INP52_YEAST
ID INP52_YEAST Reviewed; 1183 AA.
AC P50942; D6W174;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Polyphosphatidylinositol phosphatase INP52 {ECO:0000303|PubMed:9560389};
DE AltName: Full=Synaptojanin-like protein 2 {ECO:0000303|PubMed:9788876};
DE Includes:
DE RecName: Full=SAC1-like phosphoinositide phosphatase {ECO:0000303|PubMed:10224048};
DE EC=3.1.3.- {ECO:0000269|PubMed:10224048};
DE Includes:
DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase {ECO:0000303|PubMed:10224048};
DE EC=3.1.3.36 {ECO:0000269|PubMed:10224048};
GN Name=INP52 {ECO:0000303|PubMed:9560389};
GN Synonyms=SJL2 {ECO:0000303|PubMed:9788876}; OrderedLocusNames=YNL106C;
GN ORFNames=N2160;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1102.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8701612;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<403::aid-yea923>3.0.co;2-h;
RA Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.;
RT "The sequence of a 21.3 kb DNA fragment from the left arm of yeast
RT chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading
RT frames.";
RL Yeast 12:403-409(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 880-1183.
RX PubMed=9090055;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<261::aid-yea64>3.0.co;2-l;
RA de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D.,
RA Pallavicini A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces
RT cerevisiae reveals an unusually high number of overlapping open reading
RT frames.";
RL Yeast 13:261-266(1997).
RN [5]
RP FUNCTION.
RX PubMed=9265642; DOI=10.1083/jcb.138.4.731;
RA Luo W.-J., Chang A.;
RT "Novel genes involved in endosomal traffic in yeast revealed by suppression
RT of a targeting-defective plasma membrane ATPase mutant.";
RL J. Cell Biol. 138:731-746(1997).
RN [6]
RP FUNCTION.
RX PubMed=9560389; DOI=10.1093/genetics/148.4.1715;
RA Stolz L.E., Huynh C.V., Thorner J., York J.D.;
RT "Identification and characterization of an essential family of inositol
RT polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the
RT yeast Saccharomyces cerevisiae.";
RL Genetics 148:1715-1729(1998).
RN [7]
RP FUNCTION.
RX PubMed=9788876; DOI=10.1242/jcs.111.22.3347;
RA Singer-Krueger B., Nemoto Y., Daniell L., Ferro-Novick S., De Camilli P.;
RT "Synaptojanin family members are implicated in endocytic membrane traffic
RT in yeast.";
RL J. Cell Sci. 111:3347-3356(1998).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=10224048; DOI=10.1074/jbc.274.19.12990;
RA Guo S., Stolz L.E., Lemrow S.M., York J.D.;
RT "SAC1-like domains of yeast SAC1, INP52, and INP53 and of human
RT synaptojanin encode polyphosphoinositide phosphatases.";
RL J. Biol. Chem. 274:12990-12995(1999).
RN [9]
RP FUNCTION.
RX PubMed=10625610; DOI=10.1074/jbc.275.2.801;
RA Hughes W.E., Woscholski R., Cooke F.T., Patrick R.S., Dove S.K.,
RA McDonald N.Q., Parker P.J.;
RT "SAC1 encodes a regulated lipid phosphoinositide phosphatase, defects in
RT which can be suppressed by the homologous Inp52p and Inp53p phosphatases.";
RL J. Biol. Chem. 275:801-808(2000).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF GLU-631; HIS-730 AND ASP-771.
RX PubMed=10962003; DOI=10.1074/jbc.m006244200;
RA Whisstock J.C., Romero S., Gurung R., Nandurkar H., Ooms L.M.,
RA Bottomley S.P., Mitchell C.A.;
RT "The inositol polyphosphate 5-phosphatases and the apurinic/apyrimidinic
RT base excision repair endonucleases share a common mechanism for
RT catalysis.";
RL J. Biol. Chem. 275:37055-37061(2000).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11094088; DOI=10.1128/mcb.20.24.9376-9390.2000;
RA Ooms L.M., McColl B.K., Wiradjaja F., Wijayaratnam A.P.W., Gleeson P.,
RA Gething M.J., Sambrook J.F., Mitchell C.A.;
RT "The yeast inositol polyphosphate 5-phosphatases inp52p and inp53p
RT translocate to actin patches following hyperosmotic stress: mechanism for
RT regulating phosphatidylinositol 4,5-bisphosphate at plasma membrane
RT invaginations.";
RL Mol. Cell. Biol. 20:9376-9390(2000).
RN [12]
RP FUNCTION.
RX PubMed=11311145; DOI=10.1042/bj3550805;
RA O'Malley C.J., McColl B.K., Kong A.M., Ellis S.L., Wijayaratnam A.P.W.,
RA Sambrook J., Mitchell C.A.;
RT "Mammalian inositol polyphosphate 5-phosphatase II can compensate for the
RT absence of all three yeast Sac1-like-domain-containing 5-phosphatases.";
RL Biochem. J. 355:805-817(2001).
RN [13]
RP INTERACTION WITH BSP1.
