DUS16_HUMAN
ID DUS16_HUMAN Reviewed; 665 AA.
AC Q9BY84; Q547C7; Q96QS2; Q9C0G3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Dual specificity protein phosphatase 16;
DE EC=3.1.3.16;
DE EC=3.1.3.48;
DE AltName: Full=Mitogen-activated protein kinase phosphatase 7;
DE Short=MAP kinase phosphatase 7;
DE Short=MKP-7;
GN Name=DUSP16; Synonyms=KIAA1700, MKP7;
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, AND SUBCELLULAR LOCATION.
RX PubMed=11489891; DOI=10.1074/jbc.m104600200;
RA Masuda K., Shima H., Watanabe M., Kikuchi K.;
RT "MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as
RT a shuttle protein.";
RL J. Biol. Chem. 276:39002-39011(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=14586399; DOI=10.1038/sj.onc.1207089;
RA Hoornaert I., Marynen P., Goris J., Sciot R., Baens M.;
RT "MAPK phosphatase DUSP16/MKP-7, a candidate tumor suppressor for chromosome
RT region 12p12-13, reduces BCR-ABL-induced transformation.";
RL Oncogene 22:7728-7736(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Montpetit A., Boily G., Sinnett D.;
RT "A detailed transcriptional map of the chromosome 12p12 tumor suppressor
RT locus.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 PHOSPHORYLATION AT SER-446.
RX PubMed=12794087; DOI=10.1074/jbc.m213254200;
RA Masuda K., Shima H., Katagiri C., Kikuchi K.;
RT "Activation of ERK induces phosphorylation of MAPK phosphatase-7, a JNK
RT specific phosphatase, at Ser-446.";
RL J. Biol. Chem. 278:32448-32456(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARRB2.
RX PubMed=15888437; DOI=10.1074/jbc.m501926200;
RA Willoughby E.A., Collins M.K.;
RT "Dynamic interaction between the dual specificity phosphatase MKP7 and the
RT JNK3 scaffold protein beta-arrestin 2.";
RL J. Biol. Chem. 280:25651-25658(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION AT LYS-55 BY EIS (MICROBIAL INFECTION).
RX PubMed=22547814; DOI=10.1073/pnas.1120251109;
RA Kim K.H., An D.R., Song J., Yoon J.Y., Kim H.S., Yoon H.J., Im H.N.,
RA Kim J., Kim do J., Lee S.J., Kim K.H., Lee H.M., Kim H.J., Jo E.K.,
RA Lee J.Y., Suh S.W.;
RT "Mycobacterium tuberculosis Eis protein initiates suppression of host
RT immune responses by acetylation of DUSP16/MKP-7.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7729-7734(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 5-150.
RG Structural genomics consortium (SGC);
RT "The structure of the rhodanese domain of the human 2 dual specificity
RT phosphatase 16.";
RL Submitted (JUN-2009) to the PDB data bank.
CC -!- FUNCTION: Dual specificity protein phosphatase involved in the
CC inactivation of MAP kinases. Dephosphorylates MAPK10 bound to ARRB2.
CC {ECO:0000269|PubMed:11489891, ECO:0000269|PubMed:15888437}.
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};
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 ARRB2. {ECO:0000269|PubMed:15888437}.
CC -!- INTERACTION:
CC Q9BY84; P45983-4: MAPK8; NbExp=3; IntAct=EBI-3443956, EBI-18121963;
CC Q9BY84; P45984: MAPK9; NbExp=7; IntAct=EBI-3443956, EBI-713568;
CC Q9BY84; O76024: WFS1; NbExp=3; IntAct=EBI-3443956, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasmic vesicle.
CC Note=After dissociation upon AGTR stimulation, re-associates with ARRB2
CC on endocytic vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BY84-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BY84-2; Sequence=VSP_056981, VSP_056982;
CC -!- PTM: Phosphorylated at Ser-446 by MAPK1/ERK2, which prevents its
CC degradation, and thereby stabilizes it and blocks JNK MAPK activity.
CC {ECO:0000269|PubMed:12794087}.
CC -!- PTM: (Microbial infection) Acetylated at Lys-55 by the M.tuberculosis
CC Eis protein; this leads to the inhibition of JNK-dependent autophagy,
CC phagosome maturation, and ROS (reactive oxygen species) generation for
CC enhanced intracellular survival of M.tuberculosis.
