ID   M3KSL_DROME             Reviewed;        1161 AA.
AC   Q95UN8; Q8MRK7; Q95VF6; Q9W3I3;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase;
DE            EC=2.7.11.25;
DE   AltName: Full=Mixed lineage kinase;
DE   AltName: Full=Protein slipper;
DE   AltName: Full=dMLK;
GN   Name=slpr {ECO:0000312|FlyBase:FBgn0030018};
GN   Synonyms=Mlk2 {ECO:0000312|EMBL:AAM50203.1}; ORFNames=CG2272;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAK98795.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=Berkeley {ECO:0000269|PubMed:11825878};
RC   TISSUE=Head {ECO:0000312|EMBL:AAK98795.1};
RX   PubMed=11825878; DOI=10.1101/gad.953002;
RA   Stronach B., Perrimon N.;
RT   "Activation of the JNK pathway during dorsal closure in Drosophila requires
RT   the mixed lineage kinase, slipper.";
RL   Genes Dev. 16:377-387(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3] {ECO:0000305}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4] {ECO:0000305, ECO:0000312|EMBL:AAM50203.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAM50203.1};
RC   TISSUE=Head {ECO:0000269|PubMed:12537569};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5] {ECO:0000305, ECO:0000312|EMBL:AAL08011.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-1161, FUNCTION, CATALYTIC ACTIVITY, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=Berkeley {ECO:0000269|PubMed:12676357};
RC   TISSUE=Embryo {ECO:0000269|PubMed:12676357};
RX   PubMed=12676357; DOI=10.1016/s0167-4889(03)00022-3;
RA   Sathyanarayana P., Barthwal M.K., Lane M.E., Acevedo S.F., Skoulakis E.M.,
RA   Bergmann A., Rana A.;
RT   "Drosophila mixed lineage kinase/slipper, a missing biochemical link in
RT   Drosophila JNK signaling.";
RL   Biochim. Biophys. Acta 1640:77-84(2003).
RN   [6] {ECO:0000305}
RP   FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-169.
RX   PubMed=12504027; DOI=10.1016/s1097-2765(02)00734-7;
RA   Sathyanarayana P., Barthwal M.K., Kundu C.N., Lane M.E., Bergmann A.,
RA   Tzivion G., Rana A.;
RT   "Activation of the Drosophila MLK by ceramide reveals TNF-alpha and
RT   ceramide as agonists of mammalian MLK3.";
RL   Mol. Cell 10:1527-1533(2002).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525 AND THR-862, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Activates the JUN N-terminal pathway during dorsal closure.
CC       {ECO:0000269|PubMed:11825878, ECO:0000269|PubMed:12504027,
CC       ECO:0000269|PubMed:12676357}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25;
CC         Evidence={ECO:0000269|PubMed:12676357};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.25; Evidence={ECO:0000269|PubMed:12676357};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P80192};
CC   -!- ACTIVITY REGULATION: Homodimerization via the leucine zipper domains is
CC       required for autophosphorylation and subsequent activation (By
CC       similarity). Activated by C6-ceramide. {ECO:0000250|UniProtKB:Q16584,
CC       ECO:0000269|PubMed:12504027}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q16584}.
CC   -!- TISSUE SPECIFICITY: Expressed both maternally and zygotically.
CC       Expressed uniformly in large quantities in the early embryo (stages 1-
CC       4). In the late embryo, expression is ubiquitous, but expression levels
CC       are dramatically reduced. Expressed in the adult head and thorax, and
CC       in S2 cells. {ECO:0000269|PubMed:12676357}.
CC   -!- PTM: Autophosphorylation on serine and threonine residues within the
CC       activation loop plays a role in enzyme activation.
CC       {ECO:0000250|UniProtKB:Q16584}.
CC   -!- DISRUPTION PHENOTYPE: Mutants display defects in dorsal closure,
CC       resulting in a cuticle that resembles an open shoe. Therefore the
CC       protein was given the name Slipper. {ECO:0000269|PubMed:11825878}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF46344.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY045717; AAK98795.1; -; mRNA.
DR   EMBL; AE014298; AAF46344.3; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY119549; AAM50203.1; -; mRNA.
DR   EMBL; AF416233; AAL08011.1; -; mRNA.
DR   RefSeq; NP_001188559.1; NM_001201630.2.
DR   RefSeq; NP_001188560.1; NM_001201631.2.
DR   RefSeq; NP_572458.3; NM_132230.4.
DR   AlphaFoldDB; Q95UN8; -.
DR   SMR; Q95UN8; -.
DR   BioGRID; 68838; 15.
DR   IntAct; Q95UN8; 1.
DR   STRING; 7227.FBpp0292850; -.
DR   iPTMnet; Q95UN8; -.
DR   PaxDb; 7227-FBpp0292850; -.
DR   GeneID; 44111; -.
DR   KEGG; dme:Dmel_CG2272; -.
DR   AGR; FB:FBgn0030018; -.
DR   CTD; 44111; -.
DR   FlyBase; FBgn0030018; slpr.
DR   VEuPathDB; VectorBase:FBgn0030018; -.
DR   eggNOG; KOG0192; Eukaryota.
DR   InParanoid; Q95UN8; -.
DR   Reactome; R-DME-5673000; RAF activation.
DR   Reactome; R-DME-5689880; Ub-specific processing proteases.
DR   Reactome; R-DME-5689896; Ovarian tumor domain proteases.
DR   Reactome; R-DME-9013148; CDC42 GTPase cycle.
DR   Reactome; R-DME-9013424; RHOV GTPase cycle.
DR   SignaLink; Q95UN8; -.
