DS13A_HUMAN
ID DS13A_HUMAN Reviewed; 188 AA.
AC Q6B8I1; Q96J67;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Dual specificity protein phosphatase 13 isoform A;
DE Short=DUSP13A;
DE EC=3.1.3.16;
DE EC=3.1.3.48 {ECO:0000305|PubMed:15252030, ECO:0000305|PubMed:29106959};
DE AltName: Full=Branching-enzyme interacting DSP;
DE AltName: Full=Muscle-restricted DSP;
DE Short=MDSP;
GN Name=DUSP13; Synonyms=BEDP, DUSP13A, MDSP;
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 5), ALTERNATIVE SPLICING, CATALYTIC
RP ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP ALTERNATIVE PROMOTER USAGE, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=15252030; DOI=10.1074/jbc.m405286200;
RA Chen H.-H., Luche R., Wei B., Tonks N.K.;
RT "Characterization of two distinct dual specificity phosphatases encoded in
RT alternative open reading frames of a single gene located on human
RT chromosome 10q22.2.";
RL J. Biol. Chem. 279:41404-41413(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND VARIANT ARG-73.
RC TISSUE=Skeletal muscle;
RA Skurat A.V., Dietrich A.D.;
RT "Identification of novel dual-specificity protein phosphatase which
RT interacts with glycogen-branching enzyme.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 6; 7 AND 8).
RC TISSUE=Skeletal muscle;
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].
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 [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow;
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 FUNCTION IN APOPTOSIS, INTERACTION WITH MAP3K5, AND MUTAGENESIS OF ASP-97
RP AND CYS-129.
RX PubMed=20358250; DOI=10.1007/s00018-010-0353-3;
RA Park J.E., Park B.C., Kim H.A., Song M., Park S.G., Lee D.H., Kim H.J.,
RA Choi H.K., Kim J.T., Cho S.;
RT "Positive regulation of apoptosis signal-regulating kinase 1 by dual-
RT specificity phosphatase 13A.";
RL Cell. Mol. Life Sci. 67:2619-2629(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 1-185 IN COMPLEX WITH PHOSPHATE,
RP CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF CYS-129.
RX PubMed=29106959; DOI=10.1016/j.phrs.2017.10.006;
RA Wei C.H., Min H.G., Kim M., Kim G.H., Chun H.J., Ryu S.E.;
RT "Two intermediate states of the conformational switch in dual specificity
RT phosphatase 13a.";
RL Pharmacol. Res. 128:211-219(2018).
CC -!- FUNCTION: Probable protein tyrosine phosphatase. Has phosphatase
CC activity with synthetic substrates (PubMed:15252030, PubMed:29106959).
CC Has a phosphatase activity-independent regulatory role in MAP3K5/ASK1-
CC mediated apoptosis, preventing MAP3K5/ASK1 inhibition by AKT1. Shows no
CC phosphatase activity on MAPK1/ERK2, MAPK8/JNK, MAPK14/p38 and
CC MAP3K5/ASK1. {ECO:0000269|PubMed:15252030, ECO:0000269|PubMed:20358250,
CC ECO:0000269|PubMed:29106959}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000305|PubMed:15252030,
CC ECO:0000305|PubMed:29106959};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- ACTIVITY REGULATION: Inhibited by vanadate.
CC {ECO:0000269|PubMed:15252030}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.5 mM for p-nitrophenol phosphate (at pH 6.0)
CC {ECO:0000269|PubMed:15252030};
CC -!- SUBUNIT: Monomer (PubMed:29106959). Interacts with MAP3K5/ASK1; may
CC compete with AKT1 preventing MAP3K5/ASK1 phosphorylation by AKT1.
