GNPTA_DANRE
ID GNPTA_DANRE Reviewed; 1219 AA.
AC Q5RGJ8; Q568G1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=N-acetylglucosamine-1-phosphotransferase subunits alpha/beta;
DE EC=2.7.8.17 {ECO:0000250|UniProtKB:Q3T906};
DE AltName: Full=GlcNAc-1-phosphotransferase subunits alpha/beta;
DE AltName: Full=Stealth protein gnptab;
DE AltName: Full=UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta;
DE Contains:
DE RecName: Full=N-acetylglucosamine-1-phosphotransferase subunit alpha;
DE Contains:
DE RecName: Full=N-acetylglucosamine-1-phosphotransferase subunit beta;
DE Flags: Precursor;
GN Name=gnptab; Synonyms=gnpta; ORFNames=si:ch211-234f20.3, zgc:122985;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-748.
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION AS A STEALTH PROTEIN, AND PREDICTION OF FUNCTION.
RX PubMed=16299590; DOI=10.1371/journal.pcbi.0010063;
RA Sperisen P., Schmid C.D., Bucher P., Zilian O.;
RT "Stealth proteins: in silico identification of a novel protein family
RT rendering bacterial pathogens invisible to host immune defense.";
RL PLoS Comput. Biol. 1:492-499(2005).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=19834066; DOI=10.2353/ajpath.2009.090210;
RA Flanagan-Steet H., Sias C., Steet R.;
RT "Altered chondrocyte differentiation and extracellular matrix homeostasis
RT in a zebrafish model for mucolipidosis II.";
RL Am. J. Pathol. 175:2063-2075(2009).
RN [5]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LYS-729.
RX PubMed=23733939; DOI=10.1073/pnas.1308453110;
RA Qian Y., Flanagan-Steet H., van Meel E., Steet R., Kornfeld S.A.;
RT "The DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N-
RT acetylglucosamine-1-phosphotransferase is a substrate recognition module.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:10246-10251(2013).
RN [6]
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-447 AND CYS-473.
RX PubMed=25505245; DOI=10.1074/jbc.m114.612507;
RA Qian Y., van Meel E., Flanagan-Steet H., Yox A., Steet R., Kornfeld S.;
RT "Analysis of mucolipidosis II/III GNPTAB missense mutations identifies
RT domains of UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase involved
RT in catalytic function and lysosomal enzyme recognition.";
RL J. Biol. Chem. 290:3045-3056(2015).
CC -!- FUNCTION: Catalyzes the formation of mannose 6-phosphate (M6P) markers
CC on high mannose type oligosaccharides in the Golgi apparatus. M6P
CC residues are required to bind to the M6P receptors (MPR), which mediate
CC the vesicular transport of lysosomal enzymes to the
CC endosomal/prelysosomal compartment. {ECO:0000250|UniProtKB:Q3T906}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-[alpha-D-mannosyl-(1->2)-alpha-D-mannosyl-(glycan)]-L-
CC asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) +
CC N(4)-[6-(N-acetyl-alpha-D-glucosaminyl-1-phospho)-alpha-D-mannosyl-
CC (1->2)-alpha-D-mannosyl-(glycan)]-L-asparaginyl-[protein] + UMP;
CC Xref=Rhea:RHEA:13581, Rhea:RHEA-COMP:14507, Rhea:RHEA-COMP:14508,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:140357, ChEBI:CHEBI:140369; EC=2.7.8.17;
CC Evidence={ECO:0000250|UniProtKB:Q3T906};
CC -!- SUBUNIT: Hexamer of two alpha, two beta and two gamma (GNPTG) subunits;
CC disulfide-linked. The alpha and/or the beta subunits of the enzyme
CC constitute the catalytic subunits. {ECO:0000250|UniProtKB:Q3T906}.
CC -!- SUBCELLULAR LOCATION: [N-acetylglucosamine-1-phosphotransferase subunit
CC alpha]: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q3T906};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q3T906}.
CC -!- SUBCELLULAR LOCATION: [N-acetylglucosamine-1-phosphotransferase subunit
CC beta]: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q3T906}; Single-
CC pass type II membrane protein {ECO:0000250|UniProtKB:Q3T906}.
CC -!- DOMAIN: The DMAP1-binding domain mediates substrate recognition. It
CC specifically recognizes a conformation-dependent protein determinant
CC present in acid hydrolases. {ECO:0000250|UniProtKB:Q3T906}.
CC -!- PTM: The alpha- and beta-subunits are generated by a proteolytic
CC cleavage by mbtps1 protease at the Gln-893-Asp-894 bond.
