PLPL1_MOUSE
ID PLPL1_MOUSE Reviewed; 599 AA.
AC Q3V1D5;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Omega-hydroxyceramide transacylase {ECO:0000305|PubMed:28248300};
DE EC=2.3.1.296 {ECO:0000305|PubMed:27751867, ECO:0000305|PubMed:28248300};
DE AltName: Full=Patatin-like phospholipase domain-containing protein 1 {ECO:0000312|MGI:MGI:3617850};
GN Name=Pnpla1 {ECO:0000312|MGI:MGI:3617850};
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].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27751867; DOI=10.1016/j.jid.2016.08.036;
RA Grond S., Eichmann T.O., Dubrac S., Kolb D., Schmuth M., Fischer J.,
RA Crumrine D., Elias P.M., Haemmerle G., Zechner R., Lass A., Radner F.P.W.;
RT "PNPLA1 Deficiency in Mice and Humans Leads to a Defect in the Synthesis of
RT Omega-O-Acylceramides.";
RL J. Invest. Dermatol. 137:394-402(2017).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28248300; DOI=10.1038/ncomms14609;
RA Hirabayashi T., Anjo T., Kaneko A., Senoo Y., Shibata A., Takama H.,
RA Yokoyama K., Nishito Y., Ono T., Taya C., Muramatsu K., Fukami K.,
RA Munoz-Garcia A., Brash A.R., Ikeda K., Arita M., Akiyama M., Murakami M.;
RT "PNPLA1 has a crucial role in skin barrier function by directing
RT acylceramide biosynthesis.";
RL Nat. Commun. 8:14609-14609(2017).
CC -!- FUNCTION: Omega-hydroxyceramide transacylase involved in the synthesis
CC of omega-O-acylceramides (esterified omega-hydroxyacyl-sphingosine;
CC EOS), which are extremely hydrophobic lipids involved in skin barrier
CC formation (PubMed:27751867, PubMed:28248300). Catalyzes the last step
CC of the synthesis of omega-O-acylceramides by transferring linoleic acid
CC from triglycerides to an omega-hydroxyceramide (PubMed:27751867,
CC PubMed:28248300). Omega-O-acylceramides, are required for the
CC biogenesis of lipid lamellae in the stratum corneum and the formation
CC of the cornified lipid envelope which are essential for the epidermis
CC barrier function (PubMed:27751867, PubMed:28248300). These lipids also
CC play a role in keratinocyte differentiation (PubMed:28248300). May also
CC act on omega-hydroxylated ultra-long chain fatty acids (omega-OH ULCFA)
CC and acylglucosylceramides (GlcEOS) (PubMed:28248300).
CC {ECO:0000269|PubMed:27751867, ECO:0000269|PubMed:28248300}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an
CC N-(omega-hydroxy-ultra-long chain fatty acyl)-sphingoid base = a
CC diacylglycerol + an N-[omega-(9Z,12Z-octadecadienoyloxy)-O-ultra-long
CC chain fatty acyl]-sphingoid base; Xref=Rhea:RHEA:61528,
CC ChEBI:CHEBI:18035, ChEBI:CHEBI:144774, ChEBI:CHEBI:144784,
CC ChEBI:CHEBI:144785; EC=2.3.1.296;
CC Evidence={ECO:0000305|PubMed:27751867, ECO:0000305|PubMed:28248300};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61529;
CC Evidence={ECO:0000305|PubMed:27751867, ECO:0000305|PubMed:28248300};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an
CC N-(omega-hydroxy-ultra-long chain fatty acyl)-sphing-4-enine = a
CC diacylglycerol + an N-(omega-(9Z,12Z-octadecadienoyloxy)-ultra-long
CC chain fatty acyl)-sphing-4-enine; Xref=Rhea:RHEA:65692,
CC ChEBI:CHEBI:18035, ChEBI:CHEBI:144774, ChEBI:CHEBI:157662,
CC ChEBI:CHEBI:157663; Evidence={ECO:0000305|PubMed:27751867,
CC ECO:0000305|PubMed:28248300};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65693;
CC Evidence={ECO:0000305|PubMed:27751867, ECO:0000305|PubMed:28248300};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + N-
CC (28-hydroxyoctacosanoyl)-sphing-4-enine = a diacylglycerol + N-(28-
CC (9Z,12Z-octadecadienoyloxy)-octacosanoyl)-sphing-4-enine;
CC Xref=Rhea:RHEA:65648, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774,
CC ChEBI:CHEBI:157643, ChEBI:CHEBI:157652;
CC Evidence={ECO:0000305|PubMed:28248300};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65649;
CC Evidence={ECO:0000305|PubMed:28248300};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z,12Z)-octadecadienoylglycerol + N-(30-
CC hydroxytriacontanoyl)-sphing-4-enine = di-(9Z,12Z)-
CC octadecadienoylglycerol + N-[30-(9Z,12Z-octadecadienoyloxy)-
CC triacontanoyl]-sphing-4-enine; Xref=Rhea:RHEA:55264,
CC ChEBI:CHEBI:34862, ChEBI:CHEBI:75844, ChEBI:CHEBI:138658,
CC ChEBI:CHEBI:138664; Evidence={ECO:0000305|PubMed:28248300};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55265;
CC Evidence={ECO:0000305|PubMed:28248300};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + N-
