JAK_DROME
ID JAK_DROME Reviewed; 1177 AA.
AC Q24592; Q712V3; Q8SZI9; Q9VYZ7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Tyrosine-protein kinase hopscotch;
DE EC=2.7.10.2;
GN Name=hop; Synonyms=HD-160; ORFNames=CG1594;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=8314084; DOI=10.1101/gad.8.3.300;
RA Binari R., Perrimon N.;
RT "Stripe-specific regulation of pair-rule genes by hopscotch, a putative Jak
RT family tyrosine kinase in Drosophila.";
RL Genes Dev. 8:300-312(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 596-1177.
RC STRAIN=Berkeley; TISSUE=Head;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1020-1075.
RX PubMed=9731193; DOI=10.1006/bbrc.1998.9003;
RA Oates A.C., Wollberg P., Achen M.G., Wilks A.F.;
RT "Sampling the genomic pool of protein tyrosine kinase genes using the
RT polymerase chain reaction with genomic DNA.";
RL Biochem. Biophys. Res. Commun. 249:660-667(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-321, 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).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND INTERACTION WITH PIWI
RP AND HSP83.
RX PubMed=21186352; DOI=10.1038/ng.743;
RA Gangaraju V.K., Yin H., Weiner M.M., Wang J., Huang X.A., Lin H.;
RT "Drosophila Piwi functions in Hsp90-mediated suppression of phenotypic
RT variation.";
RL Nat. Genet. 43:153-158(2011).
CC -!- FUNCTION: Tyrosine kinase of the non-receptor type, phosphorylates the
CC marelle protein. Required maternally for the establishment of the
CC normal array of embryonic segments: involved in the control of pair-
CC rule gene transcription in a stripe-specific manner. Together with
CC Hsp83 and piwi, mediates canalization, also known as developmental
CC robustness, likely via epigenetic silencing of existing genetic
CC variants and suppression of transposon-induced new genetic variation.
CC {ECO:0000269|PubMed:21186352, ECO:0000269|PubMed:8314084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Forms a complex with Hsp83 and piwi; probably Hop mediates the
CC interaction between piwi and Hsp83.
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Wholly intracellular, possibly
CC membrane associated. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout development. {ECO:0000269|PubMed:8314084}.
CC -!- DOMAIN: Possesses two phosphotransferase domains. The second one
CC probably contains the catalytic domain (By similarity), while the
CC presence of slight differences suggest a different role for domain 1
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. JAK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48491.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L26975; AAA62441.1; -; mRNA.
DR EMBL; AE014298; AAF48035.1; -; Genomic_DNA.
DR EMBL; BT006331; AAP20030.1; -; mRNA.
DR EMBL; AY070869; AAL48491.1; ALT_INIT; mRNA.
DR EMBL; AJ002915; CAA05750.1; -; Genomic_DNA.
DR PIR; A36984; A36984.
DR RefSeq; NP_511119.2; NM_078564.3.
DR AlphaFoldDB; Q24592; -.
DR SMR; Q24592; -.
DR BioGRID; 58492; 42.
DR DIP; DIP-61595N; -.
DR IntAct; Q24592; 2.
DR STRING; 7227.FBpp0073313; -.
DR iPTMnet; Q24592; -.
DR PaxDb; Q24592; -.
DR PRIDE; Q24592; -.
DR DNASU; 32080; -.
DR EnsemblMetazoa; FBtr0073457; FBpp0073313; FBgn0004864.
DR GeneID; 32080; -.
DR KEGG; dme:Dmel_CG1594; -.
DR CTD; 32080; -.
DR FlyBase; FBgn0004864; hop.
DR VEuPathDB; VectorBase:FBgn0004864; -.
DR eggNOG; KOG0197; Eukaryota.
DR HOGENOM; CLU_008155_2_1_1; -.
DR InParanoid; Q24592; -.
DR OMA; ETIMDGW; -.
DR OrthoDB; 58906at2759; -.
DR PhylomeDB; Q24592; -.
DR BRENDA; 2.7.10.2; 1994.
DR Reactome; R-DME-1266695; Interleukin-7 signaling.
DR Reactome; R-DME-209209; Formation of the activated receptor complex.
DR Reactome; R-DME-209228; Formation of the activated STAT92E dimer and transport to the nucleus.
DR Reactome; R-DME-210688; Dephosphorylation by PTP61F phosphatases.
DR Reactome; R-DME-5673000; RAF activation.
DR Reactome; R-DME-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-DME-69231; Cyclin D associated events in G1.
DR Reactome; R-DME-8985947; Interleukin-9 signaling.
DR Reactome; R-DME-9020558; Interleukin-2 signaling.
DR Reactome; R-DME-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K).
DR Reactome; R-DME-9027284; Erythropoietin activates RAS.
DR SignaLink; Q24592; -.
DR BioGRID-ORCS; 32080; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 32080; -.
DR PRO; PR:Q24592; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004864; Expressed in mouthpart and 24 other tissues.
