PLBL2_MOUSE
ID PLBL2_MOUSE Reviewed; 594 AA.
AC Q3TCN2; Q3TD43; Q3TPP8; Q8BHG8; Q8BMB6; Q8BXI3; Q8C0M4; Q8R0V3; Q9DBG4;
AC Q9EQI9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Putative phospholipase B-like 2;
DE EC=3.1.1.-;
DE AltName: Full=66.3 kDa protein;
DE AltName: Full=76 kDa protein;
DE Short=p76;
DE AltName: Full=LAMA-like protein 2;
DE AltName: Full=Lamina ancestor homolog 2;
DE AltName: Full=Phospholipase B domain-containing protein 2;
DE Contains:
DE RecName: Full=Putative phospholipase B-like 2 28 kDa form;
DE Contains:
DE RecName: Full=Putative phospholipase B-like 2 40 kDa form;
DE Contains:
DE RecName: Full=Putative phospholipase B-like 2 15 kDa form;
DE Flags: Precursor;
GN Name=Plbd2;
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 [MRNA] (ISOFORM 1).
RC STRAIN=C3H/RV;
RX PubMed=12080145; DOI=10.1073/pnas.142287799;
RA Perelygin A.A., Scherbik S.V., Zhulin I.B., Stockman B.M., Li Y.,
RA Brinton M.A.;
RT "Positional cloning of the murine flavivirus resistance gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9322-9327(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Brain cortex, Cerebellum, Liver, Testis, Thymus, and Wolffian duct;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP GLYCOSYLATION AT ASN-93; ASN-115; ASN-236; ASN-441 AND ASN-520, SUBCELLULAR
RP LOCATION, PROCESSING, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17007843; DOI=10.1016/j.febslet.2006.09.029;
RA Deuschl F., Kollmann K., von Figura K., Luebke T.;
RT "Molecular characterization of the hypothetical 66.3-kDa protein in mouse:
RT lysosomal targeting, glycosylation, processing and tissue distribution.";
RL FEBS Lett. 580:5747-5752(2006).
RN [5]
RP SUBCELLULAR LOCATION, AND PROCESSING.
RX PubMed=17105447; DOI=10.1042/bj20061205;
RA Jensen A.G., Chemali M., Chapel A., Kieffer-Jaquinod S., Jadot M.,
RA Garin J., Journet A.;
RT "Biochemical characterization and lysosomal localization of the mannose-6-
RT phosphate protein p76 (hypothetical protein LOC196463).";
RL Biochem. J. 402:449-458(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 47-594, GLYCOSYLATION AT ASN-115;
RP ASN-236; ASN-441 AND ASN-520, AND DISULFIDE BONDS.
RX PubMed=19237744; DOI=10.1107/s0907444908041814;
RA Lakomek K., Dickmanns A., Mueller U., Kollmann K., Deuschl F., Berndt A.,
RA Lubke T., Ficner R.;
RT "De novo sulfur SAD phasing of the lysosomal 66.3 kDa protein from mouse.";
RL Acta Crystallogr. D 65:220-228(2009).
CC -!- FUNCTION: Putative phospholipase. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with IGF2R. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000269|PubMed:17007843,
CC ECO:0000269|PubMed:17105447}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TCN2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TCN2-2; Sequence=VSP_024998, VSP_024999;
CC -!- TISSUE SPECIFICITY: Present at highest levels in spleen, lung and brain
CC (at protein level). {ECO:0000269|PubMed:17007843}.
CC -!- PTM: The p76 protein is synthesized as a 76 kDa precursor which is then
CC processed into a N-terminal 28 kDa form and a C-terminal 40 kDa form.
CC The C-terminal peptide is further processed into a 15 kDa form.
CC -!- PTM: Glycosylated; contains mannose 6-phosphate sugars. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phospholipase B-like family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26395.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF217003; AAG44101.1; -; mRNA.
DR EMBL; AK004973; BAB23709.1; -; mRNA.
DR EMBL; AK030234; BAC26858.1; -; mRNA.
DR EMBL; AK032930; BAC28089.1; -; mRNA.
DR EMBL; AK042089; BAC31160.1; -; mRNA.
DR EMBL; AK043608; BAC31595.1; -; mRNA.