CC (32-hydroxydotriacontanoyl)-sphing-4-enine = a diacylglycerol + N-
CC (32-(9Z,12Z-octadecadienoyloxy)-dotricontanoyl)-sphing-4-enine;
CC Xref=Rhea:RHEA:65652, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774,
CC ChEBI:CHEBI:157644, ChEBI:CHEBI:157653;
CC Evidence={ECO:0000305|PubMed:28248300};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65653;
CC Evidence={ECO:0000305|PubMed:28248300};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + N-
CC (32-hydroxydotriacontenoyl)-sphing-4-enine = a diacylglycerol + an N-
CC (32-(9Z,12Z-octadecadienoyloxy)-dotriacontenoyl)-sphing-4-enine;
CC Xref=Rhea:RHEA:65668, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774,
CC ChEBI:CHEBI:157645, ChEBI:CHEBI:157657;
CC Evidence={ECO:0000305|PubMed:28248300};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65669;
CC Evidence={ECO:0000305|PubMed:28248300};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an
CC N-(34-hydroxytetratriacontenoyl)-sphing-4-enine = a diacylglycerol +
CC an N-(34-(9Z,12Z-octadecadienoyloxy)-tetratriacontenoyl)-sphing-4-
CC enine; Xref=Rhea:RHEA:65672, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774,
CC ChEBI:CHEBI:157646, ChEBI:CHEBI:157656;
CC Evidence={ECO:0000305|PubMed:28248300};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65673;
CC Evidence={ECO:0000305|PubMed:28248300};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an
CC N-(34-hydroxytetratriacontadienoyl)-sphing-4-enine = a diacylglycerol
CC + an N-(34-(9Z,12Z-octadecadienoyloxy)-tetratriacontadienoyl)-sphing-
CC 4-enine; Xref=Rhea:RHEA:65676, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774,
CC ChEBI:CHEBI:157647, ChEBI:CHEBI:157658;
CC Evidence={ECO:0000305|PubMed:28248300};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65677;
CC Evidence={ECO:0000305|PubMed:28248300};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an
CC N-(36-hydroxyhexatriacontenoyl)-sphing-4-enine = a diacylglycerol +
CC an N-(36-(9Z,12Z-octadecadienoyloxy)-hexatriacontenoyl)-sphing-4-
CC enine; Xref=Rhea:RHEA:65680, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774,
CC ChEBI:CHEBI:157648, ChEBI:CHEBI:157659;
CC Evidence={ECO:0000305|PubMed:28248300};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65681;
CC Evidence={ECO:0000305|PubMed:28248300};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an
CC N-(36-hydroxyhexatriacontadienoyl)-sphing-4-enine = a diacylglycerol
CC + an N-(36-(9Z,12Z-octadecadienoyloxy)-hexatriacontadienoyl)-sphing-
CC 4-enine; Xref=Rhea:RHEA:65684, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774,
CC ChEBI:CHEBI:157649, ChEBI:CHEBI:157660;
CC Evidence={ECO:0000305|PubMed:28248300};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65685;
CC Evidence={ECO:0000305|PubMed:28248300};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (9Z,12Z)-octadecadienoyl-containing triacyl-sn-glycerol + an
CC N-(38-hydroxyoctatriacontenoyl)-sphing-4-enine = a diacylglycerol +
CC an N-(38-(9Z,12Z-octadecadienoyloxy)-octatriacontenoyl)-sphing-4-
CC enine; Xref=Rhea:RHEA:65688, ChEBI:CHEBI:18035, ChEBI:CHEBI:144774,
CC ChEBI:CHEBI:157650, ChEBI:CHEBI:157661;
CC Evidence={ECO:0000305|PubMed:28248300};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65689;
CC Evidence={ECO:0000305|PubMed:28248300};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N8W4}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in skin by keratinocytes, at
CC the boundary area between the nucleated stratum granulosum and the
CC denucleated stratum corneum in the epidermis (at protein level)
CC (PubMed:28248300). Also expressed in stomach and other surface lining
CC tissues like intestine and tongue (PubMed:27751867, PubMed:28248300).
CC Also detected in testis as well as in other tissues but at very low
CC level (PubMed:28248300). {ECO:0000269|PubMed:27751867,
CC ECO:0000269|PubMed:28248300}.
CC -!- INDUCTION: Up-regulated upon induced differentiation of keratinocytes.
CC {ECO:0000269|PubMed:28248300}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice lacking Pnpla1 are
CC obtained at the expected Mendelian ratio but die within 24 hours after
CC birth (PubMed:27751867, PubMed:28248300). They display shiny and taut
CC skin, often with a necrotic tail tip (PubMed:27751867,
CC PubMed:28248300). They are less active, markedly smaller, and weighed
CC significantly less than their wild-type counterpart (PubMed:27751867).
