PLPP2_MOUSE
ID PLPP2_MOUSE Reviewed; 276 AA.
AC Q9DAX2; Q9WUA4;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Phospholipid phosphatase 2 {ECO:0000305};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:O43688};
DE EC=3.1.3.4 {ECO:0000250|UniProtKB:O43688};
DE AltName: Full=Lipid phosphate phosphohydrolase 2;
DE AltName: Full=PAP2-gamma;
DE Short=PAP2-G;
DE AltName: Full=Phosphatidate phosphohydrolase type 2c;
DE AltName: Full=Phosphatidic acid phosphatase 2c;
DE Short=PAP-2c;
DE Short=PAP2c;
GN Name=Plpp2 {ECO:0000312|MGI:MGI:1354945}; Synonyms=Lpp2, Ppap2c;
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 2).
RC STRAIN=C57BL/6J;
RX PubMed=10662554; DOI=10.1006/geno.1999.6055;
RA Zhang N., Copeland N.G., Gilbert D.J., Jenkins N.A., Gridley T.;
RT "Cloning, expression, and chromosomal localization of a mouse gene
RT homologous to the germ cell migration regulator wunen and to type 2
RT phosphatidic acid phosphatases.";
RL Genomics 63:142-144(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Placenta;
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 TISSUE=Mammary tumor;
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 [LARGE SCALE ANALYSIS] AT ASN-155.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=10992322;
RX DOI=10.1002/1526-968x(200008)27:4<137::aid-gene10>3.0.co;2-4;
RA Zhang N., Sundberg J.P., Gridley T.;
RT "Mice mutant for Ppap2c, a homolog of the germ cell migration regulator
RT wunen, are viable and fertile.";
RL Genesis 27:137-140(2000).
CC -!- FUNCTION: Magnesium-independent phospholipid phosphatase that catalyzes
CC the dephosphorylation of a variety of glycerolipid and sphingolipid
CC phosphate esters including phosphatidate/PA, lysophosphatidate/LPA,
CC sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P. Has no
CC apparent extracellular phosphatase activity and therefore most probably
CC acts intracellularly. Also acts on N-oleoyl ethanolamine phosphate/N-
CC (9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological
CC compound. Through dephosphorylation of these bioactive lipid mediators
CC produces new bioactive compounds and may regulate signal transduction
CC in different cellular processes (By similarity). Indirectly regulates,
CC for instance, cell cycle G1/S phase transition through its phospholipid
CC phosphatase activity (By similarity). {ECO:0000250|UniProtKB:O43688,
CC ECO:0000250|UniProtKB:Q8K593}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-
CC dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859,
CC ChEBI:CHEBI:82929; Evidence={ECO:0000250|UniProtKB:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-
CC di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333,
CC ChEBI:CHEBI:74546; Evidence={ECO:0000250|UniProtKB:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol +
CC phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-
CC octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937,
CC ChEBI:CHEBI:84973; Evidence={ECO:0000250|UniProtKB:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine;
CC Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57756, ChEBI:CHEBI:60119;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-
CC enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-
CC octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815,
CC ChEBI:CHEBI:85376; Evidence={ECO:0000250|UniProtKB:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-
CC octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466,
CC ChEBI:CHEBI:145465; Evidence={ECO:0000250|UniProtKB:O43688};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161;
CC Evidence={ECO:0000250|UniProtKB:O43688};
CC -!- ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase.
CC Insensitive to N-ethylmaleimide. {ECO:0000250|UniProtKB:O43688}.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000250|UniProtKB:O43688}.
CC -!- SUBUNIT: Forms functional homodimers and homooligomers. Can also form
CC heterooligomers with PLPP1 and PLPP3. {ECO:0000250|UniProtKB:O43688}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O43688}; Multi-
CC pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:O43688}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:O43688};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:O43688}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DAX2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DAX2-2; Sequence=VSP_009654, VSP_009655;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in lung, liver and kidney;
CC at low levels in heart and brain, and was not detected in skeletal
CC muscle.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:O43688}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Plpp2 do not show overt phenotype
CC (PubMed:10992322). Born at the expected Mendelian frequency they are
CC perfectly viable and fertile (PubMed:10992322).
CC {ECO:0000269|PubMed:10992322}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; AF123611; AAD24061.1; -; mRNA.
DR EMBL; AK005452; BAB24045.1; -; mRNA.
DR EMBL; AK049581; BAC33824.1; -; mRNA.
DR EMBL; BC010332; AAH10332.1; -; mRNA.