DR EMBL; AK046937; BAC32923.1; -; mRNA.
DR EMBL; AK164220; BAE37687.1; -; mRNA.
DR EMBL; AK170387; BAE41761.1; -; mRNA.
DR EMBL; AK170631; BAE41924.1; -; mRNA.
DR EMBL; BC026395; AAH26395.1; ALT_INIT; mRNA.
DR EMBL; BC038605; AAH38605.1; -; mRNA.
DR EMBL; BC048826; AAH48826.1; -; mRNA.
DR CCDS; CCDS19620.1; -. [Q3TCN2-1]
DR RefSeq; NP_076114.2; NM_023625.4. [Q3TCN2-1]
DR PDB; 3FBX; X-ray; 2.40 A; A=47-594.
DR PDB; 3FGR; X-ray; 1.80 A; A=47-248, B=249-594.
DR PDB; 3FGT; X-ray; 2.40 A; A=47-248, B=249-594.
DR PDB; 3FGW; X-ray; 2.80 A; A=47-594.
DR PDBsum; 3FBX; -.
DR PDBsum; 3FGR; -.
DR PDBsum; 3FGT; -.
DR PDBsum; 3FGW; -.
DR AlphaFoldDB; Q3TCN2; -.
DR SMR; Q3TCN2; -.
DR BioGRID; 214915; 3.
DR IntAct; Q3TCN2; 1.
DR MINT; Q3TCN2; -.
DR STRING; 10090.ENSMUSP00000031597; -.
DR MEROPS; C95.001; -.
DR GlyConnect; 2661; 4 N-Linked glycans (2 sites).
DR GlyGen; Q3TCN2; 6 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q3TCN2; -.
DR PhosphoSitePlus; Q3TCN2; -.
DR EPD; Q3TCN2; -.
DR jPOST; Q3TCN2; -.
DR MaxQB; Q3TCN2; -.
DR PaxDb; Q3TCN2; -.
DR PeptideAtlas; Q3TCN2; -.
DR PRIDE; Q3TCN2; -.
DR ProteomicsDB; 289443; -. [Q3TCN2-1]
DR ProteomicsDB; 289444; -. [Q3TCN2-2]
DR Antibodypedia; 2539; 100 antibodies from 19 providers.
DR DNASU; 71772; -.
DR Ensembl; ENSMUST00000031597; ENSMUSP00000031597; ENSMUSG00000029598. [Q3TCN2-1]
DR GeneID; 71772; -.
DR KEGG; mmu:71772; -.
DR UCSC; uc008zhh.2; mouse. [Q3TCN2-1]
DR UCSC; uc008zhi.2; mouse. [Q3TCN2-2]
DR CTD; 196463; -.
DR MGI; MGI:1919022; Plbd2.
DR VEuPathDB; HostDB:ENSMUSG00000029598; -.
DR eggNOG; KOG3774; Eukaryota.
DR GeneTree; ENSGT00530000063509; -.
DR HOGENOM; CLU_027106_4_0_1; -.
DR InParanoid; Q3TCN2; -.
DR OMA; FQWSKSP; -.
DR OrthoDB; 724258at2759; -.
DR PhylomeDB; Q3TCN2; -.
DR TreeFam; TF315042; -.
DR BioGRID-ORCS; 71772; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Plbd2; mouse.
DR EvolutionaryTrace; Q3TCN2; -.
DR PRO; PR:Q3TCN2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3TCN2; protein.
DR Bgee; ENSMUSG00000029598; Expressed in right kidney and 203 other tissues.
DR Genevisible; Q3TCN2; MM.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.439.20; -; 1.
DR Gene3D; 2.10.70.60; -; 1.
DR Gene3D; 3.60.60.20; -; 1.
DR InterPro; IPR007000; PLipase_B-like.
DR InterPro; IPR043040; PLipase_B-like_dom1.
DR InterPro; IPR043041; PLipase_B-like_dom2.
DR InterPro; IPR043042; PLipase_B-like_dom3.
DR PANTHER; PTHR12370; PTHR12370; 1.
DR Pfam; PF04916; Phospholip_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW Hydrolase; Lipid degradation; Lipid metabolism; Lysosome;
KW Reference proteome; Signal.