CC {ECO:0000250|UniProtKB:Q3T906}.
CC -!- DISRUPTION PHENOTYPE: Decreased mannose phosphorylation of lysosomal
CC acid hydrolases, craniofacial and cardiac defects. Impaired development
CC of pectoral fins and otic vesicles. Craniofacial defects are due to
CC changes in the timing and localization of both type II collagen and
CC sox9 expression, suggestive of an accelerated chondrocyte
CC differentiation program. Increased level of active cathepsin K (ctsk) 3
CC days post-fertilization (dpf) because of abnormal processing and
CC activation, leading to morphologic cartilage defects.
CC {ECO:0000269|PubMed:19834066, ECO:0000269|PubMed:23733939,
CC ECO:0000269|PubMed:25505245}.
CC -!- MISCELLANEOUS: Stealth proteins are part of a protein family that is
CC conserved from bacteria to higher eukaryotes. Family members were first
CC identified in microbes as proteins that help pathogens to elude the
CC host innate immune system. Microbial stealth proteins are most likely
CC involved in the biosynthesis of exopolysaccharides. Stealth proteins
CC are predicted to function as hexose-1-phosphoryltransferases.
CC -!- SIMILARITY: Belongs to the stealth family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH92871.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; BX890572; CAI11844.1; -; Genomic_DNA.
DR EMBL; BC092871; AAH92871.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001038233.1; NM_001044768.3.
DR AlphaFoldDB; Q5RGJ8; -.
DR SMR; Q5RGJ8; -.
DR STRING; 7955.ENSDARP00000040444; -.
DR PaxDb; Q5RGJ8; -.
DR Ensembl; ENSDART00000121714; ENSDARP00000106477; ENSDARG00000030153.
DR GeneID; 553365; -.
DR KEGG; dre:553365; -.
DR CTD; 79158; -.
DR ZFIN; ZDB-GENE-030131-4714; gnptab.
DR eggNOG; ENOG502QQMR; Eukaryota.
DR GeneTree; ENSGT00390000006747; -.
DR HOGENOM; CLU_002469_0_0_1; -.
DR InParanoid; Q5RGJ8; -.
DR PhylomeDB; Q5RGJ8; -.
DR PRO; PR:Q5RGJ8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000030153; Expressed in intestine and 26 other tissues.
DR ExpressionAtlas; Q5RGJ8; baseline.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003976; F:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity; IMP:UniProtKB.
DR GO; GO:0060348; P:bone development; IMP:ZFIN.
DR GO; GO:0046835; P:carbohydrate phosphorylation; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; IMP:ZFIN.
DR GO; GO:0002063; P:chondrocyte development; IMP:ZFIN.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:ZFIN.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:ZFIN.
DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR GO; GO:0016256; P:N-glycan processing to lysosome; IMP:UniProtKB.
DR InterPro; IPR010506; DMAP1-bd.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR041536; GNPTAB_reg.
DR InterPro; IPR035993; Notch-like_dom_sf.
DR InterPro; IPR000800; Notch_dom.
DR InterPro; IPR031358; Stealth_CR1.
DR InterPro; IPR021520; Stealth_CR2.
DR InterPro; IPR031357; Stealth_CR3.
DR InterPro; IPR031356; Stealth_CR4.
DR Pfam; PF06464; DMAP_binding; 1.
DR Pfam; PF18440; GlcNAc-1_reg; 1.
DR Pfam; PF00066; Notch; 2.
DR Pfam; PF17101; Stealth_CR1; 1.
DR Pfam; PF11380; Stealth_CR2; 1.
DR Pfam; PF17102; Stealth_CR3; 1.
DR Pfam; PF17103; Stealth_CR4; 1.
DR SMART; SM01137; DMAP_binding; 1.
DR SMART; SM00004; NL; 2.
DR SUPFAM; SSF90193; SSF90193; 1.
DR PROSITE; PS51912; DMAP1_BIND; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50258; LNR; 2.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..893
FT /note="N-acetylglucosamine-1-phosphotransferase subunit
FT alpha"
FT /id="PRO_0000227883"
FT CHAIN 894..1219
FT /note="N-acetylglucosamine-1-phosphotransferase subunit
FT beta"
FT /id="PRO_0000227884"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1180..1200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 443..478
FT /note="LNR 1"
FT REPEAT 508..538
FT /note="LNR 2"
FT DOMAIN 696..804
FT /note="DMAP1-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01260"
FT DOMAIN 970..1005
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 640..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 454
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 472
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 519
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 534
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 537
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 983
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 985
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 987
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 994
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 893..894
FT /note="Cleavage; by mbtps1"
FT /evidence="ECO:0000250"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 823
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 974
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1021
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1029
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1094
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 443..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 457..473
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 508..531
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 522..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT MUTAGEN 447
FT /note="C->Y: Partial loss of function due to loss of UDP-N-
FT acetylglucosamine-lysosomal-enzyme N-
FT acetylglucosaminephosphotransferase activity toward some
FT substrates."
