PPAP_MOUSE
ID PPAP_MOUSE Reviewed; 381 AA.
AC Q8CE08; A4QPG2; B8JJZ5; B8JJZ6; Q8C682; Q9QXH7;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Prostatic acid phosphatase;
DE EC=3.1.3.2 {ECO:0000250|UniProtKB:P15309};
DE AltName: Full=5'-nucleotidase;
DE Short=5'-NT;
DE EC=3.1.3.5 {ECO:0000269|PubMed:18940592};
DE AltName: Full=Acid phosphatase 3;
DE AltName: Full=Ecto-5'-nucleotidase;
DE AltName: Full=Fluoride-resistant acid phosphatase;
DE Short=FRAP;
DE AltName: Full=Protein tyrosine phosphatase ACP3;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:P15309};
DE AltName: Full=Thiamine monophosphatase;
DE Short=TMPase;
DE Flags: Precursor;
GN Name=Acp3; Synonyms=Acpp;
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).
RA Crew M.D., Chatta G.S., Borg C.D.;
RT "Sequence and expression of mouse prostatic acid phosphatase.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Head, and 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 [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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17638863; DOI=10.1158/0008-5472.can-07-1651;
RA Quintero I.B., Araujo C.L., Pulkka A.E., Wirkkala R.S., Herrala A.M.,
RA Eskelinen E.-L., Jokitalo E., Hellstroem P.A., Tuominen H.J.,
RA Hirvikoski P.P., Vihko P.T.;
RT "Prostatic acid phosphatase is not a prostate specific target.";
RL Cancer Res. 67:6549-6554(2007).
RN [6]
RP DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY (ISOFORM 2), TISSUE SPECIFICITY
RP (ISOFORM 2), AND FUNCTION (ISOFORM 2).
RX PubMed=18940592; DOI=10.1016/j.neuron.2008.08.024;
RA Zylka M.J., Sowa N.A., Taylor-Blake B., Twomey M.A., Herrala A., Voikar V.,
RA Vihko P.;
RT "Prostatic acid phosphatase is an ectonucleotidase and suppresses pain by
RT generating adenosine.";
RL Neuron 60:111-122(2008).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=20084276; DOI=10.1371/journal.pone.0008674;
RA Taylor-Blake B., Zylka M.J.;
RT "Prostatic acid phosphatase is expressed in peptidergic and nonpeptidergic
RT nociceptive neurons of mice and rats.";
RL PLoS ONE 5:E8674-E8674(2010).
CC -!- FUNCTION: A non-specific tyrosine phosphatase that dephosphorylates a
CC diverse number of substrates under acidic conditions (pH 4-6) including
CC alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated
CC proteins. Has lipid phosphatase activity and inactivates
CC lysophosphatidic acid in seminal plasma (By similarity).
CC {ECO:0000250|UniProtKB:P15309}.
CC -!- FUNCTION: [Isoform 2]: In addition to its tyrosine phosphatase
CC activity, also has ecto-5'-nucleotidase activity in dorsal root
CC ganglion (DRG) neurons. Generates adenosine from AMP. This
CC extracellular adenosine leads to a decrease in chronic pain by
CC activating A1R in nociceptive neurons. {ECO:0000269|PubMed:18940592}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC Evidence={ECO:0000250|UniProtKB:P15309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC Evidence={ECO:0000269|PubMed:18940592};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:75757; Evidence={ECO:0000250|UniProtKB:P15309};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC Evidence={ECO:0000250|UniProtKB:P15309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000250|UniProtKB:P15309};
CC -!- SUBUNIT: Homodimer; dimer formation is required for phosphatase
CC activity. {ECO:0000250|UniProtKB:P20646}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted
CC {ECO:0000305|PubMed:17638863}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:17638863}; Single-pass type I membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17638863}; Single-
CC pass type I membrane protein {ECO:0000255}. Note=Appears to shuttle
CC between the cell membrane and intracellular vesicles. Colocalizes with
CC FLOT1 at cell membrane and in intracellular vesicles (PubMed:17638863).
