ID   PI51C_RAT               Reviewed;         688 AA.
AC   Q5I6B8;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma {ECO:0000250|UniProtKB:O60331};
DE            Short=PIP5K1-gamma {ECO:0000250|UniProtKB:O60331};
DE            Short=PtdIns(4)P-5-kinase 1 gamma {ECO:0000250|UniProtKB:O60331};
DE            EC=2.7.1.68 {ECO:0000250|UniProtKB:O60331};
DE   AltName: Full=Phosphatidylinositol 4-phosphate 5-kinase type I gamma {ECO:0000250|UniProtKB:O60331};
DE            Short=PIP5KIgamma {ECO:0000250|UniProtKB:O60331};
GN   Name=Pip5k1c {ECO:0000312|RGD:1309938};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-188 AND ASP-316, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Hippocampus;
RX   PubMed=14741049; DOI=10.1042/bj20031394;
RA   Giudici M.-L., Emson P.C., Irvine R.F.;
RT   "A novel neuronal-specific splice variant of Type I phosphatidylinositol 4-
RT   phosphate 5-kinase isoform gamma.";
RL   Biochem. J. 379:489-496(2004).
RN   [2]
RP   FUNCTION, INTERACTION WITH ARF6, AND SUBCELLULAR LOCATION.
RX   PubMed=12847086; DOI=10.1083/jcb.200301006;
RA   Krauss M., Kinuta M., Wenk M.R., De Camilli P., Takei K., Haucke V.;
RT   "ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by
RT   activating phosphatidylinositol phosphate kinase type Igamma.";
RL   J. Cell Biol. 162:113-124(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554; SER-682; SER-686 AND
RP   THR-688, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-
CC       phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-
CC       bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that
CC       regulates several cellular processes such as signal transduction,
CC       vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and
CC       cell motility. PtdIns(4,5)P2 can directly act as a second messenger or
CC       can be utilized as a precursor to generate other second messengers:
CC       inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or
CC       phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (By
CC       similarity). PIP5K1A-mediated phosphorylation of PtdIns(4)P is the
CC       predominant pathway for PtdIns(4,5)P2 synthesis (By similarity).
CC       Together with PIP5K1A, is required for phagocytosis, both enzymes
CC       regulating different types of actin remodeling at sequential steps (By
CC       similarity). Promotes particle attachment by generating the pool of
CC       PtdIns(4,5)P2 that induces controlled actin depolymerization to
CC       facilitate Fc-gamma-R clustering. Mediates RAC1-dependent
CC       reorganization of actin filaments (By similarity). Required for
CC       synaptic vesicle transport (By similarity). Controls the plasma
CC       membrane pool of PtdIns(4,5)P2 implicated in synaptic vesicle
CC       endocytosis and exocytosis. Plays a role in endocytosis mediated by
CC       clathrin and AP-2 (adaptor protein complex 2) (PubMed:12847086).
CC       Required for clathrin-coated pits assembly at the synapse
CC       (PubMed:12847086). Participates in cell junction assembly. Modulates
CC       adherens junctions formation by facilitating CDH1/cadherin trafficking.
CC       Required for focal adhesion dynamics. Modulates the targeting of talins
CC       (TLN1 and TLN2) to the plasma membrane and their efficient assembly
CC       into focal adhesions. Regulates the interaction between talins (TLN1
CC       and TLN2) and beta-integrins (By similarity). Required for uropodium
CC       formation and retraction of the cell rear during directed migration.
CC       Has a role in growth factor-stimulated directional cell migration and
CC       adhesion (By similarity). Required for talin assembly into nascent
CC       adhesions forming at the leading edge toward the direction of the
CC       growth factor (By similarity). Negative regulator of T-cell activation
CC       and adhesion. Negatively regulates integrin alpha-L/beta-2 (LFA-1)
CC       polarization and adhesion induced by T-cell receptor. Together with
CC       PIP5K1A has a role during embryogenesis and together with PIP5K1B may
CC       have a role immediately after birth (By similarity).
