DUS15_HUMAN
ID DUS15_HUMAN Reviewed; 295 AA.
AC Q9H1R2; A6NH79; A8MVC8; Q5QP62; Q5QP63; Q5QP65; Q6PGN7; Q8N826; Q9BX24;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 4.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Dual specificity protein phosphatase 15 {ECO:0000312|HGNC:HGNC:16236};
DE EC=3.1.3.16 {ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:22792334};
DE EC=3.1.3.48 {ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:22792334};
DE AltName: Full=VH1-related member Y {ECO:0000303|PubMed:15138252};
DE AltName: Full=Vaccinia virus VH1-related dual-specific protein phosphatase Y {ECO:0000305|PubMed:15138252};
GN Name=DUSP15 {ECO:0000312|HGNC:HGNC:16236};
GN Synonyms=C20orf57 {ECO:0000312|HGNC:HGNC:16236},
GN VHY {ECO:0000303|PubMed:15138252};
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] (ISOFORMS 1 AND 4).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and PNS;
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 FUNCTION, MUTAGENESIS OF CYS-85, MYRISTOYLATION AT GLY-2 (ISOFORM 3),
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15138252; DOI=10.1074/jbc.m403442200;
RA Alonso A., Narisawa S., Bogetz J., Tautz L., Hadzic R., Huynh H.,
RA Williams S., Gjoerloff-Wingren A., Bremer M.C.D., Holsinger L.J.,
RA Millan J.L., Mustelin T.;
RT "VHY, a novel myristoylated testis-restricted dual specificity protein
RT phosphatase related to VHX.";
RL J. Biol. Chem. 279:32586-32591(2004).
RN [6]
RP CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=22792334; DOI=10.1371/journal.pone.0040457;
RA Schmidt F., van den Eijnden M., Pescini Gobert R., Saborio G.P.,
RA Carboni S., Alliod C., Pouly S., Staugaitis S.M., Dutta R., Trapp B.,
RA Hooft van Huijsduijnen R.;
RT "Identification of VHY/Dusp15 as a regulator of oligodendrocyte
RT differentiation through a systematic genomics approach.";
RL PLoS ONE 7:E40457-E40457(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-157 (ISOFORM 3).
RX PubMed=16170801; DOI=10.1002/prot.20642;
RA Yoon T.-S., Jeong D.G., Kim J.H., Cho Y.H., Son J.H., Lee J.W., Ryu S.E.,
RA Kim S.J.;
RT "Crystal structure of the catalytic domain of human VHY, a dual-specificity
RT protein phosphatase.";
RL Proteins 61:694-697(2005).
CC -!- FUNCTION: May dephosphorylate MAPK13, ATF2, ERBB3, PDGFRB and SNX6
CC (PubMed:22792334). {ECO:0000269|PubMed:22792334}.
CC -!- FUNCTION: [Isoform 3]: May play a role in the regulation of
CC oligodendrocyte differentiation. May play a role in the regulation of
CC myelin formation (By similarity). Involved in the regulation of Erk1/2
CC phosphorylation in Schwann cells; the signaling may be linked to the
CC regulation of myelination (By similarity).
CC {ECO:0000250|UniProtKB:B4F7B7, ECO:0000250|UniProtKB:Q8R4V2}.
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:0000269|PubMed:22792334};
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 -!- INTERACTION:
CC Q9H1R2; P16333: NCK1; NbExp=2; IntAct=EBI-1752795, EBI-389883;
CC Q9H1R2; P19174: PLCG1; NbExp=2; IntAct=EBI-1752795, EBI-79387;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:15138252}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Lipid-anchor;
CC Cytoplasmic side.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9H1R2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H1R2-2; Sequence=VSP_007292, VSP_007293;
CC Name=3; Synonyms=A;
CC IsoId=Q9H1R2-3; Sequence=VSP_019228, VSP_007292, VSP_007293;
CC Name=4;
CC IsoId=Q9H1R2-4; Sequence=VSP_043107, VSP_007292, VSP_007293;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis (PubMed:15138252).