CC Colocalizes with LAMP2 on the lysosome membrane (By similarity).
CC {ECO:0000250|UniProtKB:P15309, ECO:0000269|PubMed:17638863}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CE08-1; Sequence=Displayed;
CC Name=2; Synonyms=TMPase, TM-PAP, cellular PAP, cPAP;
CC IsoId=Q8CE08-2; Sequence=VSP_036024;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in salivary gland, thymus
CC and thyroid gland. {ECO:0000269|PubMed:17638863,
CC ECO:0000269|PubMed:18940592, ECO:0000269|PubMed:20084276}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Widely expressed in prostate lobes,
CC brain, kidney, liver, lung, muscle, placenta, salivary gland, spleen,
CC thyroid and thymus. Locates to Schwann cells and fibroblasts. Expressed
CC in peptidergic and non-peptidergic nociceptive (pain-sensing) neurons.
CC Preferentially expressed in non-peptidergic doral root ganglia neurons.
CC {ECO:0000269|PubMed:18940592}.
CC -!- DISRUPTION PHENOTYPE: Null mice display greater thermal hyperalgesia
CC (pain sensitivity) and mechanical allodynia. No thiamine
CC monophosphatase (TMPase) activity detected in dorsal root ganglion
CC (DRG) neurons. {ECO:0000269|PubMed:18940592}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {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; AF210243; AAF23171.1; -; mRNA.
DR EMBL; AK029273; BAC26366.1; -; mRNA.
DR EMBL; AK076383; BAC36318.1; -; mRNA.
DR EMBL; CT030733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139826; AAI39827.1; -; mRNA.
DR CCDS; CCDS23460.1; -. [Q8CE08-2]
DR CCDS; CCDS40750.1; -. [Q8CE08-1]
DR RefSeq; NP_062781.2; NM_019807.2. [Q8CE08-1]
DR RefSeq; NP_997551.1; NM_207668.2. [Q8CE08-2]
DR AlphaFoldDB; Q8CE08; -.
DR SMR; Q8CE08; -.
DR BioGRID; 207899; 3.
DR ComplexPortal; CPX-121; Prostatic acid phosphatase complex.
DR IntAct; Q8CE08; 1.
DR STRING; 10090.ENSMUSP00000059889; -.
DR GlyGen; Q8CE08; 3 sites.
DR PhosphoSitePlus; Q8CE08; -.
DR MaxQB; Q8CE08; -.
DR PaxDb; Q8CE08; -.
DR PeptideAtlas; Q8CE08; -.
DR PRIDE; Q8CE08; -.
DR ProteomicsDB; 289731; -. [Q8CE08-1]
DR ProteomicsDB; 289732; -. [Q8CE08-2]
DR Antibodypedia; 1343; 962 antibodies from 43 providers.
DR DNASU; 56318; -.
DR Ensembl; ENSMUST00000062723; ENSMUSP00000059889; ENSMUSG00000032561. [Q8CE08-2]
DR Ensembl; ENSMUST00000112590; ENSMUSP00000108209; ENSMUSG00000032561. [Q8CE08-1]
DR GeneID; 56318; -.
DR KEGG; mmu:56318; -.
DR UCSC; uc009rhl.1; mouse. [Q8CE08-2]
DR UCSC; uc009rhm.1; mouse. [Q8CE08-1]
DR CTD; 56318; -.
DR MGI; MGI:1928480; Acpp.
DR VEuPathDB; HostDB:ENSMUSG00000032561; -.
DR eggNOG; KOG3720; Eukaryota.
DR GeneTree; ENSGT00940000160450; -.
DR HOGENOM; CLU_030431_1_1_1; -.
DR InParanoid; Q8CE08; -.
DR OMA; GMKQHYE; -.
DR OrthoDB; 1221585at2759; -.
DR TreeFam; TF312893; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 56318; 0 hits in 74 CRISPR screens.