RX PubMed=12606027; DOI=10.1016/s0014-5793(03)00067-x;
RA Wicky S., Frischmuth S., Singer-Krueger B.;
RT "Bsp1p/Ypr171p is an adapter that directly links some synaptojanin family
RT members to the cortical actin cytoskeleton in yeast.";
RL FEBS Lett. 537:35-41(2003).
RN [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [15]
RP FUNCTION.
RX PubMed=15169871; DOI=10.1091/mbc.e04-03-0209;
RA Parrish W.R., Stefan C.J., Emr S.D.;
RT "Essential role for the myotubularin-related phosphatase Ymr1p and the
RT synaptojanin-like phosphatases Sjl2p and Sjl3p in regulation of
RT phosphatidylinositol 3-phosphate in yeast.";
RL Mol. Biol. Cell 15:3567-3579(2004).
RN [16]
RP FUNCTION.
RX PubMed=15691741; DOI=10.1016/j.femsyr.2004.09.007;
RA Nguyen P.H., Hasek J., Kohlwein S.D., Romero C., Choi J.H., Vancura A.;
RT "Interaction of Pik1p and Sjl proteins in membrane trafficking.";
RL FEMS Yeast Res. 5:363-371(2005).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ABP1.
RX PubMed=15798181; DOI=10.1128/mcb.25.8.2910-2923.2005;
RA Stefan C.J., Padilla S.M., Audhya A., Emr S.D.;
RT "The phosphoinositide phosphatase Sjl2 is recruited to cortical actin
RT patches in the control of vesicle formation and fission during
RT endocytosis.";
RL Mol. Cell. Biol. 25:2910-2923(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1005, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16406366; DOI=10.1016/j.febslet.2005.12.082;
RA Boettcher C., Wicky S., Schwarz H., Singer-Krueger B.;
RT "Sjl2p is specifically involved in early steps of endocytosis intimately
RT linked to actin dynamics via the Ark1p/Prk1p kinases.";
RL FEBS Lett. 580:633-641(2006).
RN [20]
RP FUNCTION.
RX PubMed=17452534; DOI=10.1083/jcb.200611011;
RA Sun Y., Carroll S., Kaksonen M., Toshima J.Y., Drubin D.G.;
RT "PtdIns(4,5)P2 turnover is required for multiple stages during
RT clathrin- and actin-dependent endocytic internalization.";
RL J. Cell Biol. 177:355-367(2007).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1032, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-1005 AND SER-1016,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Dephosphorylates a number of phosphatidylinositols (PIs) like
CC phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), but also
CC phosphatidylinositol 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-
CC phosphate (PtdIns(4)P), and phosphatidylinositol 3,5-bisphosphate
CC (PtdIns(3,5)P2). Controls the cellular levels and subcellular
CC distribution of phosphatidylinositol 3-phosphate and
CC phosphatidylinositol 4,5-bisphosphate. Specifically functions within
CC the early endocytic pathway and actin organization.
CC {ECO:0000269|PubMed:10224048, ECO:0000269|PubMed:10625610,
CC ECO:0000269|PubMed:10962003, ECO:0000269|PubMed:11094088,
CC ECO:0000269|PubMed:11311145, ECO:0000269|PubMed:15169871,
CC ECO:0000269|PubMed:15691741, ECO:0000269|PubMed:15798181,
CC ECO:0000269|PubMed:16406366, ECO:0000269|PubMed:17452534,
CC ECO:0000269|PubMed:9265642, ECO:0000269|PubMed:9560389,
CC ECO:0000269|PubMed:9788876}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC Evidence={ECO:0000269|PubMed:10224048};
CC -!- SUBUNIT: Interacts with ABP1 and BSP1. {ECO:0000269|PubMed:12606027,
CC ECO:0000269|PubMed:15798181}.
CC -!- INTERACTION:
CC P50942; P15891: ABP1; NbExp=2; IntAct=EBI-28834, EBI-2036;
CC P50942; Q06604: BSP1; NbExp=4; IntAct=EBI-28834, EBI-37047;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:11094088, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15798181, ECO:0000269|PubMed:16406366}.
CC -!- DOMAIN: The SAC1 domain is capable of hydrolyzing phosphatidylinositol
CC 3-phosphate (PtdIns(3)P), phosphatidylinositol 4-phosphate
CC (PtdIns(4)P), and phosphatidylinositol 3,5-bisphosphate
CC (PtdIns(3,5)P2). {ECO:0000269|PubMed:10224048}.
CC -!- SIMILARITY: Belongs to the synaptojanin family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the inositol 1,4,5-
CC trisphosphate 5-phosphatase family. {ECO:0000305}.
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DR EMBL; Z71382; CAA95982.1; -; Genomic_DNA.
DR EMBL; Z69382; CAA93402.1; -; Genomic_DNA.
DR EMBL; Z50161; CAA90520.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10440.1; -; Genomic_DNA.
DR PIR; S63046; S63046.
DR RefSeq; NP_014293.1; NM_001182944.1.
DR AlphaFoldDB; P50942; -.
