GNPTA_MOUSE
ID GNPTA_MOUSE Reviewed; 1235 AA.
AC Q69ZN6; Q3U3K6; Q3US34;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
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, Kiaa1208;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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=17962477; DOI=10.1167/iovs.07-0452;
RA Gelfman C.M., Vogel P., Issa T.M., Turner C.A., Lee W.S., Kornfeld S.,
RA Rice D.S.;
RT "Mice lacking alpha/beta subunits of GlcNAc-1-phosphotransferase exhibit
RT growth retardation, retinal degeneration, and secretory cell lesions.";
RL Invest. Ophthalmol. Vis. Sci. 48:5221-5228(2007).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q69ZN6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69ZN6-2; Sequence=VSP_017340, VSP_017341;
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 Lys-907-Asp-908 bond.
CC {ECO:0000250|UniProtKB:Q3T906}.
CC -!- DISRUPTION PHENOTYPE: Severe retinal degeneration, growth retardation
CC and secretory cell lesions. Mice are smaller with a reduced mean body
CC weight and length, along with a reduction in total tissue mass and lean
CC body mass. They show elevated levels of serum lysosomal enzymes,
CC cartilage defects, and display cytoplasmic alterations in secretory
CC cells of several exocrine glands. {ECO:0000269|PubMed:17962477}.
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=BAD32410.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE32779.1; Type=Erroneous initiation; 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; AK173132; BAD32410.1; ALT_INIT; mRNA.
DR EMBL; AK140867; BAE24503.1; -; mRNA.
DR EMBL; AK154710; BAE32779.1; ALT_INIT; mRNA.
DR CCDS; CCDS24110.1; -. [Q69ZN6-1]
DR RefSeq; NP_001004164.2; NM_001004164.2. [Q69ZN6-1]
DR AlphaFoldDB; Q69ZN6; -.
DR SMR; Q69ZN6; -.
DR BioGRID; 240639; 1.
DR STRING; 10090.ENSMUSP00000020251; -.
DR GlyGen; Q69ZN6; 8 sites.
DR iPTMnet; Q69ZN6; -.
DR PhosphoSitePlus; Q69ZN6; -.
DR SwissPalm; Q69ZN6; -.
DR EPD; Q69ZN6; -.
DR MaxQB; Q69ZN6; -.
DR PaxDb; Q69ZN6; -.
DR PeptideAtlas; Q69ZN6; -.
DR PRIDE; Q69ZN6; -.
DR ProteomicsDB; 271415; -. [Q69ZN6-1]
DR ProteomicsDB; 271416; -. [Q69ZN6-2]
DR Antibodypedia; 44958; 79 antibodies from 15 providers.
DR Ensembl; ENSMUST00000020251; ENSMUSP00000020251; ENSMUSG00000035311. [Q69ZN6-1]
DR GeneID; 432486; -.
DR KEGG; mmu:432486; -.
DR UCSC; uc007grk.1; mouse. [Q69ZN6-1]
DR UCSC; uc011xlg.1; mouse. [Q69ZN6-2]
DR CTD; 79158; -.
DR MGI; MGI:3643902; Gnptab.
DR VEuPathDB; HostDB:ENSMUSG00000035311; -.
DR eggNOG; ENOG502QQMR; Eukaryota.
DR GeneTree; ENSGT00390000006747; -.
DR HOGENOM; CLU_002469_0_0_1; -.
DR InParanoid; Q69ZN6; -.
DR OMA; NQTHYVL; -.
DR OrthoDB; 851009at2759; -.
DR PhylomeDB; Q69ZN6; -.
DR TreeFam; TF324175; -.
DR BRENDA; 2.7.8.17; 3474.
DR BioGRID-ORCS; 432486; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Gnptab; mouse.
DR PRO; PR:Q69ZN6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q69ZN6; protein.
DR Bgee; ENSMUSG00000035311; Expressed in ventral tegmental area and 244 other tissues.
DR ExpressionAtlas; Q69ZN6; baseline and differential.
DR Genevisible; Q69ZN6; MM.
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:0070622; C:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase complex; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003976; F:UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity; ISS:UniProtKB.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR GO; GO:0016256; P:N-glycan processing to lysosome; ISS:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IMP:MGI.
DR GO; GO:0033299; P:secretion of lysosomal enzymes; IMP:MGI.