DR PRO; PR:Q8CE08; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8CE08; protein.
DR Bgee; ENSMUSG00000032561; Expressed in lacrimal gland and 97 other tissues.
DR ExpressionAtlas; Q8CE08; baseline and differential.
DR Genevisible; Q8CE08; MM.
DR GO; GO:1904097; C:acid phosphatase complex; ISO:MGI.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISS:CAFA.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0031985; C:Golgi cisterna; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:1904144; C:phosphatidylinositol phosphate phosphatase complex; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; ISO:MGI.
DR GO; GO:0012506; C:vesicle membrane; IDA:UniProtKB.
DR GO; GO:0008253; F:5'-nucleotidase activity; ISS:CAFA.
DR GO; GO:0003993; F:acid phosphatase activity; ISS:CAFA.
DR GO; GO:0033265; F:choline binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; ISS:CAFA.
DR GO; GO:0016791; F:phosphatase activity; ISS:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0042131; F:thiamine phosphate phosphatase activity; IMP:UniProtKB.
DR GO; GO:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046085; P:adenosine metabolic process; IDA:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISS:CAFA.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007040; P:lysosome organization; IBA:GO_Central.
DR GO; GO:0009117; P:nucleotide metabolic process; IMP:UniProtKB.
DR GO; GO:0060168; P:positive regulation of adenosine receptor signaling pathway; ISS:CAFA.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IMP:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:UniProtKB.
DR GO; GO:0006772; P:thiamine metabolic process; IMP:UniProtKB.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Lipid metabolism; Lysosome; Membrane; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT CHAIN 32..381
FT /note="Prostatic acid phosphatase"
FT /id="PRO_0000356293"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT ACT_SITE 289
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT SITE 48
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250"
FT SITE 137
FT /note="Required for dimerization"
FT /evidence="ECO:0000250|UniProtKB:P20646"
FT SITE 143
FT /note="Required for dimerization"
FT /evidence="ECO:0000250|UniProtKB:P20646"
FT SITE 205
FT /note="Required for structural stability"
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..371
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT DISULFID 214..312
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT DISULFID 346..350
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT VAR_SEQ 378..381
FT /note="QGRN -> QVLRVILATTFCLVTGILVILLLVLIRHGPCWQRDVYRNI (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_036024"
FT CONFLICT 2
FT /note="R -> G (in Ref. 4; AAI39827)"
FT /evidence="ECO:0000305"
FT CONFLICT 3
FT /note="A -> S (in Ref. 2; BAC36318)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="R -> P (in Ref. 4; AAI39827)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="V -> L (in Ref. 2; BAC36318)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="A -> P (in Ref. 2; BAC36318)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="N -> H (in Ref. 2; BAC36318)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="F -> L (in Ref. 2; BAC36318)"
FT /evidence="ECO:0000305"
FT CONFLICT 357..358
FT /note="EL -> DV (in Ref. 1; AAF23171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 43717 MW; C0077819D77CB251 CRC64;
MRAVPLPLSR TASLSLGFLL LLSLCLDPGQ AKELKFVTLV FRHGDRGPIE TFPTDPITES
SWPQGFGQLT QWGMEQHYEL GSYIRKRYGR FLNDTYKHDQ IYIRSTDVDR TLMSAMTNLA
ALFPPEGISI WNPRLLWQPI PVHTVSLSED RLLYLPFRDC PRFEELKSET LESEEFLKRL
HPYKSFLDTL SSLSGFDDQD LFGIWSKVYD PLFCESVHNF TLPSWATEDA MIKLKELSEL
SLLSLYGIHK QKEKSRLQGG VLVNEILKNM KLATQPQKYK KLVMYSAHDT TVSGLQMALD
VYNGVLPPYA SCHMMELYHD KGGHFVEMYY RNETQNEPYP LTLPGCTHSC PLEKFAELLD
PVISQDWATE CMATSSHQGR N
