TUTL_DROME
ID TUTL_DROME Reviewed; 1531 AA.
AC Q967D7; Q6NR34; Q8IQ17; Q967D8; Q967D9; Q967E0; Q9VQY0; Q9VQY1; Q9VQY2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein turtle;
GN Name=tutl; ORFNames=CG15427;
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] (ISOFORMS 1; 3 AND 4), FUNCTION, DEVELOPMENTAL
RP STAGE, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11312296; DOI=10.1523/jneurosci.21-09-03113.2001;
RA Bodily K.D., Morrison C.M., Renden R.B., Broadie K.;
RT "A novel member of the Ig superfamily, turtle, is a CNS-specific protein
RT required for coordinated motor control.";
RL J. Neurosci. 21:3113-3125(2001).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM 2).
RC STRAIN=Berkeley;
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH BDL, AND DISRUPTION PHENOTYPE.
RX PubMed=24174674; DOI=10.1523/jneurosci.1878-13.2013;
RA Cameron S., Chang W.T., Chen Y., Zhou Y., Taran S., Rao Y.;
RT "Visual circuit assembly requires fine tuning of the novel Ig transmembrane
RT protein Borderless.";
RL J. Neurosci. 33:17413-17421(2013).
CC -!- FUNCTION: Essential protein that plays a role in the establishment of
CC coordinated motor control (PubMed:11312296). In the developing eye,
CC involved in axonal targeting of the R7 photoreceptor (PubMed:24174674).
CC {ECO:0000269|PubMed:11312296}.
CC -!- SUBUNIT: Interacts with bdl. {ECO:0000269|PubMed:24174674}.
CC -!- INTERACTION:
CC Q967D7; Q9VQW7: ed; NbExp=2; IntAct=EBI-3487134, EBI-85823;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=4;
CC IsoId=Q967D7-1; Sequence=Displayed;
CC Name=2; Synonyms=D;
CC IsoId=Q967D7-2; Sequence=VSP_028407;
CC Name=3; Synonyms=A;
CC IsoId=Q967D7-3; Sequence=VSP_028401, VSP_028402;
CC Name=4; Synonyms=C;
CC IsoId=Q967D7-4; Sequence=VSP_028403, VSP_028406;
CC Name=5; Synonyms=E;
CC IsoId=Q967D7-5; Sequence=VSP_028404, VSP_028405;
CC -!- TISSUE SPECIFICITY: Exclusively expressed in the central nervous
CC system. {ECO:0000269|PubMed:11312296}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the central nervous system
CC from segregation of neuronal precursors through the end of development.
CC Also detected in cephalic sensory structures.
CC {ECO:0000269|PubMed:11312296}.
CC -!- DISRUPTION PHENOTYPE: Adult mutant flies are unable to fly and roll
CC over when inverted, explaining the name 'turtle' (PubMed:11312296). In
CC the eye, axonal tiling of the R7 photoreceptor is defective in
CC approximately 22% of axons (PubMed:24174674). Double knockouts of tutl
CC and bdl rescue the R7 axonal tiling defect (PubMed:24174674).
CC {ECO:0000269|PubMed:11312296, ECO:0000269|PubMed:24174674}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Turtle family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC39162.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ312132; CAC39161.1; -; mRNA.
DR EMBL; AJ312133; CAC39162.1; ALT_SEQ; mRNA.
DR EMBL; AJ312134; CAC39163.1; -; mRNA.
DR EMBL; AJ312135; CAC39164.1; -; mRNA.
DR EMBL; AE014134; AAF51029.3; -; Genomic_DNA.
DR EMBL; AE014134; AAF51030.3; -; Genomic_DNA.
DR EMBL; AE014134; AAF51031.3; -; Genomic_DNA.
DR EMBL; AE014134; AAN11173.1; -; Genomic_DNA.
DR EMBL; BT010247; AAQ23565.1; -; mRNA.
DR RefSeq; NP_001162869.1; NM_001169398.1. [Q967D7-2]
DR RefSeq; NP_524866.4; NM_080127.6. [Q967D7-5]
DR RefSeq; NP_722967.2; NM_164576.4. [Q967D7-2]
DR RefSeq; NP_722968.1; NM_164577.3. [Q967D7-4]
DR RefSeq; NP_722969.1; NM_164578.4. [Q967D7-3]
DR AlphaFoldDB; Q967D7; -.
DR SMR; Q967D7; -.
DR BioGRID; 70063; 8.
