MED13_DROME
ID MED13_DROME Reviewed; 2618 AA.
AC Q7KTX8; Q95RI1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 13;
DE AltName: Full=Mediator complex subunit 13;
DE AltName: Full=Mediator complex subunit Skuld;
DE AltName: Full=Protein blind spot;
DE AltName: Full=Protein poils aux pattes;
DE AltName: Full=dTRAP240;
GN Name=skd; Synonyms=bli, Med13, pap, Trap240; ORFNames=CG9936;
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 [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=11090137; DOI=10.1101/gad.17900;
RA Boube M., Faucher C., Joulia L., Cribbs D.L., Bourbon H.-M.;
RT "Drosophila homologs of transcriptional mediator complex subunits are
RT required for adult cell and segment identity specification.";
RL Genes Dev. 14:2906-2917(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=11171343; DOI=10.1242/dev.128.4.603;
RA Treisman J.E.;
RT "Drosophila homologues of the transcriptional coactivation complex subunits
RT TRAP240 and TRAP230 are required for identical processes in eye-antennal
RT disc development.";
RL Development 128:603-615(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nairz K., Hafen E.;
RT "Isolation of flytrap (pap), the Drosophila TRAP240 homologue.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1556-2618.
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [7]
RP FUNCTION, INTERACTION WITH KTO, AND SUBCELLULAR LOCATION.
RX PubMed=12835386; DOI=10.1242/dev.00607;
RA Janody F., Martirosyan Z., Benlali A., Treisman J.E.;
RT "Two subunits of the Drosophila mediator complex act together to control
RT cell affinity.";
RL Development 130:3691-3701(2003).
RN [8]
RP FUNCTION.
RX PubMed=16751183; DOI=10.1101/gad.1418806;
RA Marr M.T. II, Isogai Y., Wright K.J., Tjian R.;
RT "Coactivator cross-talk specifies transcriptional output.";
RL Genes Dev. 20:1458-1469(2006).
RN [9]
RP FUNCTION, AND INTERACTION WITH CYCC; CDK8 AND KTO.
RX PubMed=17290221; DOI=10.1038/sj.emboj.7601566;
RA Loncle N., Boube M., Joulia L., Boschiero C., Werner M., Cribbs D.L.,
RA Bourbon H.-M.;
RT "Distinct roles for Mediator Cdk8 module subunits in Drosophila
RT development.";
RL EMBO J. 26:1045-1054(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-571; THR-575; SER-2472 AND
RP SER-2475, AND 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: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex with RNA polymerase II
CC and the general transcription factors (By similarity). Required for leg
CC and eye development and macrochaete specification or differentiation.
CC Negatively regulates sex comb development. Required for activated
CC transcription of the MtnB and MtnD genes. {ECO:0000250,
CC ECO:0000269|PubMed:11090137, ECO:0000269|PubMed:11171343,
CC ECO:0000269|PubMed:12835386, ECO:0000269|PubMed:16751183,
CC ECO:0000269|PubMed:17290221}.
CC -!- SUBUNIT: Component of the Cdk8 module of the Mediator complex, composed
CC of CycC, Cdk8, kto and skd.
CC -!- INTERACTION:
CC Q7KTX8; P25008: CycC; NbExp=2; IntAct=EBI-110730, EBI-195485;
CC Q7KTX8; Q9V9W8: pygo; NbExp=2; IntAct=EBI-110730, EBI-152653;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11090137,
CC ECO:0000269|PubMed:12835386}.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout development.
CC {ECO:0000269|PubMed:11090137}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 13 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28909.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF227214; AAF43021.1; -; mRNA.
DR EMBL; AF227215; AAF43172.1; -; Genomic_DNA.
DR EMBL; AF324425; AAG48327.1; -; mRNA.
DR EMBL; AF226855; AAF36691.1; -; mRNA.
DR EMBL; AE014296; AAN12148.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12149.1; -; Genomic_DNA.
DR EMBL; AY061361; AAL28909.1; ALT_INIT; mRNA.
DR RefSeq; NP_524653.1; NM_079914.3.
DR RefSeq; NP_730590.1; NM_168879.3.
DR AlphaFoldDB; Q7KTX8; -.
DR BioGRID; 68707; 40.
DR DIP; DIP-29988N; -.
DR IntAct; Q7KTX8; 35.
DR MINT; Q7KTX8; -.
DR STRING; 7227.FBpp0111743; -.