DR   BioGRID-ORCS; 44111; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 44111; -.
DR   PRO; PR:Q95UN8; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   ExpressionAtlas; Q95UN8; baseline and differential.
DR   GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004706; F:JUN kinase kinase kinase activity; IDA:UniProtKB.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IDA:FlyBase.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0071361; P:cellular response to ethanol; IMP:FlyBase.
DR   GO; GO:0046843; P:dorsal appendage formation; IMP:FlyBase.
DR   GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR   GO; GO:0007394; P:dorsal closure, elongation of leading edge cells; IMP:FlyBase.
DR   GO; GO:0046529; P:imaginal disc fusion, thorax closure; IMP:FlyBase.
DR   GO; GO:0048804; P:imaginal disc-derived female genitalia morphogenesis; IMP:FlyBase.
DR   GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:FlyBase.
DR   GO; GO:0007254; P:JNK cascade; IMP:UniProtKB.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IMP:FlyBase.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0009408; P:response to heat; IMP:FlyBase.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IGI:FlyBase.
DR   CDD; cd11876; SH3_MLK; 1.
DR   CDD; cd14061; STKc_MLK; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR23257:SF947; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; Q95UN8; DM.
PE   1: Evidence at protein level;
KW   ATP-binding; Developmental protein; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; SH3 domain; Transferase.
FT   CHAIN           1..1161
FT                   /note="Mitogen-activated protein kinase kinase kinase"
FT                   /id="PRO_0000086269"
FT   DOMAIN          56..120
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          142..402
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          426..447
FT                   /note="Leucine-zipper 1"
FT   REGION          461..482
FT                   /note="Leucine-zipper 2"
FT   REGION          560..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          658..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          988..1014
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1045..1093
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1137..1161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..602
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..830
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1062..1090
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        264
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q02779,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT                   ProRule:PRU10027"
FT   BINDING         148..156
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q02779,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000269|PubMed:12504027"
FT   MOD_RES         300
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         304
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         525
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         560
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16584"
FT   MOD_RES         685
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16584"
FT   MOD_RES         773
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16584"
FT   MOD_RES         792
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16584"
FT   MOD_RES         862
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         993
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q16584"
FT   MUTAGEN         169
FT                   /note="K->A: Loss of kinase activity. Attenuates bsk
FT                   activation."
FT                   /evidence="ECO:0000269|PubMed:12504027"
FT   CONFLICT        327
FT                   /note="D -> Y (in Ref. 4; AAM50203)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        670
FT                   /note="S -> P (in Ref. 5; AAL08011)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        908
FT                   /note="E -> G (in Ref. 5; AAL08011)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1161 AA;  128961 MW;  DD6C7ABAC08EDA24 CRC64;
     MPSQVSRGLD TTNMLPISEE QQLQQQQQQQ QLEQLHHPQI PEIPIPDLEQ VETQVGDGSL
     WTALYDYDAQ GEDELTLRRG EIVVVLSTDS EVSGDVGWWT GKIGDKVGVF PKDFVTDEDP
     LQLNVSSAIG DIQPHEIEYN ELDIKEVIGS GGFCKVHRGY YDGEEVAIKI AHQTGEDDMQ
     RMRDNVLQEA KLFWALKHEN IAALRGVCLN TKLCLVMEYA RGGSLNRILA GKIPPDVLVN
     WAIQIARGMN YLHNEAPMSI IHRDLKSSNV LIYEAIEGNH LQQKTLKITD FGLAREMYNT
     QRMSAAGTYA WMPPEVISVS TYSKFSDVWS YGVLLWELIT GETPYKGFDP LSVAYGVAVN
     TLTLPIPKTC PETWGALMKS CWQTDPHKRP GFKEILKQLE SIACSKFTLT PQESFHYMQE
     CWRKEIAGVL HDLREKEKEL RNKEEQLLRV QNEQREKANL LKIREQNLRE RERVLIEREL
     VMLQPVPSKR KHKKGKKNKP LQISLPTGFR HTITAVRDKA EQPGSPSFSG LRIVALTDGH
     KGKTWGPSTM HQRERSLLPS QLSGGQPEWP AQTSTHSSFS KSAPNLDKKQ QQQNQQQVAS
     LTPPPGLGIL GGSGGAGGTP ATPLLYPGIP IILTRPNNNN IGNCKAITTT ITTTTTTTTN
     NNNNNNNSIS ANNNNQLNNI STINSNNNNN QTNLTSQPNT IIVLQNGRNN SNSSTTSQSP
     AKIYHRARSQ EYGLDHPLAY QPPPLYLVTD DSSETDTVAS PTGCFHFLKS GNSSAASGAV
     HLHRFGGSLG NSPAVGRKKH SLDSSSHHPP ANGSNSFALP NQLTLPSEDN NTYDHAFYRD
     VIKKMSMASS ERVNSKSSGD LTMYNSSTPL TARDCDDAEE AFEGGRFQRN FSGSQFPRHC
     FFTRQEEEGE AEDEDAVAAE VDTADADADD ECQVPASQMR QNSTTSRKSS VTFQSVSFEE
     PDFVATPRTT ARSDLYTSSA SISFATYRSA SPSLSSSSTT ASASPSIAST EAVNGYHMQE
     NSILNTRRMQ DVQPHPDVIK LRAQEQRQQT KNQKKQRPKH ITKSKSVEAP VEGQHHEHDD
     HNDPQHQHHS AGSSKIRALF NLFTRSRKKY SKLAEHNMVG GPEFCAIDPY QTDLAMGGSS
     RSLKRKGKKP QTQSCEQLER C
//