CC {ECO:0000269|PubMed:20358250, ECO:0000269|PubMed:29106959}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15252030}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=5;
CC IsoId=Q6B8I1-1; Sequence=Displayed;
CC Name=1; Synonyms=TMDP;
CC IsoId=Q9UII6-1; Sequence=External;
CC Name=2;
CC IsoId=Q6B8I1-5; Sequence=VSP_047819;
CC Name=4; Synonyms=TMDP-L2;
CC IsoId=Q9UII6-4; Sequence=External;
CC Name=6;
CC IsoId=Q6B8I1-2; Sequence=VSP_046446, VSP_046447;
CC Name=7;
CC IsoId=Q6B8I1-3; Sequence=VSP_046445, VSP_046448;
CC Name=8;
CC IsoId=Q6B8I1-4; Sequence=VSP_046449;
CC -!- TISSUE SPECIFICITY: Skeletal muscle specific.
CC {ECO:0000269|PubMed:15252030}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative promoter usage and
CC alternative splicing. May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative promoter usage and
CC alternative splicing. May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: Produced by alternative promoter usage and
CC alternative splicing. May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 8]: Produced by alternative promoter usage and
CC alternative splicing. May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH09778.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAF84580.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAF84586.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAG51843.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAG54592.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAG62362.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG62362.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AY674051; AAT79356.1; -; mRNA.
DR EMBL; AY040091; AAK77966.1; -; mRNA.
DR EMBL; AK057012; BAG51843.1; ALT_SEQ; mRNA.
DR EMBL; AK127886; BAG54592.1; ALT_SEQ; mRNA.
DR EMBL; AK291891; BAF84580.1; ALT_SEQ; mRNA.
DR EMBL; AK291897; BAF84586.1; ALT_SEQ; mRNA.
DR EMBL; AK300679; BAG62362.1; ALT_SEQ; mRNA.
DR EMBL; CH471083; EAW54564.1; -; Genomic_DNA.
DR EMBL; BC009778; AAH09778.1; ALT_SEQ; mRNA.
DR CCDS; CCDS53542.1; -. [Q6B8I1-1]
DR RefSeq; NP_001007272.1; NM_001007271.1. [Q6B8I1-1]
DR RefSeq; NP_001007273.1; NM_001007272.1.
DR RefSeq; NP_001007274.1; NM_001007273.1.
DR RefSeq; NP_001307771.1; NM_001320842.1.
DR RefSeq; NP_001307772.1; NM_001320843.1.
DR PDB; 5XJV; X-ray; 1.69 A; A/B=1-185.
DR PDBsum; 5XJV; -.
DR AlphaFoldDB; Q6B8I1; -.
DR SMR; Q6B8I1; -.
DR BioGRID; 119380; 103.
DR IntAct; Q6B8I1; 1.
DR DEPOD; DUSP13; -.
DR BioMuta; DUSP13; -.
DR DMDM; 74748394; -.
DR MassIVE; Q6B8I1; -.
DR PeptideAtlas; Q6B8I1; -.
DR PRIDE; Q6B8I1; -.
DR ProteomicsDB; 66209; -. [Q6B8I1-1]
DR Antibodypedia; 15503; 269 antibodies from 27 providers.
DR DNASU; 51207; -.
DR Ensembl; ENST00000308475.10; ENSP00000311051.6; ENSG00000079393.21. [Q6B8I1-5]
DR Ensembl; ENST00000372702.7; ENSP00000361787.2; ENSG00000079393.21. [Q6B8I1-1]
DR Ensembl; ENST00000394707.7; ENSP00000452702.2; ENSG00000079393.21. [Q6B8I1-2]
DR Ensembl; ENST00000479884.6; ENSP00000474298.1; ENSG00000079393.21. [Q6B8I1-4]
DR Ensembl; ENST00000494588.2; ENSP00000474689.1; ENSG00000079393.21. [Q6B8I1-3]
DR GeneID; 51207; -.
DR KEGG; hsa:51207; -.
DR UCSC; uc001jws.4; human. [Q6B8I1-1]
DR CTD; 51207; -.
DR DisGeNET; 51207; -.
DR GeneCards; DUSP13; -.
DR HGNC; HGNC:19681; DUSP13.
DR HPA; ENSG00000079393; Tissue enhanced (skeletal muscle, testis, tongue).
DR MIM; 613191; gene.
DR neXtProt; NX_Q6B8I1; -.
DR OpenTargets; ENSG00000079393; -.
DR PharmGKB; PA134939640; -.