CC       {ECO:0000250|UniProtKB:O60331, ECO:0000250|UniProtKB:O70161,
CC       ECO:0000250|UniProtKB:P70182, ECO:0000269|PubMed:12847086}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC         phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC         inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178,
CC         ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68;
CC         Evidence={ECO:0000250|UniProtKB:O60331};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14426;
CC         Evidence={ECO:0000250|UniProtKB:O60331};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-
CC         3-phospho-1D-myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-
CC         (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol
CC         4,5-bisphosphate + ADP + H(+); Xref=Rhea:RHEA:40363,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77136,
CC         ChEBI:CHEBI:77137, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:O60331};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40364;
CC         Evidence={ECO:0000250|UniProtKB:O60331};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-
CC         myo-inositol 4-phosphate + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-
CC         sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:40367, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:77139, ChEBI:CHEBI:77140, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:O60331};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40368;
CC         Evidence={ECO:0000250|UniProtKB:O60331};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phospho-1D-
CC         myo-inositol + ATP = 1-octadecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC         phospho-1D-myo-inositol 5-phosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:40379, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:77163, ChEBI:CHEBI:77164, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:O60331};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40380;
CC         Evidence={ECO:0000250|UniProtKB:O60331};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC         phospho-1D-myo-inositol + ATP = 1-octadecanoyl-2-(9Z,12Z)-
CC         octadecadienoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate +
CC         ADP + H(+); Xref=Rhea:RHEA:40383, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:77158, ChEBI:CHEBI:77159,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O60331};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40384;
CC         Evidence={ECO:0000250|UniProtKB:O60331};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phospho-(1D-myo-inositol) + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 5-phosphate +
CC         ADP + H(+); Xref=Rhea:RHEA:40375, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:77160, ChEBI:CHEBI:133606,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O60331};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40376;
CC         Evidence={ECO:0000250|UniProtKB:O60331};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-di-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-1D-myo-
CC         inositol + ATP = 1,2-di(9Z,12Z)-octadecadienoyl-sn-glycero-3-phospho-
CC         1D-myo-inositol 5-phosphate + ADP + H(+); Xref=Rhea:RHEA:40387,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77165,
CC         ChEBI:CHEBI:77167, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:O60331};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40388;
CC         Evidence={ECO:0000250|UniProtKB:O60331};
CC   -!- SUBUNIT: Interacts with TLN1 (By similarity). Interacts with TLN2;
CC       interaction stimulates 1-phosphatidylinositol-4-phosphate 5-kinase
CC       activity (By similarity). May compete with beta-integrins for the same
CC       binding site on TLN1 and TLN2 (By similarity). Interacts with ARF6;
CC       interaction stimulates 1-phosphatidylinositol-4-phosphate 5-kinase
CC       activity (PubMed:12847086). Interacts with AP2B1 (By similarity).
CC       Interacts with AP2M1; phosphorylation of PIP5K1C by CSK disrupts the
CC       interaction; clathrin competes with PIP5K1C (By similarity). Interacts
CC       with CDH1 (By similarity). Interacts with CSK (By similarity).
CC       Interacts with PLCG1; interaction is abolished upon EGF stimulation (By
CC       similarity). Interacts with LAPTM4B; promotes SNX5 association with
CC       LAPTM4B; kinase activity of PIP5K1C is required; interaction is
CC       regulated by phosphatidylinositol 4,5-bisphosphate generated by PIP5K1C
CC       (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:O60331,
CC       ECO:0000250|UniProtKB:O70161, ECO:0000269|PubMed:12847086}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12847086};
CC       Peripheral membrane protein {ECO:0000269|PubMed:12847086}; Cytoplasmic
CC       side {ECO:0000269|PubMed:12847086}. Endomembrane system
CC       {ECO:0000269|PubMed:12847086}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O70161}. Cell junction, focal adhesion
CC       {ECO:0000250|UniProtKB:O60331}. Cell junction, adherens junction
CC       {ECO:0000250|UniProtKB:O60331}. Cell projection, ruffle membrane
CC       {ECO:0000269|PubMed:12847086}. Cell projection, phagocytic cup
CC       {ECO:0000250|UniProtKB:O70161}. Cell projection, uropodium
CC       {ECO:0000250|UniProtKB:O70161}.
CC   -!- PTM: Phosphorylation on Ser-672 negatively regulates binding to TLN2
CC       and is strongly stimulated in mitosis. Phosphorylation on Tyr-671 is
CC       necessary for targeting to focal adhesions. Phosphorylation on Ser-672
CC       and Tyr-671 are mutually exclusive. Phosphorylated by SYK and CSK.
CC       Tyrosine phosphorylation is enhanced by PTK2 signaling. Phosphorylated
CC       at Tyr-635 upon EGF stimulation. Some studies suggest that
CC       phosphorylation on Tyr-671 enhances binding to tailins (TLN1 and TLN2)
CC       (By similarity); others that phosphorylation at Tyr-671 does not
CC       directly enhance binding to tailins (TLN1 and TLN2) but may act
CC       indirectly by inhibiting phosphorylation at Ser-672. {ECO:0000250}.
CC   -!- PTM: Acetylation at Lys-265 and Lys-268 seems to decrease lipid kinase
CC       activity. Deacetylation of these sites by SIRT1 positively regulates
CC       the exocytosis of TSH-containing granules from pituitary cells (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; AY850259; AAW34235.1; -; mRNA.
DR   RefSeq; NP_001009967.2; NM_001009967.2.
DR   RefSeq; NP_001029142.1; NM_001033970.1.
DR   AlphaFoldDB; Q5I6B8; -.
DR   SMR; Q5I6B8; -.