FT /evidence="ECO:0000269|PubMed:25505245"
FT MUTAGEN 473
FT /note="C->S: Partial loss of function due to loss of UDP-N-
FT acetylglucosamine-lysosomal-enzyme N-
FT acetylglucosaminephosphotransferase activity toward some
FT substrates."
FT /evidence="ECO:0000269|PubMed:25505245"
FT MUTAGEN 729
FT /note="K->N: Loss of function due to loss of UDP-N-
FT acetylglucosamine-lysosomal-enzyme N-
FT acetylglucosaminephosphotransferase activity."
FT /evidence="ECO:0000269|PubMed:23733939"
FT CONFLICT 92
FT /note="I -> T (in Ref. 2; AAH92871)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="A -> V (in Ref. 2; AAH92871)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="K -> Q (in Ref. 2; AAH92871)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="S -> P (in Ref. 2; AAH92871)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="Q -> QGTA (in Ref. 2; AAH92871)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="D -> V (in Ref. 2; AAH92871)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="N -> D (in Ref. 2; AAH92871)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="D -> A (in Ref. 2; AAH92871)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="H -> L (in Ref. 2; AAH92871)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1219 AA; 138982 MW; 8073242310E99C90 CRC64;
MLVVNSLLKL LQRQTYTCLS HRYGLYLCFG GLVLMIVSAF QFGEVVVEWS RDQYHVLFDS
YRDNVAGKSF QTRLCLPMPI DVVYTWVNGT DINLLKDLRA VRQRLEEEQK ALRERLGKNG
SEITEAPKGR PECLLSHCIM GPVLVLDPAL PANITVKELP TLSAAFSSAK ELLQVAKPLH
PSSSVTALLF HSHTEAEKAH ADALKDLLTH SISRGYLTTD KEAPGLVRMH TLAYLSGFPA
SLKETEQLRV KLPAVVTSKT KKLQLYSEAS IALLHLNTAQ DFTDLTQQAK KNLTLDGKEL
TVSSAFLFWD LTAISQSKQD EDVSASRFED NEELRYSLRS IEKHAPWVRH IFIVTNGQIP
SWLNLDNPRV SVVTHQDIFQ NQTHLPTFSS PAIETHIHRI PGLSQKFIYL NDDVMFGKDV
WPDDFYSHSK GQKVYLTWPV PNCAEGCPGS WIKDGYCDKA CNNSACDWDG GDCQGSSRFG
GAGGSVIGGG QPWQFAGGLG GLAGMSFCNQ GCANSWLADK FCDQACNVLA CGFDVGDCGQ
DNLNQLHRIV LRRNQTLYTL PQGELRPYFS FSGLANRVSE AHVADNQVLR HTSVANKWKT
IHLLLLPGHN ATQIHYNITF QSTDHHDFIM TFSVSVDTRE LPKSNTSTPV RDKEEEPKPT
VATPEPEVPF EAVPKEKQGP KVREQTHGDV QVPVLNETLL PDEVKIELKK LNEKLMSGDI
TIKGFNLTKA MLLEPYKEKD QFTLKHEKDK EEKQKLSPVA QLQNERAAAR VKREKGENVD
QLKPVAPSLV PVQIDDVTTK AQSRLFNIEK PHMFHLLSNL KGNLSKERDS DSEGHLRERP
TGRRLQFYSD SLNRGFLPWE KRKFFQDLME EVNRLQTELQ YTADRTATGR RLQDTFADSL
RYVNRLLNAQ FGFTSRKVPA HMPHMIDRLI MQELQDTFPQ EFDKTSSHRV RHSEDMQFAF
SYFYFLMSAV QQLNISEVFD EIDTDHSGVL SDREIRTLAT RIHELPLSLQ DLTSLEQMLI
NCSKSLPSNL THLHAVSPTQ EAYYDPSMPP VTKGLVIHCK PITERIHKAF KDQNKYKFEI
MGEEEIAFKM IRTNVSHVVG QLDDIRKNPR KFICLNDNID HIHKDAGTVK AVLRDFYESM
FPLPSQFELP REYRNRFLHM TELQEWRIYR DKLKFWTHCV LVTLVVFTVM SFFAEQLVML
KRWLFPRRRV SKDANPERV