CC Expressed in brain; up-regulated in patients with multiple sclerosis
CC gray matter lesions (PubMed:22792334). {ECO:0000269|PubMed:15138252,
CC ECO:0000269|PubMed:22792334}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- CAUTION: Although assigned as two separate genes (c20orf57 and DUSP15),
CC it is probable that C20orf57 does not exist by itself and is a part of
CC the DUSP15 gene. {ECO:0000305}.
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DR EMBL; AK091960; BAG52450.1; -; mRNA.
DR EMBL; AK097430; BAC05048.1; -; mRNA.
DR EMBL; AL160175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76410.1; -; Genomic_DNA.
DR EMBL; BC056911; AAH56911.1; -; mRNA.
DR EMBL; BM554314; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13193.1; -. [Q9H1R2-3]
DR CCDS; CCDS42862.1; -. [Q9H1R2-4]
DR CCDS; CCDS82606.1; -. [Q9H1R2-1]
DR CCDS; CCDS82607.1; -. [Q9H1R2-2]
DR RefSeq; NP_001012662.1; NM_001012644.2. [Q9H1R2-4]
DR RefSeq; NP_001307407.1; NM_001320478.1. [Q9H1R2-2]
DR RefSeq; NP_001307408.1; NM_001320479.1. [Q9H1R2-1]
DR RefSeq; NP_542178.2; NM_080611.4. [Q9H1R2-3]
DR RefSeq; NP_817130.1; NM_177991.2. [Q9H1R2-4]
DR PDB; 1YZ4; X-ray; 2.40 A; A/B=5-145.
DR PDBsum; 1YZ4; -.
DR AlphaFoldDB; Q9H1R2; -.
DR SMR; Q9H1R2; -.
DR BioGRID; 126164; 36.
DR IntAct; Q9H1R2; 21.
DR MINT; Q9H1R2; -.
DR STRING; 9606.ENSP00000341658; -.
DR BindingDB; Q9H1R2; -.
DR ChEMBL; CHEMBL2396507; -.
DR DEPOD; DUSP15; -.
DR iPTMnet; Q9H1R2; -.
DR PhosphoSitePlus; Q9H1R2; -.
DR BioMuta; DUSP15; -.
DR DMDM; 30316387; -.
DR MassIVE; Q9H1R2; -.
DR PaxDb; Q9H1R2; -.
DR PeptideAtlas; Q9H1R2; -.
DR PRIDE; Q9H1R2; -.
DR ProteomicsDB; 80441; -. [Q9H1R2-1]
DR ProteomicsDB; 80442; -. [Q9H1R2-2]
DR ProteomicsDB; 80443; -. [Q9H1R2-3]
DR ProteomicsDB; 80444; -. [Q9H1R2-4]
DR Antibodypedia; 25257; 215 antibodies from 23 providers.
DR DNASU; 128853; -.
DR Ensembl; ENST00000278979.7; ENSP00000278979.3; ENSG00000149599.16. [Q9H1R2-1]
DR Ensembl; ENST00000339738.10; ENSP00000341658.5; ENSG00000149599.16. [Q9H1R2-3]
DR Ensembl; ENST00000375966.8; ENSP00000365133.4; ENSG00000149599.16. [Q9H1R2-2]
DR Ensembl; ENST00000398083.5; ENSP00000381157.1; ENSG00000149599.16. [Q9H1R2-4]
DR Ensembl; ENST00000398084.6; ENSP00000381158.2; ENSG00000149599.16. [Q9H1R2-4]
DR Ensembl; ENST00000486996.5; ENSP00000419818.1; ENSG00000149599.16. [Q9H1R2-4]
DR GeneID; 128853; -.
DR KEGG; hsa:128853; -.
DR MANE-Select; ENST00000339738.10; ENSP00000341658.5; NM_080611.5; NP_542178.2. [Q9H1R2-3]
DR UCSC; uc002wwu.2; human. [Q9H1R2-1]
DR CTD; 128853; -.