DR BMRB; P50942; -.
DR SMR; P50942; -.
DR BioGRID; 35718; 190.
DR DIP; DIP-2764N; -.
DR IntAct; P50942; 25.
DR MINT; P50942; -.
DR STRING; 4932.YNL106C; -.
DR iPTMnet; P50942; -.
DR MaxQB; P50942; -.
DR PaxDb; P50942; -.
DR PRIDE; P50942; -.
DR EnsemblFungi; YNL106C_mRNA; YNL106C; YNL106C.
DR GeneID; 855618; -.
DR KEGG; sce:YNL106C; -.
DR SGD; S000005050; INP52.
DR VEuPathDB; FungiDB:YNL106C; -.
DR eggNOG; KOG0566; Eukaryota.
DR GeneTree; ENSGT00940000170400; -.
DR HOGENOM; CLU_003016_2_0_1; -.
DR InParanoid; P50942; -.
DR OMA; EDMLWNS; -.
DR BioCyc; YEAST:MON3O-69; -.
DR Reactome; R-SCE-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-SCE-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR Reactome; R-SCE-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR PRO; PR:P50942; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P50942; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043813; F:phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity; IDA:SGD.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IDA:SGD.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:SGD.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; IDA:SGD.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR002013; SAC_dom.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF02383; Syja_N; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS50275; SAC; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase; Lipid metabolism;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..1183
FT /note="Polyphosphatidylinositol phosphatase INP52"
FT /id="PRO_0000209745"
FT DOMAIN 167..507
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT REGION 133..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1018
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1127..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1005
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1032
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 1095
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12271"
FT MUTAGEN 631
FT /note="E->A: Impairs completely enzyme activity."
FT /evidence="ECO:0000269|PubMed:10962003"
FT MUTAGEN 730
FT /note="H->A: Impairs completely enzyme activity."
FT /evidence="ECO:0000269|PubMed:10962003"
FT MUTAGEN 771
FT /note="D->A: Impairs completely enzyme activity."
FT /evidence="ECO:0000269|PubMed:10962003"
SQ SEQUENCE 1183 AA; 133331 MW; 97B279870DFE6F65 CRC64;
MKILLSKQQT RKIAIVSETH GLVFRPINSK NSRRSTCAVE LVPKAELNGN GFRRLSNHEI
YGFIGLIEIE GLMFIATITG KSKVAQPIPN KTVNKIYAVD FFCLNNSKWD FMDIDSSGYP
IVTNDGDFAI SSPPSISTHS SRSSLRSSSS RSLNAQEQAP KHPCHELRKL LSNGSFYYST
DFDLTCTLQK RGFTEHSLSF DDFDREFMWN SFLMDEIITY RDRLDVTAKE LLDQRGFLTT
VIRGFAETIF SYINRLKVGL TIISRQSWKR AGTRFNARGI DDDGHVANFV ETEMIMYSSQ
YCYAFTQIRG SLPIFWEQDT SLISPKIQIT RSVEATQPTF DEHFIRLFKK YGPVHIINLL
STKSSEIQLS RRYKEQLKNS EKMKIGRDVF LTSFDFHRET SQDGFAAASR IIPKIRNTIL
DAGYFSYDVK EGRLISEQDG VFRTNCLDCL DRTNLIQQTI SLAVFKLFLE DFRLVKPSSF
IDDNEFVQKV NALWADNGDQ ISQIYTGTNA LKSSYSRKGK MSFSGALSDA TKSVSRMYIN
NFVDKGKQQN IDTLLGKLPH QQVVELYDPI CEYVNERLLE SEEKFTTHSN INLFVGTFNV
NGNSRRADLS KWLFPIGDKF KPDVVVLGLQ EVIELTAGSI LNADYTKSSF WETMVTDCLN
QYEEKYLLLR VEQMSSLLIL FFARSDRAYN IKEVGGSTKK TGFGGITGNK GAVAIRFDYG
ATSFCFVNTH LSAGASNIDE RRNDYNNIYR NITFPRSKTI PHHDSLFWLG DLNYRITLTN
DEVRRELRAQ KDGYIDRLLQ YDQLTQEINE GVVFQGFKEP TLQFRPTYKY DYGTDNYDTS
EKARTPSWTD RIIYKGENLH PLAYSDAPLK ISDHKPVYAA YRANVKFVDE KEKLNLVEKL
YAEYKNTHPE ALTTGPDELS HARMEKQKES IPLDATVQSA GIKLIDLDDT SSCVSPLLSG
PSPQPSVVGP GGLSNVSPDK SKLNVLPPPP PTSRHNKEPS SKLLSPTKEI SIVSVSPRKG
ESNLPALERH STPKPLPPVP ALSLSKPVSL QKSSSELQHA KETIDNGKIV PRPCPPIRRK
SSTAPDEIST STKNSGVSTT EDPEPAKAST KPEKPPVVKK PHYLSVAANK LNTSQEHSIK
VSPSNSKSEE ELPCKKKSKP KVPAKNPELE KLSVHPLKPC DPN