DR IntAct; Q967D7; 2.
DR STRING; 7227.FBpp0305668; -.
DR PaxDb; Q967D7; -.
DR PRIDE; Q967D7; -.
DR EnsemblMetazoa; FBtr0089268; FBpp0088325; FBgn0010473. [Q967D7-3]
DR EnsemblMetazoa; FBtr0089269; FBpp0088326; FBgn0010473. [Q967D7-4]
DR EnsemblMetazoa; FBtr0089270; FBpp0088327; FBgn0010473. [Q967D7-2]
DR EnsemblMetazoa; FBtr0089271; FBpp0088328; FBgn0010473. [Q967D7-5]
DR EnsemblMetazoa; FBtr0301864; FBpp0291078; FBgn0010473. [Q967D7-2]
DR GeneID; 46015; -.
DR KEGG; dme:Dmel_CG15427; -.
DR UCSC; CG15427-RA; d. melanogaster. [Q967D7-1]
DR CTD; 46015; -.
DR FlyBase; FBgn0010473; tutl.
DR VEuPathDB; VectorBase:FBgn0010473; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000170870; -.
DR InParanoid; Q967D7; -.
DR OMA; FWHCHAN; -.
DR PhylomeDB; Q967D7; -.
DR Reactome; R-DME-1474228; Degradation of the extracellular matrix.
DR Reactome; R-DME-210991; Basigin interactions.
DR Reactome; R-DME-216083; Integrin cell surface interactions.
DR Reactome; R-DME-376172; DSCAM interactions.
DR Reactome; R-DME-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR Reactome; R-DME-433692; Proton-coupled monocarboxylate transport.
DR Reactome; R-DME-70268; Pyruvate metabolism.
DR Reactome; R-DME-9749641; Aspirin ADME.
DR BioGRID-ORCS; 46015; 0 hits in 3 CRISPR screens.
DR ChiTaRS; tutl; fly.
DR GenomeRNAi; 46015; -.
DR PRO; PR:Q967D7; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0010473; Expressed in brain and 32 other tissues.
DR ExpressionAtlas; Q967D7; baseline and differential.
DR Genevisible; Q967D7; DM.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IPI:FlyBase.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0016199; P:axon midline choice point recognition; IMP:FlyBase.
DR GO; GO:0007414; P:axonal defasciculation; IMP:FlyBase.
DR GO; GO:0070593; P:dendrite self-avoidance; IMP:FlyBase.
DR GO; GO:0007629; P:flight behavior; IMP:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0030537; P:larval behavior; IMP:FlyBase.
DR GO; GO:0007638; P:mechanosensory behavior; IMP:FlyBase.
DR GO; GO:0045467; P:R7 cell development; IMP:FlyBase.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:FlyBase.
DR GO; GO:0008039; P:synaptic target recognition; IMP:FlyBase.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 7.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SMART; SM00406; IGv; 3.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Immunoglobulin domain; Membrane;
KW Neurogenesis; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1531
FT /note="Protein turtle"
FT /id="PRO_0000306106"
FT TOPO_DOM 1..858
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 859..879
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 880..1531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 132..243
FT /note="Ig-like C2-type 1"
FT DOMAIN 253..340
FT /note="Ig-like C2-type 2"
FT DOMAIN 344..436
FT /note="Ig-like C2-type 3"
FT DOMAIN 440..529
FT /note="Ig-like C2-type 4"
FT DOMAIN 536..624
FT /note="Ig-like C2-type 5"
FT DOMAIN 632..728
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 760..851
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 19..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 150..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 275..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 366..419