DR iPTMnet; Q7KTX8; -.
DR PaxDb; Q7KTX8; -.
DR EnsemblMetazoa; FBtr0078328; FBpp0077984; FBgn0003415.
DR EnsemblMetazoa; FBtr0078329; FBpp0077985; FBgn0003415.
DR GeneID; 43906; -.
DR KEGG; dme:Dmel_CG9936; -.
DR CTD; 43906; -.
DR FlyBase; FBgn0003415; skd.
DR VEuPathDB; VectorBase:FBgn0003415; -.
DR eggNOG; KOG3600; Eukaryota.
DR GeneTree; ENSGT00390000013680; -.
DR InParanoid; Q7KTX8; -.
DR OrthoDB; 177884at2759; -.
DR SignaLink; Q7KTX8; -.
DR BioGRID-ORCS; 43906; 0 hits in 3 CRISPR screens.
DR ChiTaRS; skd; fly.
DR GenomeRNAi; 43906; -.
DR PRO; PR:Q7KTX8; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0003415; Expressed in cleaving embryo and 42 other tissues.
DR ExpressionAtlas; Q7KTX8; baseline and differential.
DR Genevisible; Q7KTX8; DM.
DR GO; GO:0070847; C:core mediator complex; IPI:FlyBase.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR GO; GO:0045165; P:cell fate commitment; IGI:FlyBase.
DR GO; GO:0022416; P:chaeta development; IMP:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:FlyBase.
DR GO; GO:0036011; P:imaginal disc-derived leg segmentation; IMP:FlyBase.
DR GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045498; P:sex comb development; IMP:FlyBase.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:FlyBase.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IGI:FlyBase.
DR InterPro; IPR009401; Med13_C.
DR InterPro; IPR021643; Mediator_Med13_N.
DR InterPro; IPR041285; MID_MedPIWI.
DR Pfam; PF06333; Med13_C; 1.
DR Pfam; PF11597; Med13_N; 1.
DR Pfam; PF18296; MID_MedPIWI; 1.
PE 1: Evidence at protein level;
KW Activator; Developmental protein; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..2618
FT /note="Mediator of RNA polymerase II transcription subunit
FT 13"
FT /id="PRO_0000314242"
FT REGION 232..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 970..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1268..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1521..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1614..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1985..2060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..957
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1989..2017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 571
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 575
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2472
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2475
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 2618 AA; 280024 MW; 735A8A502076844E CRC64;
MTHQNHQTNG ASLEDCHTNF YALTDLCGIK WRKFVNGERP NASSDPLADP ILRSYSRCIQ
ADMLCVWRRV QSTKTDHADP NALTFEMTTS TKVHPPLSLA AAKELWIFWY GEEPDLSELV
DAELLRVAAN QALWNGTWKG ALTYECRSLL FKALHNLMER FVLTKDIVRF GKWFVQPCTS