CC {ECO:0000269|PubMed:22547814}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21791.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB052156; BAB40814.1; -; mRNA.
DR EMBL; AF506796; AAN75120.1; -; mRNA.
DR EMBL; AY038927; AAK69770.1; -; mRNA.
DR EMBL; AB051487; BAB21791.1; ALT_INIT; mRNA.
DR EMBL; AC007619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109235; AAI09236.1; -; mRNA.
DR CCDS; CCDS8650.1; -. [Q9BY84-1]
DR RefSeq; NP_085143.1; NM_030640.2. [Q9BY84-1]
DR RefSeq; XP_006719218.1; XM_006719155.2. [Q9BY84-1]
DR RefSeq; XP_011519158.1; XM_011520856.1. [Q9BY84-1]
DR RefSeq; XP_011519159.1; XM_011520857.1.
DR PDB; 2VSW; X-ray; 2.20 A; A/B=5-150.
DR PDB; 3TG3; X-ray; 2.68 A; A/B/C/D=5-138.
DR PDB; 4YR8; X-ray; 2.40 A; B/D/G/H=156-301.
DR PDBsum; 2VSW; -.
DR PDBsum; 3TG3; -.
DR PDBsum; 4YR8; -.
DR AlphaFoldDB; Q9BY84; -.
DR BMRB; Q9BY84; -.
DR SMR; Q9BY84; -.
DR BioGRID; 123321; 245.
DR IntAct; Q9BY84; 32.
DR MINT; Q9BY84; -.
DR STRING; 9606.ENSP00000298573; -.
DR DEPOD; DUSP16; -.
DR iPTMnet; Q9BY84; -.
DR PhosphoSitePlus; Q9BY84; -.
DR BioMuta; DUSP16; -.
DR DMDM; 20137933; -.
DR EPD; Q9BY84; -.
DR jPOST; Q9BY84; -.
DR MassIVE; Q9BY84; -.
DR MaxQB; Q9BY84; -.
DR PaxDb; Q9BY84; -.
DR PeptideAtlas; Q9BY84; -.
DR PRIDE; Q9BY84; -.
DR ProteomicsDB; 77894; -.
DR ProteomicsDB; 79602; -. [Q9BY84-1]
DR Antibodypedia; 11891; 225 antibodies from 34 providers.
DR DNASU; 80824; -.
DR Ensembl; ENST00000228862.3; ENSP00000228862.3; ENSG00000111266.9. [Q9BY84-2]
DR Ensembl; ENST00000298573.9; ENSP00000298573.5; ENSG00000111266.9. [Q9BY84-1]
DR Ensembl; ENST00000626413.3; ENSP00000487512.1; ENSG00000280962.3. [Q9BY84-1]
DR Ensembl; ENST00000628303.1; ENSP00000487034.1; ENSG00000280962.3. [Q9BY84-2]
DR GeneID; 80824; -.
DR KEGG; hsa:80824; -.
DR MANE-Select; ENST00000298573.9; ENSP00000298573.5; NM_030640.3; NP_085143.1.
DR UCSC; uc001rao.3; human. [Q9BY84-1]
DR CTD; 80824; -.
DR DisGeNET; 80824; -.
DR GeneCards; DUSP16; -.
DR HGNC; HGNC:17909; DUSP16.
DR HPA; ENSG00000111266; Low tissue specificity.
DR MIM; 607175; gene.
DR neXtProt; NX_Q9BY84; -.
DR OpenTargets; ENSG00000111266; -.
DR PharmGKB; PA38475; -.
DR VEuPathDB; HostDB:ENSG00000111266; -.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000157164; -.
DR HOGENOM; CLU_027074_16_0_1; -.
DR InParanoid; Q9BY84; -.
DR OMA; TLEYYKH; -.
DR PhylomeDB; Q9BY84; -.
DR TreeFam; TF105122; -.
DR PathwayCommons; Q9BY84; -.
DR Reactome; R-HSA-112409; RAF-independent MAPK1/3 activation.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-HSA-9636569; Suppression of autophagy.
DR Reactome; R-HSA-9652817; Signaling by MAPK mutants.
DR SignaLink; Q9BY84; -.
DR SIGNOR; Q9BY84; -.
DR BioGRID-ORCS; 80824; 12 hits in 1084 CRISPR screens.
