MAS_DROME
ID MAS_DROME Reviewed; 1047 AA.
AC Q9VZH2; M9PE44; Q24019; Q960I5;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Protein masquerade {ECO:0000303|PubMed:7851790};
DE Flags: Precursor;
GN Name=mas {ECO:0000303|PubMed:7851790, ECO:0000312|FlyBase:FBgn0011653};
GN Synonyms=c-SPH79 {ECO:0000312|EMBL:AAF47850.1},
GN SPH79 {ECO:0000312|EMBL:AAF47850.1};
GN ORFNames=CG15002 {ECO:0000312|EMBL:AAF47850.1,
GN ECO:0000312|FlyBase:FBgn0011653};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:AAC46512.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA], FUNCTION,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PROTEOLYTIC CLEAVAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=7851790; DOI=10.1101/gad.9.2.139;
RA Murugasu-Oei B., Rodrigues V., Yang X., Chia W.;
RT "Masquerade: a novel secreted serine protease-like molecule is required for
RT somatic muscle attachment in the Drosophila embryo.";
RL Genes Dev. 9:139-154(1995).
RN [2] {ECO:0000312|Proteomes:UP000000803}
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] {ECO:0000312|Proteomes:UP000000803}
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:0000312|EMBL:AAK93468.1, ECO:0000312|EMBL:AAN71352.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo, Larva, and Pupae;
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}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=8817456; DOI=10.1016/0925-4773(96)00537-0;
RA Murugasu-Oei B., Balakrishnan R., Yang X., Chia W., Rodrigues V.;
RT "Mutations in masquerade, a novel serine-protease-like molecule, affect
RT axonal guidance and taste behavior in Drosophila.";
RL Mech. Dev. 57:91-101(1996).
CC -!- FUNCTION: In embryogenesis, has a role in somatic muscle attachment and
CC in the development of axonal pathways probably by stabilizing cell-
CC matrix adhesion and/or by acting as a competitive antagonist of serine
CC proteases. {ECO:0000269|PubMed:7851790, ECO:0000269|PubMed:8817456}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7851790}. Cell
CC projection, axon {ECO:0000269|PubMed:7851790,
CC ECO:0000269|PubMed:8817456}. Note=Localizes to vesicle-like structures
CC in epidermal cells. {ECO:0000305|PubMed:7851790,
CC ECO:0000305|PubMed:8817456}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000312|FlyBase:FBgn0011653};
CC IsoId=Q9VZH2-1; Sequence=Displayed;
CC Name=C {ECO:0000312|FlyBase:FBgn0011653};
CC IsoId=Q9VZH2-2; Sequence=VSP_059330;
CC -!- DEVELOPMENTAL STAGE: In embryos, from stage 14 till stage 17, expressed
CC in epidermal cells, tracheal system and denticle belts (at protein
CC level) (PubMed:7851790). In larva and in early pupa, expressed in brain
CC cells along the ventral midline, in cell bodies in the cellular cortex
CC of the ventral nerve cord, in cells contributing to the perineum around
CC the cerebral hemispheres and in axons of the longitudinal connectives
CC of the central nervous system (CNS); at low level, expressed throughout
CC the antennal disk (at protein level) (PubMed:7851790, PubMed:8817456).
CC In pupae, expressed in pupal appendages and body epidermis, in the
CC proboscis and pseudotrachea (at protein level) (PubMed:8817456).
CC Expressed in embryos; from stage 11 until the end of stage 13 expressed
CC in small cells along the midline of the central nervous system; at
CC state 12, expressed in the epidermis; from stage 13 onwards, expressed
CC in the epidermal cells in particular in the anterior border of each
CC segment; from stage 14-17, detected in the cells of the tracheal system
CC (PubMed:7851790). Detected in larva and pupa, but not in adult flies
CC (PubMed:7851790, PubMed:8817456). {ECO:0000269|PubMed:7851790,
CC ECO:0000269|PubMed:8817456}.