SDRLFGRSSQ HLSFSFTFFV HGDTVCASID LREHPAVRPL TKEHLTEAAA AFAAASSPPG
SNGSAASAGG AVPNPGQDPN GASMDGLDGG EGAAKAAPPP HARKVMLAPF GIAGILTGNS
YKASDPIAEK ILEDWASFFP LCNKDNTDVP PVVEVVSGGH KMYHPTNYVL VTDLDDMEHM
EFVEMQKMQS SVAGAAAESA VLASLSCPPG AASAPSSMGA APSATAVPLG PASLNAPALA
GAGVGATASS AAKEISRKAA PQAVSALERL AFQPYYDQRP TSGFTFNTNN THIPASAAVE
MPERTWQDCV MNTLHVDAAA AAAAVASSTP ASGTGSLSAD GDENEQNKPP QDSKQLVQQQ
IQQQQQRQKL WNFVDPMQKA PCICTKHLGN TPHGTPHGGA STYSRNSLGG DSSMPVASVE
SPATPAPSPH PNSAHSQPTS VPPAEQLLNM SPHAPTSVSN LQQPPTPIDH LLDKNTPAPT
PTDQHDSKSI TASPYVHQTP SVEPPSYTDH AAGGGPAGGQ GLGTGPGSVP AQQPATPTAA
TSAGGAGSGG PSNAIGANAV GTISVKKLEM QQQTPSAAMA IKQEPGAQGR GVGGVTSTTE
ALNNFKRLYN PPKLTLKDPD SFYDEEWLKE VIYDFQYQEY WDYSTVKRPK MEKQRRPRYA
KNLYEGQNHV KPVMPSPGSV YGSQLLSLDE SASQAGGRGG GGQAAGSSGG GLVGIANSTA
SGSDVEADGS SFFQGLNIKT EPGLHSPSCK ETSKSSGGNS SGGGSGSGGN LFTAEGLNPS
LNDLEQLFET SSNDECSSVQ IHTPPDSNNP SNGGCSAVTN TIEDLKRSTA VASAAVAAAA
AAAASGAGNI QAEDLTKMFP TPPSHEQQHP NSSPCQTDVV MTDLSVDTTT TIITSSITTT
CNTTITSSIN TTTTACSNPS NSIMLAAAQA PVTVVAIQTV SKMVKQEYNL ELGSPMEEPI
NDWDYVYRPP QQEKFVGSTR YAPLTNLPSQ TQPPLTLPTG CFYQPTWSSH KSRAATLAKA
AAAQQQQHQK HQALQQRIQL HQQKLQQLQL QNQQQQQAAA AAAAAASGGV GHQKHQHQHL
HDLLSAAPRT PLTPSTVPQP LSSGGSQYLL NQLNCPQAPP GASMQQLMHR AGMSPISPGP
GMGPYAARSS PMSRATPTHP PPPYPYDLAV ASPATSTSSY LNRPLHSQEH PHMHGLGGGA
TGVVGHGTGG GGHMGMVAYT GDAGIVSGGT AMAAGSSSLL QELPEVNSVL VNILLYDTAL
NVFRDHNFDS SSVCVCNADT QKIGNIRGAD SGVYVPLPGV SFNPFPSGAG GALAGQRMLN
GPSSAGFGGM RMISAFGGSP ASASMPGAGS GHGHGPNGGS NSSSCTPPSS NPHITGYVDD
DPVECTCGFS AVVNRRLSHR AGLFYEDEVE ITGIADDPGR NKQPTLLSII QSLSRKNQNK
QGPGETSSAL DKIGAGGLPN GQLEQLGHAV FDLLLDQCSI IQTSSSSVHR ALQSHRRRMS
RQRRIFGNNG APTASLASIA NVLEFMDAHD VISLALEQSR LAFENQRMDN MMDFHGNGSS
SSHQQQQLTA FHAPPPALRH KLAGIGAGRL TVHKWPYLPV GFTRSNKEIV RTMNAIQPML
QNAFHCKSRG GSGSKDASSY NTVSGPLTWR QFHRLAGRAS GQCEPQPIPS VVVGYEKDWI
SVAPHSIHYW DKFLLEPYSY ARDVVYVVVC PDNEHVVNCT RSYFRELSST YEMCKLGKHT
PIRGWDGFLQ VGAARNNVPA DRETTPLDDW LRTLEHAALA EQIRRYAVAF IHQLAPYLSR
VPNDKTLLNP PDGSGNSHSK GGSSCSSNSS SVSGLPGGDL PTDNIKLEPG TEPQVQPMET
NEIKQEPGVG KGGTAAGETK PTLILGDPLG MGETLEDINP SAIVLYVVNP FTFASDSCEL
ERLALIALLR CYAELLKAVP DSVRSQMNIQ IISLESVMEL GPCGNRKRFS DEIRCLALNI
FSQCRRHLVH AQSVKSLTGF GTAANMEAFL KTKDEPNRRA YKMYTAPFVL APMHERNDKT
DFSRSAGSMH GQNEHRYSVM YCNYCLSEDQ AWLLATATDE RGEMLEKICI NIDVPNRARR
RKAPARYVAL KKLMDFIMGI ISQTSQMWRL VIGRIGRIGH SELKSWSFLL SKQQLQKASK
QFKDMCKQCT LMYPPTILSA CLVTLEPDAK LRVMPDQFTP DERFSQISMQ NPLATPQDVT
CTHILVFPTS AVCAPFTRQF QNEPQVDDDF LTFEEEGNED FSDADIGDLF WDTHMDRVSN
HGSPGRMDDN RSWQSAGGNN FKCTPPQEVE EVGSLNQQPI SVGYMVSTAP TGRMPAWFWS
ACPHLEDVCP VFLKTALHLH VPSIQSADDI LNSTNAHQSG NDHPLDSNLT ADVLRFVLEG
YNALSWLALD SNTHDRLSCL PINVQTLMDL YYLTAAIA
