence="ECO:0000305"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:6HFO"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:6HFO"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:6HFO"
FT STRAND 274..282
FT /evidence="ECO:0007829|PDB:6HFO"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:6HFO"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:6HFO"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:6HFO"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6HFO"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:6HFO"
FT TURN 332..335
FT /evidence="ECO:0007829|PDB:6HFO"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:6HFO"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:6HFO"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:6HFO"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:6HFO"
FT HELIX 372..377
FT /evidence="ECO:0007829|PDB:6HFO"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:6HFO"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:6HFO"
SQ SEQUENCE 387 AA; 44679 MW; 4FA45889C4C9E427 CRC64;
MEQPGQDPTS DDVMDSFLEK FQSQPYRGGF HEDQWEKEFE KVPLFMSRAP SEIDPRENPD
LACLQSIIFD EERSPEEQAK TYKDEGNDYF KEKDYKKAVI SYTEGLKKKC ADPDLNAVLY
TNRAAAQYYL GNFRSALNDV TAARKLKPCH LKAIIRGALC HLELKHFAEA VNWCDEGLQI
DAKEKKLLEM RAKADKLKRI EQRDVRKANL KEKKERNQNE ALLQAIKARN IRLSEAACED
EDSASEGLGE LFLDGLSTEN PHGARLSLDG QGRLSWPVLF LYPEYAQSDF ISAFHEDSRF
IDHLMVMFGE TPSWDLEQKY CPDNLEVYFE DEDRAELYRV PAKSTLLQVL QHQRYFVKAL
TPAFLVCVGS SPFCKNFLRG RKVYQIR