CC -!- DOMAIN: The CLIP domain consists of 37-55 residues which are 'knitted'
CC together usually by 3 conserved disulfide bonds forming a clip-like
CC compact structure. {ECO:0000305}.
CC -!- PTM: Proteolytically cleaved and thereafter secreted.
CC {ECO:0000269|PubMed:7851790}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal as a result of neuronal defects
CC in the central nervous system (CNS) and peripheral nervous system (PNS)
CC from stage 15, and defective muscle attachment from stage 16
CC (PubMed:7851790, PubMed:8817456). Defects in the CNS include stalling
CC of the growth cones of pioneer axons of anterior and posterior corner
CC cells (aCC and pCC) leading to abnormalities in the horizontal
CC commissures and discontinuities in the longitudinal connectives
CC respectively (PubMed:8817456). Defects in the PNS include defects in
CC the location of the sense organs and in their projections in the
CC sensory nerves, including missing neurons and more often defects in the
CC axonal paths with erroneous connections with the ventral ganglia
CC (PubMed:8817456). Defects in muscle attachment include the appearance
CC of myospheroid-like bodies and the collapse of lateral transverse
CC muscles 1-3 (PubMed:7851790). {ECO:0000269|PubMed:7851790,
CC ECO:0000269|PubMed:8817456}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Ser residue within the catalytic triad
CC which is replaced by a Gly residue, probably resulting in a loss of
CC proteolytic activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK93468.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U18130; AAC46512.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47850.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94103.1; -; Genomic_DNA.
DR EMBL; AY052044; AAK93468.1; ALT_INIT; mRNA.
DR EMBL; BT001597; AAN71352.1; -; mRNA.
DR PIR; A55617; A55617.
DR RefSeq; NP_001261408.1; NM_001274479.1. [Q9VZH2-2]
DR RefSeq; NP_523919.1; NM_079195.3. [Q9VZH2-1]
DR AlphaFoldDB; Q9VZH2; -.
DR SMR; Q9VZH2; -.
DR STRING; 7227.FBpp0073116; -.
DR MEROPS; S01.024; -.
DR GlyGen; Q9VZH2; 6 sites.
DR PaxDb; Q9VZH2; -.
DR EnsemblMetazoa; FBtr0073260; FBpp0073116; FBgn0011653. [Q9VZH2-1]
DR EnsemblMetazoa; FBtr0332659; FBpp0304905; FBgn0011653. [Q9VZH2-2]
DR GeneID; 38499; -.
DR KEGG; dme:Dmel_CG15002; -.
DR UCSC; CG15002-RB; d. melanogaster. [Q9VZH2-1]
DR CTD; 38499; -.
DR FlyBase; FBgn0011653; mas.
DR VEuPathDB; VectorBase:FBgn0011653; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000172378; -.
DR InParanoid; Q9VZH2; -.
DR OMA; CIENAPG; -.
DR PhylomeDB; Q9VZH2; -.
DR BioGRID-ORCS; 38499; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38499; -.
DR PRO; PR:Q9VZH2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0011653; Expressed in eye disc (Drosophila) and 33 other tissues.
DR ExpressionAtlas; Q9VZH2; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0061564; P:axon development; IMP:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; IMP:UniProtKB.
DR GO; GO:0016203; P:muscle attachment; IMP:UniProtKB.
