ID PA24D_MOUSE Reviewed; 825 AA.
AC Q50L43; A2AQJ1; Q3TJC5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 24-JAN-2024, entry version 129.
DE RecName: Full=Cytosolic phospholipase A2 delta {ECO:0000305};
DE Short=cPLA2-delta {ECO:0000303|PubMed:15866882};
DE EC=3.1.1.4 {ECO:0000269|PubMed:15866882};
DE AltName: Full=Phospholipase A2 group IVD;
GN Name=Pla2g4d {ECO:0000312|MGI:MGI:1925640};
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], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=15866882; DOI=10.1074/jbc.m413711200;
RA Ohto T., Uozumi N., Hirabayashi T., Shimizu T.;
RT "Identification of novel cytosolic phospholipase A(2)s, murine
RT cPLA(2)delta, epsilon, and zeta, which form a gene cluster with
RT cPLA(2)beta.";
RL J. Biol. Chem. 280:24576-24583(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Calcium-dependent phospholipase A2 that selectively
CC hydrolyzes glycerophospholipids in the sn-2 position (PubMed:15866882).
CC Compared to its human ortholog, may have no preference for the fatty
CC acid found at the sn-2 position (PubMed:15866882).
CC {ECO:0000269|PubMed:15866882}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:15866882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:15866882};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000269|PubMed:15866882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000305|PubMed:15866882};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000269|PubMed:15866882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000305|PubMed:15866882};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:Q86XP0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:Q86XP0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000269|PubMed:15866882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000305|PubMed:15866882};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC Evidence={ECO:0000269|PubMed:15866882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40816;
CC Evidence={ECO:0000305|PubMed:15866882};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000269|PubMed:15866882};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000305|PubMed:15866882};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- ACTIVITY REGULATION: Stimulated by cytosolic Ca(2+).
CC {ECO:0000269|PubMed:15866882}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=13.4 pmol/min/mg enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphocholine as substrate (at 37
CC degrees Celsius) {ECO:0000269|PubMed:15866882};
CC Vmax=8.1 pmol/min/mg enzyme with 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphocholine as substrate (at 37
CC degrees Celsius) {ECO:0000269|PubMed:15866882};
CC Vmax=14.5 pmol/min/mg enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine as substrate (at
CC 37 degrees Celsius) {ECO:0000269|PubMed:15866882};
CC Vmax=19.9 pmol/min/mg enzyme with 1-hexadecanoyl-2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphoethanolamine as substrate (at 37
CC degrees Celsius) {ECO:0000269|PubMed:15866882};
CC Vmax=16.4 pmol/min/mg enzyme with 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine as substrate (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:15866882};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000269|PubMed:15866882}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15866882}.
CC Membrane {ECO:0000305|PubMed:15866882}; Peripheral membrane protein
CC {ECO:0000305|PubMed:15866882}; Cytoplasmic side
CC {ECO:0000305|PubMed:15866882}. Note=Translocates to perinuclear
CC membranes that may correspond to endoplasmic reticulum or Golgi in a
CC calcium-dependent fashion. {ECO:0000269|PubMed:15866882}.
CC -!- TISSUE SPECIFICITY: Weakly or not expressed in most tissues. Detected
CC in placenta of 17.5 dpc embryos. {ECO:0000269|PubMed:15866882}.
CC -!- DOMAIN: The N-terminal C2 domain mediates the association with lipid
CC membranes upon calcium binding. An additional second C2 domain may
CC stand in between the C2 domain and the PLA2c domain.
CC {ECO:0000250|UniProtKB:Q86XP0}.
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DR EMBL; AB195276; BAD98152.1; -; mRNA.
DR EMBL; AK167492; BAE39570.1; -; mRNA.
DR EMBL; AK145985; BAE26807.1; -; mRNA.
DR EMBL; AL844608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS16617.1; -.
DR RefSeq; NP_001019308.1; NM_001024137.1.
DR AlphaFoldDB; Q50L43; -.
DR SMR; Q50L43; -.
DR STRING; 10090.ENSMUSP00000092252; -.
DR iPTMnet; Q50L43; -.
DR PhosphoSitePlus; Q50L43; -.
DR PaxDb; 10090-ENSMUSP00000092252; -.
DR ProteomicsDB; 294370; -.
DR Antibodypedia; 23488; 92 antibodies from 22 providers.
DR DNASU; 78390; -.
DR Ensembl; ENSMUST00000094665.5; ENSMUSP00000092252.5; ENSMUSG00000070719.5.
DR GeneID; 78390; -.
DR KEGG; mmu:78390; -.
