DUS6_HUMAN
ID DUS6_HUMAN Reviewed; 381 AA.
AC Q16828; O75109; Q53Y75; Q9BSH6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Dual specificity protein phosphatase 6;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=Dual specificity protein phosphatase PYST1;
DE AltName: Full=Mitogen-activated protein kinase phosphatase 3;
DE Short=MAP kinase phosphatase 3;
DE Short=MKP-3;
GN Name=DUSP6; Synonyms=MKP3, PYST1;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP VARIANT LEU-114.
RC TISSUE=Foreskin;
RX PubMed=8670865; DOI=10.1002/j.1460-2075.1996.tb00731.x;
RA Groom L.A., Sneddon A.A., Alessi D.R., Dowd S., Keyse S.M.;
RT "Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a
RT novel cytosolic dual-specificity phosphatase.";
RL EMBO J. 15:3621-3632(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP LEU-114.
RC TISSUE=Liver;
RX PubMed=9858808; DOI=10.1159/000015091;
RA Furukawa T., Yatsuoka T., Youssef E.M., Abe T., Yokoyama T., Fukushige S.,
RA Soeda E., Hoshi M., Hayashi Y., Sunamura M., Kobari M., Horii A.;
RT "Genomic analysis of DUSP6, a dual specificity MAP kinase phosphatase, in
RT pancreatic cancer.";
RL Cytogenet. Cell Genet. 82:156-159(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-114.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, Kidney, Skin, and Stomach;
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 X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 204-347, AND ACTIVE SITE.
RX PubMed=10048930; DOI=10.1038/5861;
RA Stewart A.E., Dowd S., Keyse S.M., McDonald N.Q.;
RT "Crystal structure of the MAPK phosphatase Pyst1 catalytic domain and
RT implications for regulated activation.";
RL Nat. Struct. Biol. 6:174-181(1999).
RN [6]
RP VARIANTS HH19 ILE-77; PHE-182; SER-189 AND MET-346.
RX PubMed=23643382; DOI=10.1016/j.ajhg.2013.04.008;
RA Miraoui H., Dwyer A.A., Sykiotis G.P., Plummer L., Chung W., Feng B.,
RA Beenken A., Clarke J., Pers T.H., Dworzynski P., Keefe K., Niedziela M.,
RA Raivio T., Crowley W.F. Jr., Seminara S.B., Quinton R., Hughes V.A.,
RA Kumanov P., Young J., Yialamas M.A., Hall J.E., Van Vliet G.,
RA Chanoine J.P., Rubenstein J., Mohammadi M., Tsai P.S., Sidis Y., Lage K.,
RA Pitteloud N.;
RT "Mutations in FGF17, IL17RD, DUSP6, SPRY4, and FLRT3 are identified in
RT individuals with congenital hypogonadotropic hypogonadism.";
RL Am. J. Hum. Genet. 92:725-743(2013).
RN [7]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=29043977; DOI=10.7554/elife.27356;
RA Mishra A., Oules B., Pisco A.O., Ly T., Liakath-Ali K., Walko G.,
RA Viswanathan P., Tihy M., Nijjher J., Dunn S.J., Lamond A.I., Watt F.M.;
RT "A protein phosphatase network controls the temporal and spatial dynamics
RT of differentiation commitment in human epidermis.";
RL Elife 6:0-0(2017).
RN [8]
RP INTERACTION WITH MAPK1.
RX PubMed=32721402; DOI=10.1016/j.ajhg.2020.06.018;
RA Motta M., Pannone L., Pantaleoni F., Bocchinfuso G., Radio F.C.,
RA Cecchetti S., Ciolfi A., Di Rocco M., Elting M.W., Brilstra E.H., Boni S.,
RA Mazzanti L., Tamburrino F., Walsh L., Payne K., Fernandez-Jaen A.,
RA Ganapathi M., Chung W.K., Grange D.K., Dave-Wala A., Reshmi S.C.,
RA Bartholomew D.W., Mouhlas D., Carpentieri G., Bruselles A., Pizzi S.,
RA Bellacchio E., Piceci-Sparascio F., Lissewski C., Brinkmann J.,
RA Waclaw R.R., Waisfisz Q., van Gassen K., Wentzensen I.M., Morrow M.M.,
RA Alvarez S., Martinez-Garcia M., De Luca A., Memo L., Zampino G., Rossi C.,
RA Seri M., Gelb B.D., Zenker M., Dallapiccola B., Stella L., Prada C.E.,
RA Martinelli S., Flex E., Tartaglia M.;
RT "Enhanced MAPK1 function causes a neurodevelopmental disorder within the
RT RASopathy clinical spectrum.";
RL Am. J. Hum. Genet. 107:499-513(2020).
