TIPRL_HUMAN
ID TIPRL_HUMAN Reviewed; 272 AA.
AC O75663; B2R8V3; Q5HYB2; Q8IZ86;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=TIP41-like protein;
DE AltName: Full=Putative MAPK-activating protein PM10;
DE AltName: Full=Type 2A-interacting protein;
DE Short=TIP;
GN Name=TIPRL;
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] (ISOFORM 1).
RA Rhodes S.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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=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 [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 205-272 (ISOFORM 1).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP INTERACTION WITH PPP2CB; PPP4C AND PPP6C.
RX PubMed=16085932; DOI=10.1074/mcp.m500231-mcp200;
RA Gingras A.-C., Caballero M., Zarske M., Sanchez A., Hazbun T.R., Fields S.,
RA Sonenberg N., Hafen E., Raught B., Aebersold R.;
RT "A novel, evolutionarily conserved protein phosphatase complex involved in
RT cisplatin sensitivity.";
RL Mol. Cell. Proteomics 4:1725-1740(2005).
RN [9]
RP INTERACTION WITH PPP2CA; PPP2CB; PPP4C; PPP6C AND IGBP1, SUBUNIT,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-71; TYR-79; ILE-136; MET-196
RP AND ASP-198.
RX PubMed=17944932; DOI=10.1111/j.1742-4658.2007.06112.x;
RA Smetana J.H., Zanchin N.I.;
RT "Interaction analysis of the heterotrimer formed by the phosphatase 2A
RT catalytic subunit, alpha4 and the mammalian ortholog of yeast Tip41
RT (TIPRL).";
RL FEBS J. 274:5891-5904(2007).
RN [10]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORM 2), AND INTERACTION WITH PPP2CA;
RP PPP4C AND PPP6C.
RX PubMed=17384681; DOI=10.1038/sj.onc.1210406;
RA McConnell J.L., Gomez R.J., McCorvey L.R., Law B.K., Wadzinski B.E.;
RT "Identification of a PP2A-interacting protein that functions as a negative
RT regulator of phosphatase activity in the ATM/ATR signaling pathway.";
RL Oncogene 26:6021-6030(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106, 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 [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-265, 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 [14]
RP INTERACTION WITH PPP4C AND PPP4R2, AND FUNCTION.
RX PubMed=26717153; DOI=10.1371/journal.pone.0145938;
RA Rosales K.R., Reid M.A., Yang Y., Tran T.Q., Wang W.I., Lowman X., Pan M.,
RA Kong M.;
RT "TIPRL inhibits protein phosphatase 4 activity and promotes H2AX
RT phosphorylation in the DNA damage response.";
RL PLoS ONE 10:E0145938-E0145938(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 16-256.
RX PubMed=27489114; DOI=10.1038/srep30813;
RA Scorsato V., Lima T.B., Righetto G.L., Zanchin N.I., Brandao-Neto J.,
RA Sandy J., Pereira H.D., Ferrari A.J., Gozzo F.C., Smetana J.H.,
RA Aparicio R.;
RT "Crystal structure of the human Tip41 orthologue, TIPRL, reveals a novel
RT fold and a binding site for the PP2Ac C-terminus.";
RL Sci. Rep. 6:30813-30813(2016).
CC -!- FUNCTION: May be a allosteric regulator of serine/threonine-protein
CC phosphatase 2A (PP2A). Isoform 1 inhibits catalytic activity of the
CC PP2A(D) core complex in vitro. The PP2A(C):TIPRL complex does not show
CC phosphatase activity. Acts as negative regulator of serine/threonine-
CC protein phosphatase 4 probably by inhibiting the formation of the
CC active PPP4C:PPP4R2 complex; the function is proposed to implicate it
CC in DNA damage response by promoting H2AX phosphorylated on Ser-140
CC (gamma-H2AX). May play a role in the regulation of ATM/ATR signaling
CC pathway controlling DNA replication and repair.
CC {ECO:0000269|PubMed:17384681, ECO:0000269|PubMed:26717153}.