DR ExpressionAtlas; Q24592; baseline and differential.
DR Genevisible; Q24592; DM.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:FlyBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005126; F:cytokine receptor binding; IPI:FlyBase.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:FlyBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
DR GO; GO:0007350; P:blastoderm segmentation; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0001751; P:compound eye photoreceptor cell differentiation; IMP:FlyBase.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IMP:FlyBase.
DR GO; GO:0045317; P:equator specification; IMP:FlyBase.
DR GO; GO:0042067; P:establishment of ommatidial planar polarity; IMP:FlyBase.
DR GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:FlyBase.
DR GO; GO:0007481; P:haltere disc morphogenesis; IMP:FlyBase.
DR GO; GO:0042386; P:hemocyte differentiation; IMP:FlyBase.
DR GO; GO:0007442; P:hindgut morphogenesis; IMP:FlyBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0035167; P:larval lymph gland hemopoiesis; IMP:FlyBase.
DR GO; GO:0007478; P:leg disc morphogenesis; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0060031; P:mediolateral intercalation; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0016318; P:ommatidial rotation; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0030713; P:ovarian follicle cell stalk formation; IMP:FlyBase.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IDA:FlyBase.
DR GO; GO:0007365; P:periodic partitioning; IMP:FlyBase.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0007538; P:primary sex determination; IMP:FlyBase.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IDA:FlyBase.
DR GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase.
DR GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; TAS:FlyBase.
DR GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 2.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Developmental protein; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; SH2 domain; Transcription;
KW Transcription regulation; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..1177
FT /note="Tyrosine-protein kinase hopscotch"
FT /id="PRO_0000088118"
FT DOMAIN 46..414
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 433..539
FT /note="SH2; atypical"
FT DOMAIN 582..843
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 892..1164
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1014
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 898..906
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 926
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1047
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 1048
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CONFLICT 365
FT /note="F -> V (in Ref. 1; AAA62441)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="G -> A (in Ref. 1; AAA62441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1177 AA; 135062 MW; BF8587C420BF3A8F CRC64;
MALANGGEDR MDDSSSGRTS LADSASLTNS SLRSGTSSQS IHTNDGTIRV FNFTTGEFER
FHPNMLCEEI CNTMCRQLGI APIAQLLYGI REHSTSRRPS PLVRLDLTWC LPGERLNCQL
VYCFRMRFRV PELDSQLELI DGRSHKFLYR QMRYDMRTEQ IPEIRYPEHK DKSTGLAVMD
MLIDDQEQSE DQQAMRSIEK LYKLYLPPSL WRAHSFFVGS KIREVFRSLK ANSLSVERLK
WHYVHQVSHL APTYMTEQFT CTVQYLPNEE VARGSGPIGT SLAHSTSTLA SSGSTNTLST
LTTNTNSVAL GGSGKKAKRR STSGGIDVYV RVFPHDSLEP GLKVARVTSE ATLKWILVGA
VEGIFMISKI NDTSVRLEIV GLPKGYEMQF QTEKEMKSFI SYLGIYIRLS SKWMQDLCHS
YRTPSLEELS SLHCHGPIGG AYSLMKLHEN GDKCGSYIVR ECDREYNIYY IDINTKIMAK
KTDQERCKTE TFRIVRKDSQ WKLSYNNGEH VLNSLHEVAH IIQADSPDRY RIPASKYDKP
PLLLLLLPKN LKAKKTDLQL SEAELQRRNP QIFNPRTDLQ WYPDSISLSD DGMMFTMRGD
WIQQSPVKDV SVTMKMLKSD GNFMEFFRLA QTWSLIQSPQ FLKLYGLTLA DPYTMVMEYS
RYGPLNKFLH SMPNVTLHCL LDLMHGLVRG MHYLEDNKII HNYIRCSNLY VTKYDPNSYV
LDAKISDPGY PRPYRESDSP WIPVKYYRNL QAAKTDQFAQ LWAFATTIYE IFSRCKEDLS
TLRQEQLLRQ KNLDGNILKM LDQDICPAPI FETIMDGWSD DETKRFSHHD IFSRLNTIKA
EILPNYMPPP EIATNGTGDE TVIDRSDIPF LPFPRSNMLM VIPLTSECRV IYNMENMIGR
GHYGTVYKGH LEFNDKDQPR EQVAIKMLNT MQVSTDFHRE IGIMRTLSHP NIVKFKYWAE
KSHCIIMEYL QSGSFDIYLR FTAPNLNNPR LVSFALDIAN GMKYLSDMGL IHRDLAARNI
LVDHNGDGDC VKISDFGLAQ FANSDGYYYA KSKRDIPIRW YSPEAISTCR FSSYSDVWSY
GVTLFEMFSR GEEPNLVPIQ TSQEDFLNRL QSGERLNRPA SCPDFIYDLM QLCWHATPRS
RPSFATIVDI ITREVATKVT HPTDGHQSPP NQPTDAE