CC -!- FUNCTION: Inactivates MAP kinases. Has a specificity for the ERK family
CC (PubMed:9858808). Plays an important role in alleviating chronic
CC postoperative pain. Necessary for the normal dephosphorylation of the
CC long-lasting phosphorylated forms of spinal MAPK1/3 and MAP kinase p38
CC induced by peripheral surgery, which drives the resolution of acute
CC postoperative allodynia (By similarity). Also important for
CC dephosphorylation of MAPK1/3 in local wound tissue, which further
CC contributes to resolution of acute pain (By similarity). Promotes cell
CC differentiation by regulating MAPK1/MAPK3 activity and regulating the
CC expression of AP1 transcription factors (PubMed:29043977).
CC {ECO:0000250|UniProtKB:Q9DBB1, ECO:0000269|PubMed:29043977,
CC ECO:0000269|PubMed:8670865}.
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;
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 -!- SUBUNIT: Interacts with MAPK1/ERK2. {ECO:0000269|PubMed:32721402}.
CC -!- INTERACTION:
CC Q16828; P05067: APP; NbExp=3; IntAct=EBI-746870, EBI-77613;
CC Q16828; P28482: MAPK1; NbExp=5; IntAct=EBI-746870, EBI-959949;
CC Q16828; P27361: MAPK3; NbExp=5; IntAct=EBI-746870, EBI-73995;
CC Q16828; Q99623: PHB2; NbExp=3; IntAct=EBI-746870, EBI-358348;
CC Q16828; P42681: TXK; NbExp=3; IntAct=EBI-746870, EBI-7877438;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8670865}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16828-1; Sequence=Displayed;
CC Name=2; Synonyms=DUSP6-ALT;
CC IsoId=Q16828-2; Sequence=VSP_005137;
CC -!- TISSUE SPECIFICITY: Expressed in keratinocytes (at protein level).
CC {ECO:0000269|PubMed:29043977}.
CC -!- DISEASE: Hypogonadotropic hypogonadism 19 with or without anosmia
CC (HH19) [MIM:615269]: A disorder characterized by absent or incomplete
CC sexual maturation by the age of 18 years, in conjunction with low
CC levels of circulating gonadotropins and testosterone and no other
CC abnormalities of the hypothalamic-pituitary axis. In some cases, it is
CC associated with non-reproductive phenotypes, such as anosmia, cleft
CC palate, and sensorineural hearing loss. Anosmia or hyposmia is related
CC to the absence or hypoplasia of the olfactory bulbs and tracts.
CC Hypogonadism is due to deficiency in gonadotropin-releasing hormone and
CC probably results from a failure of embryonic migration of gonadotropin-
CC releasing hormone-synthesizing neurons. In the presence of anosmia,
CC idiopathic hypogonadotropic hypogonadism is referred to as Kallmann
CC syndrome, whereas in the presence of a normal sense of smell, it has
CC been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH).
CC {ECO:0000269|PubMed:23643382}. Note=The disease is caused by variants
CC affecting distinct genetic loci, including the gene represented in this
CC entry. Some patients carrying mutations in DUSP6 also have a
CC heterozygous mutation in another HH-associated gene including FGFR1 and
CC SPRY4 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DUSP6ID46105ch12q21.html";
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DR EMBL; X93920; CAA63813.1; -; mRNA.
DR EMBL; AB013601; BAA31968.1; -; Genomic_DNA.
DR EMBL; AB013382; BAA34369.1; -; mRNA.
DR EMBL; AB013602; BAA31969.1; -; mRNA.
DR EMBL; BT006895; AAP35541.1; -; mRNA.
DR EMBL; BC003143; AAH03143.1; -; mRNA.
DR EMBL; BC003562; AAH03562.1; -; mRNA.