DR ChiTaRS; DUSP16; human.
DR EvolutionaryTrace; Q9BY84; -.
DR GeneWiki; DUSP16; -.
DR GenomeRNAi; 80824; -.
DR Pharos; Q9BY84; Tbio.
DR PRO; PR:Q9BY84; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9BY84; protein.
DR Bgee; ENSG00000111266; Expressed in adrenal tissue and 107 other tissues.
DR ExpressionAtlas; Q9BY84; baseline and differential.
DR Genevisible; Q9BY84; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008432; F:JUN kinase binding; IPI:UniProtKB.
DR GO; GO:0017017; F:MAP kinase tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:UniProtKB.
DR GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; 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:0004721; F:phosphoprotein phosphatase activity; IMP:UniProtKB.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008330; F:protein tyrosine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0045204; P:MAPK export from nucleus; IDA:UniProtKB.
DR GO; GO:0043508; P:negative regulation of JUN kinase activity; IDA:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:UniProtKB.
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; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR Pfam; PF00581; Rhodanese; 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; 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; Acetylation; Alternative splicing; Cytoplasm;
KW Cytoplasmic vesicle; Hydrolase; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..665
FT /note="Dual specificity protein phosphatase 16"
FT /id="PRO_0000094826"
FT DOMAIN 22..137
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 158..300
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 321..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 244
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MOD_RES 55
FT /note="(Microbial infection) N6-acetyllysine; by EIS"
FT /evidence="ECO:0000269|PubMed:22547814"
FT MOD_RES 446
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:12794087"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 124..143
FT /note="GFAEFSRCFPGLCEGKSTLV -> ADAAEWDWLCVKCQQYLSKA (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_056981"
FT VAR_SEQ 144..665
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_056982"
FT VARIANT 23
FT /note="T -> M (in dbSNP:rs36049447)"
FT /id="VAR_051753"
FT VARIANT 366
FT /note="V -> M (in dbSNP:rs3809199)"
FT /id="VAR_051754"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2VSW"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:2VSW"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:3TG3"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:2VSW"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:2VSW"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:2VSW"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:2VSW"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2VSW"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2VSW"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:2VSW"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2VSW"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:2VSW"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2VSW"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:4YR8"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4YR8"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:4YR8"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:4YR8"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:4YR8"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4YR8"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4YR8"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:4YR8"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:4YR8"
FT STRAND 240..249
FT /evidence="ECO:0007829|PDB:4YR8"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:4YR8"
FT HELIX 267..277
FT /evidence="ECO:0007829|PDB:4YR8"
FT HELIX 285..297
FT /evidence="ECO:0007829|PDB:4YR8"
SQ SEQUENCE 665 AA; 73102 MW; 1BD853FF08460DFF CRC64;
MAHEMIGTQI VTERLVALLE SGTEKVLLID SRPFVEYNTS HILEAININC SKLMKRRLQQ
DKVLITELIQ HSAKHKVDID CSQKVVVYDQ SSQDVASLSS DCFLTVLLGK LEKSFNSVHL
LAGGFAEFSR CFPGLCEGKS TLVPTCISQP CLPVANIGPT RILPNLYLGC QRDVLNKELM
QQNGIGYVLN ASNTCPKPDF IPESHFLRVP VNDSFCEKIL PWLDKSVDFI EKAKASNGCV
LVHCLAGISR SATIAIAYIM KRMDMSLDEA YRFVKEKRPT ISPNFNFLGQ LLDYEKKIKN
QTGASGPKSK LKLLHLEKPN EPVPAVSEGG QKSETPLSPP CADSATSEAA GQRPVHPASV
PSVPSVQPSL LEDSPLVQAL SGLHLSADRL EDSNKLKRSF SLDIKSVSYS ASMAASLHGF
SSSEDALEYY KPSTTLDGTN KLCQFSPVQE LSEQTPETSP DKEEASIPKK LQTARPSDSQ
SKRLHSVRTS SSGTAQRSLL SPLHRSGSVE DNYHTSFLFG LSTSQQHLTK SAGLGLKGWH
SDILAPQTST PSLTSSWYFA TESSHFYSAS AIYGGSASYS AYSCSQLPTC GDQVYSVRRR
QKPSDRADSR RSWHEESPFE KQFKRRSCQM EFGESIMSEN RSREELGKVG SQSSFSGSME
IIEVS
