INP53_YEAST
ID INP53_YEAST Reviewed; 1107 AA.
AC Q12271; D6W2G8;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Polyphosphatidylinositol phosphatase INP53 {ECO:0000303|PubMed:10224048};
DE AltName: Full=Suppressor of PMA1 protein 2;
DE AltName: Full=Synaptojanin-like protein 3;
DE Includes:
DE RecName: Full=SAC1-like phosphoinositide phosphatase;
DE EC=3.1.3.-;
DE Includes:
DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase;
DE EC=3.1.3.36 {ECO:0000269|PubMed:10224048};
GN Name=INP53; Synonyms=SJL3, SOP2; OrderedLocusNames=YOR109W;
GN ORFNames=YOR3231w;
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 [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, DOMAIN, AND CATALYTIC ACTIVITY.
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 [8]
RP FUNCTION.
RX PubMed=10029994;
RX DOI=10.1002/(sici)1097-0061(19990130)15:2<155::aid-yea342>3.0.co;2-u;
RA Saiz J.E., de Los Angeles Santos M., Vazquez de Aldana C.R., Revuelta J.L.;
RT "Disruption of six unknown open reading frames from Saccharomyces
RT cerevisiae reveals two genes involved in vacuolar morphogenesis and one
RT gene required for sporulation.";
RL Yeast 15:155-164(1999).
RN [9]
RP FUNCTION.
RX PubMed=10628971; DOI=10.1093/genetics/154.1.83;
RA Bensen E.S., Costaguta G., Payne G.S.;
RT "Synthetic genetic interactions with temperature-sensitive clathrin in
RT Saccharomyces cerevisiae. Roles for synaptojanin-like Inp53p and dynamin-
RT related Vps1p in clathrin-dependent protein sorting at the trans-Golgi
RT network.";
RL Genetics 154:83-97(2000).
RN [10]
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 [11]
RP FUNCTION, DOMAIN, 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=11598201; DOI=10.1091/mbc.12.10.3175;
RA Ha S.-A., Bunch J.T., Hama H., DeWald D.B., Nothwehr S.F.;
RT "A novel mechanism for localizing membrane proteins to yeast trans-Golgi
RT network requires function of synaptojanin-like protein.";
RL Mol. Biol. Cell 12:3175-3190(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 FUNCTION, DOMAINS, MUTAGENESIS OF CYS-421; CYS-424; ARG-427; ASP-746 AND
RP ASN-748, AND INTERACTION WITH CHC1.
RX PubMed=12686590; DOI=10.1091/mbc.e02-10-0686;
RA Ha S.-A., Torabinejad J., DeWald D.B., Wenk M.R., Lucast L., De Camilli P.,
RA Newitt R.A., Aebersold R., Nothwehr S.F.;
RT "The synaptojanin-like protein Inp53/Sjl3 functions with clathrin in a
RT yeast TGN-to-endosome pathway distinct from the GGA protein-dependent
RT pathway.";
RL Mol. Biol. Cell 14:1319-1333(2003).
RN [15]
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 [16]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [17]
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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1105, 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1035, 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-986 AND THR-1105, AND
RP 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).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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. Plays an essential role in a TGN
CC (trans Golgi network)-to-early endosome pathway. Involved in clathrin-
CC mediated protein sorting at the TGN. {ECO:0000269|PubMed:10029994,
CC ECO:0000269|PubMed:10224048, ECO:0000269|PubMed:10625610,
CC ECO:0000269|PubMed:10628971, ECO:0000269|PubMed:11094088,
CC ECO:0000269|PubMed:11598201, ECO:0000269|PubMed:12686590,
CC ECO:0000269|PubMed:15169871, ECO:0000269|PubMed:15691741,
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22765;
CC Evidence={ECO:0000305|PubMed:10224048};
CC -!- SUBUNIT: Interacts with BSP1 and CHC1. {ECO:0000269|PubMed:12606027,
CC ECO:0000269|PubMed:12686590}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11094088,
CC ECO:0000269|PubMed:14562095}. Note=Cytoplasmic punctate structures.
CC Hyperosmotic stress causes translocation to actin patches.
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).
CC -!- DOMAIN: The 5-phosphatase domain (residues 568 to 856) selectively
CC removes the phosphate group at the 5' position of inositol of
CC phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2).
CC -!- DOMAIN: The C-terminal proline-rich domain is required for the function
CC and associates with clathrin heavy chain CHC1.
CC -!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; X94335; CAA64029.1; -; Genomic_DNA.
DR EMBL; Z75017; CAA99307.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10884.1; -; Genomic_DNA.
DR PIR; S61667; S61667.
DR RefSeq; NP_014752.3; NM_001183528.3.
DR AlphaFoldDB; Q12271; -.
DR SMR; Q12271; -.
DR BioGRID; 34505; 317.
DR DIP; DIP-2555N; -.
DR IntAct; Q12271; 14.
DR MINT; Q12271; -.
DR STRING; 4932.YOR109W; -.
DR iPTMnet; Q12271; -.