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 462..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 558..611
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 349..377
FT /note="VPPTNQTKLEGEKVIFSCEAKAMPGNVTV -> DKAAPDKHTRTKSKSNVVN
FT ERLTIRVSPN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11312296"
FT /id="VSP_028401"
FT VAR_SEQ 378..1531
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11312296"
FT /id="VSP_028402"
FT VAR_SEQ 893..903
FT /note="EFNMVACRITD -> GNTEAKANTHT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11312296"
FT /id="VSP_028403"
FT VAR_SEQ 894..902
FT /note="FNMVACRIT -> IIRLQSSTW (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_028404"
FT VAR_SEQ 903..1531
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_028405"
FT VAR_SEQ 904..1531
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11312296"
FT /id="VSP_028406"
FT VAR_SEQ 931..970
FT /note="NNTEHYRDYESVFIVPGHPVIIKIVQTNPNIKSNRHSHCH -> KYKQTRIS
FT SLTAILIAI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_028407"
FT CONFLICT 731
FT /note="A -> P (in Ref. 1; CAC39163)"
FT /evidence="ECO:0000305"
FT CONFLICT 796
FT /note="T -> M (in Ref. 4; AAQ23565)"
FT /evidence="ECO:0000305"
FT CONFLICT 904
FT /note="A -> T (in Ref. 4; AAQ23565)"
FT /evidence="ECO:0000305"
FT CONFLICT 1502
FT /note="D -> G (in Ref. 4; AAQ23565)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1531 AA; 170993 MW; BAAD00872B5237D0 CRC64;
MGVCADLGSH RWCRALSTQH NTEKSKEQQQ QSQPLEIPEQ RASKCRGDID RTTTTTIPAS
KTLTASPAKT AAFTVKTTRR RRSRRRAEGS SICVPIRRGQ GSTPTPTIQV LQFVLVSLLA
LLAKNAQAHN IPEDAVHITA ILGEGVIFNC HVEFPNDHPV PYVLQWDKKV SETGSDLPIY
IWYESYPEHI EEGYKGRVSR VSQDSPFGSA SLNLTNIRES DQGWYECKVV FLNRDPKQHK
NGTWFHLDVH APPRFSVTPE DIIYVNLGDS IILNCQADGT PTPEILWYKD ANPVDPSPTV
GIFNDGTELR ISTIRHEDIG EYTCIARNGE GQVSHTARVI IAGGAVIMVP PTNQTKLEGE
KVIFSCEAKA MPGNVTVRWY REGSPVREVA ALETRVTIRK DGSLIINPIK PDDSGQYLCE
VTNGIGDPQS ASAYLSVEYP AKVTFTPTVQ YLPFRLAGVV QCYIKSSPQL QYVTWTKDKR
LLEPYQMKDI VVMANGSLLF TRVNEEHQGQ YACTPYNAQG TAGASGVMDV LVRKPPAFTV
EPETLYQRKV GDSVEMHCDA LEAEGTERPT IKWQRQEGEQ LTESQRNRIK ISGGNITIEN
LRREDFGYYQ CVVSNEVATL MAVTQLVIEG TQPHAPYNIT GKATESSITL QWLPGYSGGS
EYKQDYTIWF REAGVNDWQT ISVTPSGSTQ VTINGLASGT TYEFQVVGRN VLGDGMMSKV
MTVRTLEDAP AAPRNVKAAT QPPDSFFQLM PDEAGPKPGP PRNVSVTEVS NGFLITWQSP
LERAHIVKFY TIKYRTDAQW KTLNRGQIRP EETQYLVKNL VGGRTYYFRV LANSEKSYES
SDEVKFPVPA RVKHKAITAG VVGGILFFIV AIILSVCAVK ICNKRKRRKQ EKEFNMVACR
ITDARNIAAN NHHLHNRSTG SISSGQVPLK NNTEHYRDYE SVFIVPGHPV IIKIVQTNPN
IKSNRHSHCH LHWIWPPDRC TNCHSIYSSP NLEDGDEDDG GGGRRRSVSR IQRSLDGRFV
LDVEGVSKLG YSQQTLESGN VDVVDGGLFE RRNSNVSQKS SSDDGGFLSR RNFITARASW
RRPLVASSSQ LSLQSAADSA RGFLQGLLKI GAKQSAVPPN SQSYFDEAVS GARYQNVLRP
YTSSNNLYGN ADRSRPLHIN TISGSLSQQQ QLYTPSRISR IFSSSPQQLQ PHHQQLLLSS
GGSGAYPTHF SDLSTVYPPN SAERSSHNLS SRYRYYSQEL PSLRTIQEET RRQQQQKQHP
LEDHFVPLQL PSPPSWRSYY QSQASYRPRT RWYPRHHSRL FSNRQQQHEM LSPLPQLNLN
LRNSMNPGGL EASPESRSSS SGFGSKNTSN HPGSTSEWRL LPPYRAPPSP PKHSGYFGGQ
QAQGQTPHGS YSYPRATTPP YTMAHWLEMI SRLNAATDSN LPKAPCPVDV GSVDGHYEFD
PATPTPSASS MLREDLNLHI DTHPYHHHTL GPLSGSLLHS HAPYGGGARK QRSLPAHLPR
YDNVEVRLQA MREEFYAYRK RQAMQQMESV C