DR VEuPathDB; HostDB:ENSG00000079393; -.
DR GeneTree; ENSGT00940000154628; -.
DR HOGENOM; CLU_027074_11_3_1; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q6B8I1; -.
DR PathwayCommons; Q6B8I1; -.
DR SABIO-RK; Q6B8I1; -.
DR SignaLink; Q6B8I1; -.
DR BioGRID-ORCS; 51207; 13 hits in 1080 CRISPR screens.
DR ChiTaRS; DUSP13; human.
DR GeneWiki; DUSP13; -.
DR GenomeRNAi; 51207; -.
DR Pharos; Q6B8I1; Tbio.
DR Proteomes; UP000005640; Chromosome 10.
DR Bgee; ENSG00000079393; Expressed in hindlimb stylopod muscle and 125 other tissues.
DR ExpressionAtlas; Q6B8I1; baseline and differential.
DR Genevisible; Q6B8I1; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020405; Atypical_DUSP_subfamA.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45682; PTHR45682; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01909; ADSPHPHTASEA.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing; Cytoplasm;
KW Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..188
FT /note="Dual specificity protein phosphatase 13 isoform A"
FT /id="PRO_0000381973"
FT DOMAIN 37..184
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 129
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000269|PubMed:29106959"
FT VAR_SEQ 51..188
FT /note="ATANNRFELWKLGITHVLNAAHKGLYCQGGPDFYGSSVSYLGVPAHDLPDFD
FT ISAYFSSAADFIHRALNTPGAKVLVHCVVGVSRSATLVLAYLMLHQRLSLRQAVITVRQ
FT HRWVFPNRGFLHQLCRLDQQLRGAGQS -> NSIKCAETGG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047819"
FT VAR_SEQ 51..92
FT /note="ATANNRFELWKLGITHVLNAAHKGLYCQGGPDFYGSSVSYLG -> RGPGTA
FT SLLVPWLGRHQVPFLPSPGPRQTTALSCGSWASPTC (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046445"
FT VAR_SEQ 52..67
FT /note="TANNRFELWKLGITHV -> GPYSLPWGSATLPPWH (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046446"
FT VAR_SEQ 68..188
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046447"
FT VAR_SEQ 93..188
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046448"
FT VAR_SEQ 123..188
FT /note="AKVLVHCVVGVSRSATLVLAYLMLHQRLSLRQAVITVRQHRWVFPNRGFLHQ
FT LCRLDQQLRGAGQS -> ELVLTPCHGALPLCHPGTDPAGAAGGSGPGGHTEDGGSPAW
FT GRP (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046449"
FT VARIANT 73
FT /note="K -> R (in dbSNP:rs7912300)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_058495"
FT MUTAGEN 97
FT /note="D->A: No effect on interaction with MAP3K5."
FT /evidence="ECO:0000269|PubMed:20358250"
FT MUTAGEN 129
FT /note="C->S: Loss of enzyme activity. No effect on
FT interaction with MAP3K5."
FT /evidence="ECO:0000269|PubMed:20358250,
FT ECO:0000269|PubMed:29106959"
FT CONFLICT 20
FT /note="S -> G (in Ref. 5; AAH09778)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="F -> S (in Ref. 3; BAG62362)"
FT /evidence="ECO:0000305"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:5XJV"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:5XJV"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:5XJV"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:5XJV"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:5XJV"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:5XJV"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5XJV"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:5XJV"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:5XJV"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:5XJV"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:5XJV"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:5XJV"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:5XJV"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:5XJV"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:5XJV"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:5XJV"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:5XJV"
SQ SEQUENCE 188 AA; 20658 MW; 88E604BD26E70EE5 CRC64;
MAETSLPELG GEDKATPCPS ILELEELLRA GKSSCSRVDE VWPNLFIGDA ATANNRFELW
KLGITHVLNA AHKGLYCQGG PDFYGSSVSY LGVPAHDLPD FDISAYFSSA ADFIHRALNT
PGAKVLVHCV VGVSRSATLV LAYLMLHQRL SLRQAVITVR QHRWVFPNRG FLHQLCRLDQ
QLRGAGQS