DR MaxQB; Q12271; -.
DR PaxDb; Q12271; -.
DR PRIDE; Q12271; -.
DR EnsemblFungi; YOR109W_mRNA; YOR109W; YOR109W.
DR GeneID; 854276; -.
DR KEGG; sce:YOR109W; -.
DR SGD; S000005635; INP53.
DR VEuPathDB; FungiDB:YOR109W; -.
DR eggNOG; KOG0566; Eukaryota.
DR GeneTree; ENSGT00940000170400; -.
DR HOGENOM; CLU_003016_2_0_1; -.
DR InParanoid; Q12271; -.
DR OMA; ECFVAIV; -.
DR BioCyc; YEAST:YOR109W-MON; -.
DR Reactome; R-SCE-1660499; Synthesis of PIPs at the plasma membrane.
DR PRO; PR:Q12271; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12271; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0016020; C:membrane; IDA:SGD.
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; Endocytosis; Hydrolase; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1107
FT /note="Polyphosphatidylinositol phosphatase INP53"
FT /id="PRO_0000268681"
FT DOMAIN 142..482
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT REGION 926..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..974
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50942"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1035
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1105
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 421
FT /note="C->A: Reduces hydrolysis of PtdIns(4)P; when
FT associated with A-424 and A-427."
FT /evidence="ECO:0000269|PubMed:12686590"
FT MUTAGEN 424
FT /note="C->A: Reduces hydrolysis of PtdIns(4)P; when
FT associated with A-421 and A-427."
FT /evidence="ECO:0000269|PubMed:12686590"
FT MUTAGEN 427
FT /note="R->A: Reduces hydrolysis of PtdIns(4)P; when
FT associated with A-421 and A-424."
FT /evidence="ECO:0000269|PubMed:12686590"
FT MUTAGEN 746
FT /note="D->A: Abolishes hydrolysis of PtdIns(4,5)P2; when
FT associated with A-748."
FT /evidence="ECO:0000269|PubMed:12686590"
FT MUTAGEN 748
FT /note="N->A: Abolishes hydrolysis of PtdIns(4,5)P2; when
FT associated with A-746."
FT /evidence="ECO:0000269|PubMed:12686590"
SQ SEQUENCE 1107 AA; 124577 MW; 1E024F15085261EA CRC64;
MIIFVSEEPE RRLAIVSNLY ALVLKPVGKK PSDKPLCAIE LLQKNDLKKY GFKRLTSHEI
FGVIGLIEVN GLLFVGAITG KSKVAQPCPG ETVNKIFAVD FFCLNDNSWD FIEIDSSGYP
VLPETASTEY QDALPKHPCY ELKKLLSNGS FYYSSDFDLT STLQHRGYGQ HSLSTDTYEE
EYMWNSFLMQ EMITYRDHLD TNLKQILDDE GFLTTVIRGF AETFVSYVKK LKVALTIISK
QSWKRAGTRF NARGVDDEAN VANFVETEFI MYSSQYCYAF TQIRGSIPVF WEQGTSLINP
RVQITRSFEA TQPVFDKHIM KSVEKYGPVH VVNLLSTKSS EIELSKRYKE HLTHSKKLNF
NKDIFLTEFD FHKETSQEGF SGVRKLIPLI LDSLLSSGYY SYDVREKKNI SEQHGIFRTN
CLDCLDRTNL AQQIISLAAF RTFLEDFRLI SSNSFIDDDD FVSKHNTLWA DHGDQISQIY
TGTNALKSSF SRKGKMSLAG ALSDATKSVS RIYINNFMDK EKQQNIDTLL GRLPYQKAVQ
LYDPVNEYVS TKLQSMSDKF TSTSNINLLI GSFNVNGATK KVDLSKWLFP IGEKFKPDIV
VLGLQEVIEL SAGSILNADY SKSSFWENLV GDCLNQYDDK YLLLRVEQMT SLLILFFVKA
DKAKYVKQVE GATKKTGFRG MAGNKGAVSI RFEYGATSFC FVNSHLAAGA TNVEERRSDY
ESIVRGITFT RTKMIPHHDS IFWLGDMNYR INLPNEDVRR ELLNQEEGYI DKLLHFDQLT
LGINSGSVFE GFKEPTLKFR PTYKYDPGTG TYDSSEKERT PSWTDRIIYK GENLLPLSYS
DAPIMISDHR PVYAAYRAKI TFVDDKERLS LKKRLFTEYK QEHPEEPGSL ISDLLSLDLD
NKSTDGFKSS SESSLLDIDP IMAQPTASSV ASSSPVSSAS ASLQPVRTQN SSQSRTPIKK
PVLRPPPPPA HKSVSAPAPS TSKEKSPTPQ TSTASLSSVT KNIQENKPLA QNRRIPPPGF
SQNILTPKST SNLASPMSSK VDLYNSASES TRSAQDARQQ TPTAFAASRD VNGQPEALLG
DENPIEPEEK AKLNHMTLDS WQPLTPK