CC -!- SUBUNIT: Isoform 1 interacts with PPP2CA. Isoform 2 does not interact
CC with PPP2CA. Interacts with PPP2CB, PPP4C and PPP6C. Interacts with
CC IGBP1; the interaction is dependent on PPP2CA. Associates with a
CC protein phosphatase 2A PP2A(C):IGBP1 complex. Interacts with PPP4C and
CC PPP4R2. {ECO:0000269|PubMed:16085932, ECO:0000269|PubMed:17384681,
CC ECO:0000269|PubMed:17944932, ECO:0000269|PubMed:26717153}.
CC -!- INTERACTION:
CC O75663; P78318: IGBP1; NbExp=2; IntAct=EBI-1054735, EBI-1055954;
CC O75663; P67775: PPP2CA; NbExp=3; IntAct=EBI-1054735, EBI-712311;
CC O75663; P67775-1: PPP2CA; NbExp=3; IntAct=EBI-1054735, EBI-16765970;
CC O75663; P67775-2: PPP2CA; NbExp=3; IntAct=EBI-1054735, EBI-16766021;
CC O75663; P62714: PPP2CB; NbExp=2; IntAct=EBI-1054735, EBI-1044367;
CC O75663; P60510: PPP4C; NbExp=5; IntAct=EBI-1054735, EBI-1046072;
CC O75663; O00743: PPP6C; NbExp=4; IntAct=EBI-1054735, EBI-359751;
CC O75663; P63331: Ppp2ca; Xeno; NbExp=3; IntAct=EBI-1054735, EBI-7050205;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17944932}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75663-1; Sequence=Displayed;
CC Name=2; Synonyms=TIP_i2;
CC IsoId=O75663-2; Sequence=VSP_027883, VSP_027884;
CC -!- SIMILARITY: Belongs to the TIP41 family. {ECO:0000305}.
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DR EMBL; AL049670; CAB41244.1; -; mRNA.
DR EMBL; AB097034; BAC77387.1; -; mRNA.
DR EMBL; AK313520; BAG36300.1; -; mRNA.
DR EMBL; AL021397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90821.1; -; Genomic_DNA.
DR EMBL; BC009506; AAH09506.1; -; mRNA.
DR EMBL; BX648646; CAI46265.1; -; Transcribed_RNA.
DR CCDS; CCDS1270.1; -. [O75663-1]
DR CCDS; CCDS30935.1; -. [O75663-2]
DR RefSeq; NP_001026970.1; NM_001031800.2. [O75663-2]
DR RefSeq; NP_690866.1; NM_152902.4. [O75663-1]
DR PDB; 5D9G; X-ray; 2.15 A; A/B=16-256.
DR PDBsum; 5D9G; -.
DR AlphaFoldDB; O75663; -.
DR SMR; O75663; -.
DR BioGRID; 129283; 79.
DR IntAct; O75663; 20.
DR MINT; O75663; -.
DR STRING; 9606.ENSP00000356807; -.
DR GlyGen; O75663; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75663; -.
DR PhosphoSitePlus; O75663; -.
DR BioMuta; TIPRL; -.
DR EPD; O75663; -.
DR jPOST; O75663; -.
DR MassIVE; O75663; -.
DR MaxQB; O75663; -.
DR PaxDb; O75663; -.
DR PeptideAtlas; O75663; -.
DR PRIDE; O75663; -.
DR ProteomicsDB; 50143; -. [O75663-1]
DR ProteomicsDB; 50144; -. [O75663-2]
DR Antibodypedia; 34349; 253 antibodies from 32 providers.
DR CPTC; O75663; 1 antibody.
DR DNASU; 261726; -.
DR Ensembl; ENST00000367830.3; ENSP00000356804.3; ENSG00000143155.13. [O75663-2]
DR Ensembl; ENST00000367833.7; ENSP00000356807.2; ENSG00000143155.13. [O75663-1]
DR GeneID; 261726; -.
DR KEGG; hsa:261726; -.
DR MANE-Select; ENST00000367833.7; ENSP00000356807.2; NM_152902.5; NP_690866.1.
DR UCSC; uc001gff.5; human. [O75663-1]
DR CTD; 261726; -.
DR DisGeNET; 261726; -.
DR GeneCards; TIPRL; -.
DR HGNC; HGNC:30231; TIPRL.
