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 27-MAR-2024, entry version 214. 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="https://atlasgeneticsoncology.org/gene/46105/DUSP6"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 124. 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; 9606-ENSP00000279488; -. DR PeptideAtlas; Q16828; -. DR ProteomicsDB; 61089; -. [Q16828-1] DR ProteomicsDB; 61090; -. [Q16828-2] DR Antibodypedia; 4315; 633 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 AGR; HGNC:3072; -. 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; NDQRCIG; -. DR OrthoDB; 2901840at2759; -. 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; 23 hits in 1175 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 213 other cell types or tissues. DR ExpressionAtlas; Q16828; baseline and differential. 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:0033550; F:MAP kinase tyrosine phosphatase activity; IBA:GO_Central. 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: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 CDD; cd01446; DSP_MapKP; 1. DR CDD; cd14566; DSP_MKP_classII; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1. DR IDEAL; IID00728; -. 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 PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR10159:SF45; DUAL SPECIFICITY PROTEIN PHOSPHATASE 6; 1. 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; (Phosphotyrosine protein) phosphatases II; 1. DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1. DR PROSITE; PS50206; RHODANESE_3; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. DR Genevisible; Q16828; HS. 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; 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; 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 //