DR DisGeNET; 128853; -.
DR GeneCards; DUSP15; -.
DR HGNC; HGNC:16236; DUSP15.
DR HPA; ENSG00000149599; Tissue enriched (testis).
DR MIM; 616776; gene.
DR neXtProt; NX_Q9H1R2; -.
DR OpenTargets; ENSG00000149599; -.
DR PharmGKB; PA27524; -.
DR VEuPathDB; HostDB:ENSG00000149599; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000162011; -.
DR HOGENOM; CLU_979904_0_0_1; -.
DR InParanoid; Q9H1R2; -.
DR OMA; TSPFNDE; -.
DR OrthoDB; 1576308at2759; -.
DR PhylomeDB; Q9H1R2; -.
DR TreeFam; TF105126; -.
DR PathwayCommons; Q9H1R2; -.
DR SABIO-RK; Q9H1R2; -.
DR SignaLink; Q9H1R2; -.
DR BioGRID-ORCS; 128853; 7 hits in 1073 CRISPR screens.
DR EvolutionaryTrace; Q9H1R2; -.
DR GeneWiki; DUSP15; -.
DR GenomeRNAi; 128853; -.
DR Pharos; Q9H1R2; Tbio.
DR PRO; PR:Q9H1R2; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H1R2; protein.
DR Bgee; ENSG00000149599; Expressed in left testis and 142 other tissues.
DR ExpressionAtlas; Q9H1R2; baseline and differential.
DR Genevisible; Q9H1R2; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; IDA:UniProtKB.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0048713; P:regulation of oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF49879; SSF49879; 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 splicing; Cell membrane; Cytoplasm; Hydrolase;
KW Lipoprotein; Membrane; Myristate; Protein phosphatase; Reference proteome.
FT CHAIN 1..295
FT /note="Dual specificity protein phosphatase 15"
FT /id="PRO_0000094824"
FT DOMAIN 1..141
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 251..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 85
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043107"
FT VAR_SEQ 1..4
FT /note="MTEG -> MGNGMTK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019228"
FT VAR_SEQ 143..232
FT /note="GARHRTSKTSGAQCPPMTSATCLLAARVALLSAALVREATGRTAQRCRLSPR
FT AAAERLLGPPPHVAAGWSPDPKYQICLCFGEEDPGPTQ -> LRRQLEERFGESPFRDE
FT EELRALLPLCKRCRQGSATSASSAGPHSAASEGTVQRLVPRTPREAHRPLPLLARVKQT
FT FSCLPRCLSRKGGK (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007292"
FT VAR_SEQ 233..295
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007293"
FT MUTAGEN 85
FT /note="C->S: Loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:15138252"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1YZ4"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1YZ4"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:1YZ4"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1YZ4"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1YZ4"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:1YZ4"
FT HELIX 64..76
FT /evidence="ECO:0007829|PDB:1YZ4"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1YZ4"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1YZ4"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:1YZ4"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:1YZ4"
FT HELIX 126..137
FT /evidence="ECO:0007829|PDB:1YZ4"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:1YZ4"
FT INIT_MET Q9H1R2-3:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT LIPID Q9H1R2-3:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:15138252"
SQ SEQUENCE 295 AA; 31882 MW; 28F8A687ECB5C219 CRC64;
MTEGVLPGLY LGNFIDAKDL DQLGRNKITH IISIHESPQP LLQDITYLRI PVADTPEVPI
KKHFKECINF IHCCRLNGGN CLVHCFAGIS RSTTIVTAYV MTVTGLGWRD VLEAIKATRP
IANPNPGFRQ QLEEFGWASS QKGARHRTSK TSGAQCPPMT SATCLLAARV ALLSAALVRE
ATGRTAQRCR LSPRAAAERL LGPPPHVAAG WSPDPKYQIC LCFGEEDPGP TQHPKEQLIM
ADVQVQLRPG SSSCTLSAST ERPDGSSTPG NPDGITHLQC SCLHPKRAAS SSCTR