DR HPA; ENSG00000143155; Low tissue specificity.
DR MIM; 611807; gene.
DR neXtProt; NX_O75663; -.
DR OpenTargets; ENSG00000143155; -.
DR PharmGKB; PA142670811; -.
DR VEuPathDB; HostDB:ENSG00000143155; -.
DR eggNOG; KOG3224; Eukaryota.
DR GeneTree; ENSGT00390000006659; -.
DR HOGENOM; CLU_039187_2_0_1; -.
DR InParanoid; O75663; -.
DR OMA; GIPIPEM; -.
DR OrthoDB; 1377237at2759; -.
DR PhylomeDB; O75663; -.
DR TreeFam; TF105943; -.
DR PathwayCommons; O75663; -.
DR SignaLink; O75663; -.
DR BioGRID-ORCS; 261726; 263 hits in 1098 CRISPR screens.
DR ChiTaRS; TIPRL; human.
DR GenomeRNAi; 261726; -.
DR Pharos; O75663; Tbio.
DR PRO; PR:O75663; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75663; protein.
DR Bgee; ENSG00000143155; Expressed in cauda epididymis and 212 other tissues.
DR Genevisible; O75663; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR InterPro; IPR007303; TIP41-like.
DR PANTHER; PTHR21021:SF16; PTHR21021:SF16; 1.
DR Pfam; PF04176; TIP41; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..272
FT /note="TIP41-like protein"
FT /id="PRO_0000301853"
FT REGION 173..272
FT /note="Interaction with PPP2CA"
FT MOD_RES 106
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 173..178
FT /note="RVMPSS -> PGGGHL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027883"
FT VAR_SEQ 179..272
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027884"
FT MUTAGEN 71
FT /note="D->L: Abolishes interaction with PPP2CA, PPP2CB and
FT PPP4C."
FT /evidence="ECO:0000269|PubMed:17944932"
FT MUTAGEN 79
FT /note="Y->H: Diminishes interaction with PPP2CA."
FT /evidence="ECO:0000269|PubMed:17944932"
FT MUTAGEN 136
FT /note="I->T: Abolishes interaction with PPP2CA, PPP2CB and
FT PPP4C."
FT /evidence="ECO:0000269|PubMed:17944932"
FT MUTAGEN 196
FT /note="M->V: Abolishes interaction with PPP2CA, PPP2CB and
FT PPP4C."
FT /evidence="ECO:0000269|PubMed:17944932"
FT MUTAGEN 198
FT /note="D->N: Abolishes interaction with PPP2CA, PPP2CB and
FT PPP4C."
FT /evidence="ECO:0000269|PubMed:17944932"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:5D9G"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:5D9G"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:5D9G"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:5D9G"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5D9G"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:5D9G"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:5D9G"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5D9G"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:5D9G"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:5D9G"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:5D9G"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:5D9G"
FT STRAND 164..175
FT /evidence="ECO:0007829|PDB:5D9G"
FT STRAND 178..189
FT /evidence="ECO:0007829|PDB:5D9G"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5D9G"
FT STRAND 193..206
FT /evidence="ECO:0007829|PDB:5D9G"
FT STRAND 208..220
FT /evidence="ECO:0007829|PDB:5D9G"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:5D9G"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:5D9G"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:5D9G"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:5D9G"
FT STRAND 244..253
FT /evidence="ECO:0007829|PDB:5D9G"
SQ SEQUENCE 272 AA; 31444 MW; 23B730E0BC27DCEA CRC64;
MMIHGFQSSH RDFCFGPWKL TASKTHIMKS ADVEKLADEL HMPSLPEMMF GDNVLRIQHG
SGFGIEFNAT DALRCVNNYQ GMLKVACAEE WQESRTEGEH SKEVIKPYDW TYTTDYKGTL
LGESLKLKVV PTTDHIDTEK LKAREQIKFF EEVLLFEDEL HDHGVSSLSV KIRVMPSSFF
LLLRFFLRID GVLIRMNDTR LYHEADKTYM LREYTSRESK ISSLMHVPPS LFTEPNEISQ
YLPIKEAVCE KLIFPERIDP NPADSQKSTQ VE