DR UCSC; uc008lvh.1; mouse.
DR AGR; MGI:1925640; -.
DR CTD; 283748; -.
DR MGI; MGI:1925640; Pla2g4d.
DR VEuPathDB; HostDB:ENSMUSG00000070719; -.
DR eggNOG; KOG1028; Eukaryota.
DR eggNOG; KOG1325; Eukaryota.
DR GeneTree; ENSGT01030000234606; -.
DR HOGENOM; CLU_011663_0_0_1; -.
DR InParanoid; Q50L43; -.
DR OMA; NSSHPVW; -.
DR OrthoDB; 4250045at2759; -.
DR PhylomeDB; Q50L43; -.
DR TreeFam; TF325228; -.
DR Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR Reactome; R-MMU-1482801; Acyl chain remodelling of PS.
DR Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
DR Reactome; R-MMU-1482925; Acyl chain remodelling of PG.
DR Reactome; R-MMU-1483115; Hydrolysis of LPC.
DR Reactome; R-MMU-1483166; Synthesis of PA.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 78390; 3 hits in 78 CRISPR screens.
DR PRO; PR:Q50L43; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q50L43; Protein.
DR Bgee; ENSMUSG00000070719; Expressed in esophagus and 26 other cell types or tissues.
DR Genevisible; Q50L43; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047498; F:calcium-dependent phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; ISS:UniProtKB.
DR CDD; cd04036; C2_cPLA2; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR041847; C2_cPLA2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR040723; cPLA2_C2.
DR InterPro; IPR002642; LysoPLipase_cat_dom.
DR PANTHER; PTHR10728; CYTOSOLIC PHOSPHOLIPASE A2; 1.
DR PANTHER; PTHR10728:SF31; CYTOSOLIC PHOSPHOLIPASE A2 DELTA; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF18695; cPLA2_C2; 1.
DR Pfam; PF01735; PLA2_B; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00022; PLAc; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51210; PLA2C; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Reference proteome.
FT CHAIN 1..825
FT /note="Cytosolic phospholipase A2 delta"
FT /id="PRO_0000247024"
FT DOMAIN 14..133
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 281..825
FT /note="PLA2c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00555"
FT ACT_SITE 370
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q86XP0"
FT ACT_SITE 654
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P47712"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 339..340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q86XP0"
FT CONFLICT 222
FT /note="R -> G (in Ref. 2; BAE39570/BAE26807)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="E -> G (in Ref. 2; BAE39570/BAE26807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 825 AA; 93042 MW; 257668A34FFA841B CRC64;
MWSGDRRVGM ESLSPERLHG HPYQEEASVF CRLTVKILEA RSLPRADLLS QADPYVTVQL
PTASGMKFKT QTVTNSSHPV WNETFSFLIQ SQVKNILELT IYDEDVITKD DICFKVSYDV
SEILPGQLLQ KTFSLNPQGP EELDVELLME RTWDPPENLI TNNVLVAREL SHLDVSLDRA
GNTAMAAGQD KLELELMLKG SYEDTQTFFP DTAFTFSFHY MRGQDTELNG YLRGPRNSGW
NSDTSVTPFN VPLMSLAAGK EMTIDIPAMK APEGKLQLKT DCCPKELSVR LSYGLCPEEQ
AFLSRRKKVV AAALKQALQL DEDLNEDEVP VVGINAEGGG MRAMISLYGH LLALQKLGLL
DCVTYFSGIS GSTWTMAHLY RDPEWSQRDL EGPISHAREH VAKTLLKEFL PEHLASYRQT
LKLREEQGYT VTVADLWGLV LESKLHGQVT DQKLSGQRAA LERGQNPLPL YLSLNVKENH
LETLHFKEWV EFSPYEVGFL KYGGFVPSEL FGSEFFMGRL MKRLPESQIC FLEGIWSNLF
SVNLMDIWYD ITYGKDSNNF PVDVRNSEKE FSGSAGTSSG VEAPWLESGT ALAQALKGFL
TGRPFHQRSA NFLHGLQLHR DYCNQRHFST WADCNLDDTP NQLTPQDPQL CLIDAGCFMN
SSCPSLFRPG RQVDLIISFN YNQSLPFKGL QQSEKYSRAR GLPFPRVEPS PEDHSQPQEC
YLFSDPTCPE APVVLHFPLV NDSFRDHSAP GVRRSPDELK AGQVNLTGAA SPYFMYNMTY
KNEDFDRLLQ LSDYNVQNNQ GTILQALRTV LKRRASETRP LGVKT
//