DR CCDS; CCDS35966.1; -. [Q9DAX2-1]
DR RefSeq; NP_001289318.1; NM_001302389.1.
DR RefSeq; NP_001289319.1; NM_001302390.1.
DR RefSeq; NP_001289371.1; NM_001302442.1.
DR RefSeq; NP_056632.2; NM_015817.3. [Q9DAX2-1]
DR AlphaFoldDB; Q9DAX2; -.
DR BioGRID; 206116; 1.
DR IntAct; Q9DAX2; 1.
DR STRING; 10090.ENSMUSP00000069670; -.
DR GlyGen; Q9DAX2; 2 sites.
DR iPTMnet; Q9DAX2; -.
DR PhosphoSitePlus; Q9DAX2; -.
DR MaxQB; Q9DAX2; -.
DR PaxDb; Q9DAX2; -.
DR PRIDE; Q9DAX2; -.
DR ProteomicsDB; 289938; -. [Q9DAX2-1]
DR ProteomicsDB; 289939; -. [Q9DAX2-2]
DR Antibodypedia; 22287; 169 antibodies from 22 providers.
DR DNASU; 50784; -.
DR Ensembl; ENSMUST00000063879; ENSMUSP00000069670; ENSMUSG00000052151. [Q9DAX2-1]
DR GeneID; 50784; -.
DR KEGG; mmu:50784; -.
DR UCSC; uc007fyq.2; mouse. [Q9DAX2-1]
DR UCSC; uc007fyt.1; mouse. [Q9DAX2-2]
DR CTD; 8612; -.
DR MGI; MGI:1354945; Plpp2.
DR VEuPathDB; HostDB:ENSMUSG00000052151; -.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000155885; -.
DR InParanoid; Q9DAX2; -.
DR OMA; MDVVCVL; -.
DR OrthoDB; 1621899at2759; -.
DR PhylomeDB; Q9DAX2; -.
DR TreeFam; TF316040; -.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 50784; 3 hits in 45 CRISPR screens.
DR ChiTaRS; Plpp2; mouse.
DR PRO; PR:Q9DAX2; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9DAX2; protein.
DR Bgee; ENSMUSG00000052151; Expressed in metanephric ureteric bud and 227 other tissues.
DR ExpressionAtlas; Q9DAX2; baseline and differential.
DR Genevisible; Q9DAX2; MM.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0106235; F:ceramide-1-phosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042577; F:lipid phosphatase activity; IBA:GO_Central.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB.
DR GO; GO:0046839; P:phospholipid dephosphorylation; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:UniProtKB.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0006670; P:sphingosine metabolic process; ISS:UniProtKB.
DR InterPro; IPR028674; LPP2.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; PTHR10165; 1.
DR PANTHER; PTHR10165:SF25; PTHR10165:SF25; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Endoplasmic reticulum; Endosome;
KW Glycoprotein; Hydrolase; Lipid metabolism; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..276
FT /note="Phospholipid phosphatase 2"
FT /id="PRO_0000220910"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..51
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..161
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..218
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 117..125
FT /note="Phosphatase sequence motif I"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 164..167
FT /note="Phosphatase sequence motif II"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 212..223
FT /note="Phosphatase sequence motif III"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT REGION 251..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /note="Proton donors"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT ACT_SITE 219
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT SITE 223
FT /note="Stabilizes the active site histidine for
FT nucleophilic attack"
FT /evidence="ECO:0000250|UniProtKB:O34349"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT VAR_SEQ 240..250
FT /note="RYVSDFFKSRP -> SPTCLTHRLCF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10662554"
FT /id="VSP_009654"
FT VAR_SEQ 251..276
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10662554"
FT /id="VSP_009655"
SQ SEQUENCE 276 AA; 31193 MW; 978A83D4681113D2 CRC64;
MERRWVFVLL DVLCVLVASL PFIILTLVNA PYKRGFYCGD DSIRYPYRPD TITHGLMAGV
IITATVILVS LGEAYLVYTD RLYSRSNFNN YVAAIYKVLG TFLFGAAVSQ SLTDLAKYMI
GRLRPSFLAV CDPDWSQVNC SGYVQLEVCR GSPANVTEAR LSFYSGHSSF GMYCMLFLAL
YVQARLCWKW ARLLRPTVQF FLVAFAIYVG YTRVSDHKHH WSDVLVGLLQ GALVACLTVR
YVSDFFKSRP PQPCQEDEVP ERKPSLSLTL TLGDRP