FT SIGNAL 1..46
FT CHAIN 47..594
FT /note="Putative phospholipase B-like 2"
FT /id="PRO_0000286111"
FT CHAIN 47..248
FT /note="Putative phospholipase B-like 2 28 kDa form"
FT /id="PRO_0000314076"
FT CHAIN 249..594
FT /note="Putative phospholipase B-like 2 40 kDa form"
FT /id="PRO_0000314077"
FT CHAIN 514..594
FT /note="Putative phospholipase B-like 2 15 kDa form"
FT /id="PRO_0000314078"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17007843"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17007843,
FT ECO:0000269|PubMed:19237744"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17007843,
FT ECO:0000269|PubMed:19237744"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17007843,
FT ECO:0000269|PubMed:19237744"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17007843,
FT ECO:0000269|PubMed:19237744"
FT DISULFID 147..157
FT /evidence="ECO:0000269|PubMed:19237744"
FT DISULFID 497..500
FT /evidence="ECO:0000269|PubMed:19237744"
FT VAR_SEQ 436..451
FT /note="FETVFNASGLQALVAQ -> VALFFHVAPSPQVCPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024998"
FT VAR_SEQ 452..594
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024999"
FT CONFLICT 22
FT /note="A -> S (in Ref. 2; BAC28089)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="W -> L (in Ref. 2; BAC28089)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="D -> G (in Ref. 2; BAE41761)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="R -> M (in Ref. 2; BAB23709)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="Q -> H (in Ref. 2; BAB23709)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="D -> Y (in Ref. 2; BAB23709)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="D -> N (in Ref. 2; BAB23709)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="E -> K (in Ref. 2; BAB23709)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="D -> N (in Ref. 2; BAB23709)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="V -> E (in Ref. 2; BAE37687)"
FT /evidence="ECO:0000305"
FT CONFLICT 381
FT /note="N -> S (in Ref. 1; AAG44101)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="A -> T (in Ref. 2; BAE41924)"
FT /evidence="ECO:0000305"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:3FGR"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 116..142
FT /evidence="ECO:0007829|PDB:3FGR"
FT TURN 143..147
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 154..177
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 182..202
FT /evidence="ECO:0007829|PDB:3FGR"
FT TURN 216..219
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 323..330
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 336..341
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 350..360
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 364..371
FT /evidence="ECO:0007829|PDB:3FGR"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 381..387
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 388..390
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 399..409
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 419..425
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 437..442
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 445..452
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:3FGR"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 477..484
FT /evidence="ECO:0007829|PDB:3FGR"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 500..504
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 543..547
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 551..557
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:3FGR"
FT HELIX 567..569
FT /evidence="ECO:0007829|PDB:3FGR"
FT TURN 571..574
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:3FGR"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:3FGR"
SQ SEQUENCE 594 AA; 66289 MW; 202556A56C1AD0BA CRC64;
MAAPVDGSSG GWAARALRRA LALTSLTTLA LLASLTGLLL SGPAGALPTL GPGWQRQNPD
PPVSRTRSLL LDAASGQLRL EDGFHPDAVA WANLTNAIRE TGWAYLDLST NGRYNDSLQA
YAAGVVEASV SEELIYMHWM NTVVNYCGPF EYEVGYCEKL KNFLEANLEW MQREMELNPD
SPYWHQVRLT LLQLKGLEDS YEGRLTFPTG RFTIKPLGFL LLQISGDLED LEPALNKTNT
KPSLGSGSCS ALIKLLPGGH DLLVAHNTWN SYQNMLRIIK KYRLQFREGP QEEYPLVAGN
NLVFSSYPGT IFSGDDFYIL GSGLVTLETT IGNKNPALWK YVQPQGCVLE WIRNVVANRL
ALDGATWADV FKRFNSGTYN NQWMIVDYKA FLPNGPSPGS RVLTILEQIP GMVVVADKTA
ELYKTTYWAS YNIPYFETVF NASGLQALVA QYGDWFSYTK NPRAKIFQRD QSLVEDMDAM
VRLMRYNDFL HDPLSLCEAC NPKPNAENAI SARSDLNPAN GSYPFQALHQ RAHGGIDVKV
TSFTLAKYMS MLAASGPTWD QCPPFQWSKS PFHSMLHMGQ PDLWMFSPIR VPWD