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 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Membrane; Metal-binding; Reference proteome; Repeat;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..907
FT /note="N-acetylglucosamine-1-phosphotransferase subunit
FT alpha"
FT /id="PRO_0000225010"
FT CHAIN 908..1235
FT /note="N-acetylglucosamine-1-phosphotransferase subunit
FT beta"
FT /id="PRO_0000225011"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1194..1214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 438..473
FT /note="LNR 1"
FT REPEAT 505..545
FT /note="LNR 2"
FT DOMAIN 699..823
FT /note="DMAP1-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01260"
FT DOMAIN 984..1019
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 751..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 449
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 464
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 516
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT BINDING 531
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 997
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 999
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1001
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1008
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 907..908
FT /note="Cleavage; by MBTPS1"
FT /evidence="ECO:0000250"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 988
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 438..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 452..468
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 505..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT DISULFID 519..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00525"
FT VAR_SEQ 1..46
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017340"
FT VAR_SEQ 47..67
FT /note="DQYHVLFDSYRDNIAGKSFQN -> MGSTSASWASLSPSSRLSSSE (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017341"
FT CONFLICT 444
FT /note="G -> S (in Ref. 2; BAE24503)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="A -> V (in Ref. 2; BAE32779)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1235 AA; 140984 MW; 683038D0FDB673FF CRC64;
MLLKLLQRQT YTCLSHRYGL YVCFVGVVVT IVSAFQFGEV VLEWSRDQYH VLFDSYRDNI
AGKSFQNRLC LPMPIDVVYT WVNGTDLELL KELQQVREHM EEEQRAMRET LGKNTTEPTK
KSEKQLECLL THCIKVPMLV LDPPLPANCT LKDLPTLYPS FHAASDMFNV AKPKNPSTNV
SVVVFDTTKD VEDAHAGPFK GGSKQMVWRA YLTTDKEAPG LVLMQGLAFL SGFPPTFKET
SQLKTKLPEK LSSKIKLLRL YSEASVALLK LNNPKGFQEL NKQTKKNMTI DGKELTISPA
YLLWDLSAIS QSKQDEDVSA SRFEDNEELR YSLRSIERHA PWVRNIFIVT NGQIPSWLNL
DNPRVTIVTH QDIFQNLSHL PTFSSPAIES HIHRIEGLSQ KFIYLNDDVM FGKDVWPDDF
YSHSKGQKVY LTWPVPNCAE GCPGSWIKDG YCDKACNNSA CDWDGGDCSG NTAGNRFVAG
GGGTGNIGAG QHWQFGGGIN TISYCNQGCA NSWLADKFCD QACNVLSCGF DAGDCGQDHF
HELYKVTLLP NQTHYVVPKG EYLSYFSFAN IARRGVEGTY SDNPIIRHAS IANKWKTIHL
IMHSGMNATT IYFNLTLQNA NDEEFKIQIA VEVDTREAPK LNSTTQKAYE SLVSPVTPLP
QADVPFEDVP KEKRFPKIRR HDVNATGRFQ EEVKIPRVNI SLLPKEAQVR LSNLDLQLER
GDITLKGYNL SKSALLRSFL GNSLDTKIKP QARTDETKGN LEVPQENPSH RRPHGFAGEH
RSERWTAPAE TVTVKGRDHA LNPPPVLETN ARLAQPTLGV TVSKENLSPL IVPPESHLPK
EEESDRAEGN AVPVKELVPG RRLQQNYPGF LPWEKKKYFQ DLLDEEESLK TQLAYFTDSK
HTGRQLKDTF ADSLRYVNKI LNSKFGFTSR KVPAHMPHMI DRIVMQELQD MFPEEFDKTS
FHKVRHSEDM QFAFSYFYYL MSAVQPLNIS QVFHEVDTDQ SGVLSDREIR TLATRIHDLP
LSLQDLTGLE HMLINCSKML PANITQLNNI PPTQEAYYDP NLPPVTKSLV TNCKPVTDKI
HKAYKDKNKY RFEIMGEEEI AFKMIRTNVS HVVGQLDDIR KNPRKFVCLN DNIDHNHKDA
RTVKAVLRDF YESMFPIPSQ FELPREYRNR FLHMHELQEW RAYRDKLKFW THCVLATLII
FTIFSFFAEQ IIALKRKIFP RRRIHKEASP DRIRV