DR EMBL; BC005047; AAH05047.1; -; mRNA.
DR EMBL; BC037236; AAH37236.1; -; mRNA.
DR CCDS; CCDS9033.1; -. [Q16828-1]
DR CCDS; CCDS9034.1; -. [Q16828-2]
DR RefSeq; NP_001937.2; NM_001946.3. [Q16828-1]
DR RefSeq; NP_073143.2; NM_022652.3. [Q16828-2]
DR PDB; 1HZM; NMR; -; A=1-154.
DR PDB; 1MKP; X-ray; 2.35 A; A=205-347.
DR PDBsum; 1HZM; -.
DR PDBsum; 1MKP; -.
DR AlphaFoldDB; Q16828; -.
DR BMRB; Q16828; -.
DR SMR; Q16828; -.
DR BioGRID; 108181; 120.
DR ELM; Q16828; -.
DR IntAct; Q16828; 42.
DR MINT; Q16828; -.
DR STRING; 9606.ENSP00000279488; -.
DR BindingDB; Q16828; -.
DR ChEMBL; CHEMBL1250381; -.
DR DEPOD; DUSP6; -.
DR iPTMnet; Q16828; -.
DR PhosphoSitePlus; Q16828; -.
DR BioMuta; DUSP6; -.
DR DMDM; 108860971; -.
DR CPTAC; CPTAC-1564; -.
DR EPD; Q16828; -.
DR jPOST; Q16828; -.
DR MassIVE; Q16828; -.
DR MaxQB; Q16828; -.
DR PaxDb; Q16828; -.
DR PeptideAtlas; Q16828; -.
DR PRIDE; Q16828; -.
DR ProteomicsDB; 61089; -. [Q16828-1]
DR ProteomicsDB; 61090; -. [Q16828-2]
DR Antibodypedia; 4315; 550 antibodies from 38 providers.
DR DNASU; 1848; -.
DR Ensembl; ENST00000279488.8; ENSP00000279488.6; ENSG00000139318.8. [Q16828-1]
DR Ensembl; ENST00000308385.6; ENSP00000307835.6; ENSG00000139318.8. [Q16828-2]
DR GeneID; 1848; -.
DR KEGG; hsa:1848; -.
DR MANE-Select; ENST00000279488.8; ENSP00000279488.6; NM_001946.4; NP_001937.2.
DR UCSC; uc001tay.5; human. [Q16828-1]
DR CTD; 1848; -.
DR DisGeNET; 1848; -.
DR GeneCards; DUSP6; -.
DR GeneReviews; DUSP6; -.
DR HGNC; HGNC:3072; DUSP6.
DR HPA; ENSG00000139318; Tissue enhanced (salivary).
DR MalaCards; DUSP6; -.
DR MIM; 602748; gene.
DR MIM; 615269; phenotype.
DR neXtProt; NX_Q16828; -.
DR OpenTargets; ENSG00000139318; -.
DR Orphanet; 478; Kallmann syndrome.
DR Orphanet; 432; Normosmic congenital hypogonadotropic hypogonadism.
DR PharmGKB; PA27529; -.
DR VEuPathDB; HostDB:ENSG00000139318; -.
DR eggNOG; KOG1717; Eukaryota.
DR GeneTree; ENSGT00940000158342; -.
DR InParanoid; Q16828; -.
DR OMA; IEFDRWA; -.
DR PhylomeDB; Q16828; -.
DR TreeFam; TF105122; -.
DR BRENDA; 3.1.3.16; 2681.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; Q16828; -.
DR Reactome; R-HSA-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-HSA-202670; ERKs are inactivated.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-HSA-9652817; Signaling by MAPK mutants.
DR SignaLink; Q16828; -.
DR SIGNOR; Q16828; -.
DR BioGRID-ORCS; 1848; 19 hits in 1084 CRISPR screens.
DR ChiTaRS; DUSP6; human.
DR EvolutionaryTrace; Q16828; -.
DR GeneWiki; DUSP6; -.
DR GenomeRNAi; 1848; -.
DR Pharos; Q16828; Tchem.
DR PRO; PR:Q16828; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q16828; protein.
DR Bgee; ENSG00000139318; Expressed in parotid gland and 211 other tissues.
