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 Genevisible; Q95UN8; DM.
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.
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
//