CC Unique linoleate-containing lipids including acylceramides,
CC acylglucosylceramides and (O-acyl)-omega-hydroxy fatty acids are almost
CC absent in the epidermis while there is a reciprocal increase in their
CC putative precursors (PubMed:27751867, PubMed:28248300). The absence of
CC these highly hydrophobic linoleate-containing lipids in the epidermis
CC is responsible for the lethal disruption of the epidermal permeability
CC barrier which is characterized by a decrease in intercellular lipid
CC lamellae in the stratum corneum, the loss or abnormalities of the
CC cornified lipid envelope, and aberrant keratinocyte differentiation
CC (PubMed:27751867, PubMed:28248300). Keratinocyte-specific conditional
CC knockout mice also die shortly after birth, displaying desquamation
CC with alteration of the stratum corneum and of the lipid composition of
CC the epidermis (PubMed:28248300). {ECO:0000269|PubMed:27751867,
CC ECO:0000269|PubMed:28248300}.
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; AK132521; BAE21216.1; -; mRNA.
DR CCDS; CCDS37533.1; -.
DR RefSeq; NP_001030057.1; NM_001034885.3.
DR AlphaFoldDB; Q3V1D5; -.
DR SMR; Q3V1D5; -.
DR STRING; 10090.ENSMUSP00000050123; -.
DR iPTMnet; Q3V1D5; -.
DR PhosphoSitePlus; Q3V1D5; -.
DR jPOST; Q3V1D5; -.
DR PaxDb; Q3V1D5; -.
DR PRIDE; Q3V1D5; -.
DR ProteomicsDB; 288256; -.
DR Antibodypedia; 29651; 130 antibodies from 17 providers.
DR Ensembl; ENSMUST00000056866; ENSMUSP00000050123; ENSMUSG00000043286.
DR GeneID; 433091; -.
DR KEGG; mmu:433091; -.
DR UCSC; uc008brt.1; mouse.
DR CTD; 285848; -.
DR MGI; MGI:3617850; Pnpla1.
DR VEuPathDB; HostDB:ENSMUSG00000043286; -.
DR eggNOG; KOG3773; Eukaryota.
DR GeneTree; ENSGT00940000160828; -.
DR HOGENOM; CLU_039943_0_0_1; -.
DR InParanoid; Q3V1D5; -.
DR OMA; EDSNWMS; -.
DR OrthoDB; 1204225at2759; -.
DR PhylomeDB; Q3V1D5; -.
DR TreeFam; TF314272; -.
DR BioGRID-ORCS; 433091; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q3V1D5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3V1D5; protein.
DR Bgee; ENSMUSG00000043286; Expressed in tail skin and 41 other tissues.
DR ExpressionAtlas; Q3V1D5; baseline and differential.
DR Genevisible; Q3V1D5; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IMP:UniProtKB.
DR GO; GO:0106341; F:omega-hydroxyceramide transacylase activity; IMP:UniProtKB.
DR GO; GO:0030280; F:structural constituent of skin epidermis; IMP:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; IBA:GO_Central.
DR GO; GO:0046513; P:ceramide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; IMP:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0106342; P:omega-hydroxyceramide biosynthetic process; IMP:UniProtKB.
DR GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR033562; PLPL.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR12406; PTHR12406; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..599
FT /note="Omega-hydroxyceramide transacylase"
FT /id="PRO_0000292020"
FT DOMAIN 16..185
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 289..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 51..55
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 172..174
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 326..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 53
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
SQ SEQUENCE 599 AA; 65170 MW; F9FDE58FA441F9F0 CRC64;
MDEQVFKGDP DTPHSISFSG SGFLSYYQAG AVDALRDLAP RMLDTAHRFA GTSAGAVIAA
LVVCGIEMEK YLRVLNMGLA EVKKFFLGPL SPSCKMVQMM RQFLYDVLPE DSYKFATGKL
HVSLTRVTDG ENVVVSEYRS KEELIEALYC SCFVPVYCGF IPPTYRGERY IDGGFTSMQP
CSFWTDSITI STFSSQQDIC PRDCPTIFHD FRMFNFSFQF SLENITRMTH ALFPPDLVIL
QEYYYRGYND AVSYLRRLNA AYLDSPSKRV IFPRVEVYCQ IEVALGHEPP PPSLQNLPAL
RRSPADSSQT HAQGSPKKDR KDSHSSAAPS VQTPESGCKE SVESPVSLRV SISKQPSVSP
LSPAQPVPVM RPTGPRDSCP INVQTPNPER GVKGALDSAT ERGMKDALAS ATDEQSTTTL
PPVLLPAADS RGSKTGSSVP IGSPESPRLL LRSSQGATAS RATLGLPPLS PSTPPAGPPV
EDLGPERPTA TGSPALSQLT GSAAPGTGKK APHKPLLVEG PGEDSNTAKT MFKRKQKTNA
TRECFHRNAQ SKKPASKLKS APCPLNFPVL PKRVWVTYKP HPSRIQDYSY PEGVSGQNS