DR ExpressionAtlas; Q16828; baseline and differential.
DR Genevisible; Q16828; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; TAS:Reactome.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; TAS:Reactome.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:Ensembl.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; TAS:Reactome.
DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IDA:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0060420; P:regulation of heart growth; IBA:GO_Central.
DR GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
DR GO; GO:0051409; P:response to nitrosative stress; IEP:UniProtKB.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR Gene3D; 3.40.250.10; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR008343; MKP.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PIRSF; PIRSF000939; MAPK_Ptase; 1.
DR PRINTS; PR01764; MAPKPHPHTASE.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 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 splicing; Cytoplasm; Disease variant; Hydrolase;
KW Hypogonadotropic hypogonadism; Kallmann syndrome; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..381
FT /note="Dual specificity protein phosphatase 6"
FT /id="PRO_0000094804"
FT DOMAIN 30..148
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 206..349
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 176..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 293
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000269|PubMed:10048930"
FT VAR_SEQ 134..279
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9858808"
FT /id="VSP_005137"
FT VARIANT 77
FT /note="F -> I (in HH19; dbSNP:rs587776978)"
FT /evidence="ECO:0000269|PubMed:23643382"
FT /id="VAR_069943"
FT VARIANT 114
FT /note="V -> L (in dbSNP:rs2279574)"
FT /evidence="ECO:0000269|PubMed:8670865,
FT ECO:0000269|PubMed:9858808, ECO:0000269|Ref.3"
FT /id="VAR_015113"
FT VARIANT 144
FT /note="S -> A (in dbSNP:rs770087)"
FT /id="VAR_051750"
FT VARIANT 182
FT /note="S -> F (in HH19; rare variant associated with
FT susceptibility to disease; the patient carries a second
FT mutation in the HH-associated gene FGFR1;
FT dbSNP:rs139318648)"
FT /evidence="ECO:0000269|PubMed:23643382"
FT /id="VAR_069944"
FT VARIANT 189
FT /note="N -> S (in HH19; dbSNP:rs143946794)"
FT /evidence="ECO:0000269|PubMed:23643382"
FT /id="VAR_069945"
FT VARIANT 313
FT /note="N -> I (in dbSNP:rs12828557)"
FT /id="VAR_051751"
FT VARIANT 346
FT /note="T -> M (in HH19; rare variant associated with
FT susceptibility to disease; the patient carries a second
FT variant in the HH-associated gene SPRY4;
FT dbSNP:rs146089505)"
FT /evidence="ECO:0000269|PubMed:23643382"
FT /id="VAR_069946"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:1HZM"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:1HZM"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:1HZM"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1HZM"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1HZM"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:1HZM"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1HZM"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1HZM"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:1HZM"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:1HZM"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1HZM"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1HZM"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:1HZM"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1HZM"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:1HZM"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:1MKP"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1MKP"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:1MKP"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:1MKP"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1MKP"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:1MKP"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:1MKP"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:1MKP"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:1MKP"
FT HELIX 298..312
FT /evidence="ECO:0007829|PDB:1MKP"
FT HELIX 316..326
FT /evidence="ECO:0007829|PDB:1MKP"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:1MKP"
SQ SEQUENCE 381 AA; 42320 MW; 386612227F5D3B2A CRC64;
MIDTLRPVPF ASEMAISKTV AWLNEQLELG NERLLLMDCR PQELYESSHI ESAINVAIPG
IMLRRLQKGN LPVRALFTRG EDRDRFTRRC GTDTVVLYDE SSSDWNENTG GESVLGLLLK
KLKDEGCRAF YLEGGFSKFQ AEFSLHCETN LDGSCSSSSP PLPVLGLGGL RISSDSSSDI
ESDLDRDPNS ATDSDGSPLS NSQPSFPVEI LPFLYLGCAK DSTNLDVLEE FGIKYILNVT
PNLPNLFENA GEFKYKQIPI SDHWSQNLSQ FFPEAISFID EARGKNCGVL VHCLAGISRS
VTVTVAYLMQ KLNLSMNDAY DIVKMKKSNI SPNFNFMGQL LDFERTLGLS SPCDNRVPAQ
QLYFTTPSNQ NVYQVDSLQS T