DR GO; GO:0106030; P:neuron projection fasciculation; IMP:UniProtKB.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR InterPro; IPR040479; CLIP_SPH_mas.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR Pfam; PF18398; CLIP_SPH_mas; 5.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Developmental protein;
KW Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Serine protease homolog; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1047
FT /note="Protein masquerade"
FT /evidence="ECO:0000305|PubMed:7851790"
FT /id="PRO_5010686327"
FT REGION 54..87
FT /note="CLIP 1"
FT /evidence="ECO:0000255"
FT REGION 98..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..224
FT /note="CLIP 2"
FT /evidence="ECO:0000255"
FT REGION 252..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..374
FT /note="CLIP 3"
FT /evidence="ECO:0000255"
FT REGION 376..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..492
FT /note="CLIP 4"
FT /evidence="ECO:0000255"
FT REGION 498..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..567
FT /note="CLIP 5"
FT /evidence="ECO:0000255"
FT REGION 583..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..1043
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT COMPBIAS 98..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..324
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..417
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..527
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..662
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 794
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 56..85
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 60..78
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 69..86
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 193..222
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 197..216
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 206..223
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 344..372
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 348..366
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 357..373
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 458..490
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 462..484
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 471..491
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 533..565
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 537..558
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 546..566
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 682..916
FT /evidence="ECO:0000250|UniProtKB:Q9VB68"
FT DISULFID 829..845
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 930..1001
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 961..981
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 991..1019
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 191..192
FT /note="KD -> N (in isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_059330"
FT CONFLICT 158..160
FT /note="ATV -> PTA (in Ref. 1; AAC46512)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="N -> K (in Ref. 1; AAC46512)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="S -> C (in Ref. 1; AAC46512)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="E -> G (in Ref. 1; AAC46512)"
FT /evidence="ECO:0000305"
FT CONFLICT 647..648
FT /note="SG -> WP (in Ref. 1; AAC46512)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="R -> C (in Ref. 1; AAC46512)"
FT /evidence="ECO:0000305"
FT CONFLICT 936
FT /note="G -> R (in Ref. 1; AAC46512)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1047 AA; 111564 MW; D1FBB8E6E6030B55 CRC64;
MPRHSSTMSR LVLPLIFSIL LVSKPSPSQA QDESLAGSFL SGLLDTITST ADSKDCPGVC
VHTLATLICY EVLDDVACPS PSMKCCIENA PAGKNATAVR ATTTPKTTTT ASTTTTQRTT
TTVATTSTTK RTTTTSTTPK PKPKPQTKRP ATSSTTKATV ATTKKPSTTK KVATAKPKDK
EEATKADDAN KDCTGVCVAD RIAEYCEAYL TSDGLCKEGT KCCVSLDEYS NGKLPKDIYI
PAKHMSNLKP NQTLSEKSAP AKSSSTSTTS TTTTTSTTTT PEPARINNSS PKPTKHKKHP
TTTTTEAAEE EEEQETEEDG EEEEPPLSNK LKSGQGQGQV LKECEGECMN GIFAIFCDDI
DSDAFCPGEE SCCVTGGASE ATPSSKAPPT KPAIKHAPKP AAKPARPASP PPAPPSSTSG
GGGGGDFLSQ IISFAESTLN SPSPPPPPPQ APIQVPRCPG FCLLNIMAAF CERPSVLVST
PTTCAKGSVC CDNSRAGAPK PKLPPPTPSP TASPTAPPYV LPNTPSPDPR EECPGSCIVS
LLSFTCFKNA EMTDLFRCKR SGQICCAPKS KILEKQQFQT RNDTAYYPAP PPPPIGPPQA
YPPQTPPYSY MNNPPPQGPP PQMAPHHPNP YQPPPPAPNY ADYYPVSGPG LPPQPQPPMT
TPPTTTTTTT TPRPHVYSKY VCGVKGTLRT GRSQALSFVS YARAKYGVQR TARQMTSAAG
YSPNFNKSNE RLVLGSAIVP IQIHNDKLGD LVESSSLQSN QLRSYHNHQA QADQPDLVYP
EYYQQRSLYG LQSNFSGRRR ARVVGGEDGE NGEWCWQVAL INSLNQYLCG AALIGTQWVL
TAAHCVTNIV RSGDAIYVRV GDYDLTRKYG SPGAQTLRVA TTYIHHNHNS QTLDNDIALL
KLHGQAELRD GVCLVCLPAR GVSHAAGKRC TVTGYGYMGE AGPIPLRVRE AEIPIVSDTE
CIRKVNAVTE KIFILPASSF CAGGEEGHDA CQGDGGGPLV CQDDGFYELA GLVSWGFGCG
RQDVPGVYVK TSSFIGWINQ IISVNNL