DR   BioGRID; 260791; 2.
DR   STRING; 10116.ENSRNOP00000057873; -.
DR   iPTMnet; Q5I6B8; -.
DR   PhosphoSitePlus; Q5I6B8; -.
DR   SwissPalm; Q5I6B8; -.
DR   PaxDb; 10116-ENSRNOP00000057873; -.
DR   GeneID; 314641; -.
DR   KEGG; rno:314641; -.
DR   UCSC; RGD:1309938; rat.
DR   AGR; RGD:1309938; -.
DR   CTD; 23396; -.
DR   RGD; 1309938; Pip5k1c.
DR   eggNOG; KOG0229; Eukaryota.
DR   InParanoid; Q5I6B8; -.
DR   OrthoDB; 5481504at2759; -.
DR   PhylomeDB; Q5I6B8; -.
DR   Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR   Reactome; R-RNO-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR   Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:Q5I6B8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR   GO; GO:0098835; C:presynaptic endocytic zone membrane; IDA:SynGO.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001931; C:uropod; IEA:UniProtKB-SubCell.
DR   GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISO:RGD.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:RGD.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0070527; P:platelet aggregation; ISO:RGD.
DR   GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:RGD.
DR   GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:RGD.
DR   CDD; cd17308; PIPKc_PIP5K1C; 1.
DR   Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR   Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR   InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR   InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR   InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR   InterPro; IPR023610; PInositol-4/5-P-5/4-kinase.
DR   PANTHER; PTHR23086:SF26; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE TYPE-1 GAMMA; 1.
DR   PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 1.
DR   Pfam; PF01504; PIP5K; 1.
DR   SMART; SM00330; PIPKc; 1.
DR   SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR   PROSITE; PS51455; PIPK; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cell adhesion; Cell junction; Cell membrane;
KW   Cell projection; Chemotaxis; Cytoplasm; Endocytosis; Exocytosis; Kinase;
KW   Lipid metabolism; Membrane; Methylation; Nucleotide-binding; Phagocytosis;
KW   Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..688
FT                   /note="Phosphatidylinositol 4-phosphate 5-kinase type-1
FT                   gamma"
FT                   /id="PRO_0000185464"
FT   DOMAIN          75..443
FT                   /note="PIPK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT   REGION          48..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..541
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..565
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         265
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O60331"
FT   MOD_RES         268
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O60331"
FT   MOD_RES         459
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O70161"
FT   MOD_RES         459
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O70161"
FT   MOD_RES         554
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         635
FT                   /note="Phosphotyrosine; by EGFR"
FT                   /evidence="ECO:0000250|UniProtKB:O70161"
FT   MOD_RES         671
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000250|UniProtKB:O60331"
FT   MOD_RES         672
FT                   /note="Phosphoserine; by CDK5, MAPK1 and CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:O60331"
FT   MOD_RES         682
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         686
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         688
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MUTAGEN         188
FT                   /note="K->A: Reduces activity by over 99%."
FT                   /evidence="ECO:0000269|PubMed:14741049"
FT   MUTAGEN         316
FT                   /note="D->K: Loss of kinase activity."
FT                   /evidence="ECO:0000269|PubMed:14741049"
SQ   SEQUENCE   688 AA;  75594 MW;  F34E175EFFF54D5D CRC64;
     MELEVPDEAE SAEAGAVTAE AAWSAESGAA AGMTQKKAIL AEAPLVTGQP GPGHGKKLGH
     RGVDASGETT YKKTTSSTLK GAIQLGIGYT VGNLSSKPER DVLMQDFYVV ESIFFPSEGS
     NLTPAHHFQD FRFKTYAPVA FRYFRELFGI RPDDYLYSLC NEPLIELSNP GASGSVFYVT
     SDDEFIIKTV MHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG KNIRVVVMNN
     VLPRVVKMHL KFDLKGSTYK RRASKKEKEK SLPTYKDLDF MQDMPEGLLL DSDTFGALVK
     TLQRDCLVLE SFKIMDYSLL LGVHNIDQQE RERQAEGAQS KADEKRPVAQ KALYSTARES
     IQGGAARGEA IETDDTMGGI PAVNGRGERL LLHIGIIDIL QSYRFIKKLE HTWKALVHDG
     DTVSVHRPSF YAERFFKFMS STVFRKSSSL KSSPSKKGRG ALLAVKPLGP TAAFSASQIP
     SEREDVQYDL RGARSYPTLE DEGRPDLLPC TPPSFEEATT ASIATTLSST SLSIPERSPS
     DTSEQPRYRR RTQSSGQDGR PQEELHAEDL QKITVQVEPV CGVGVVVPKE QGAGVEVPPS
     GASAAATVEV DAASQASEPA SQASDEEDAP STDIYFFAHG RYWLFSPRRR RLRAVTPSHT
     GAPTDGRSWV YSPLHYSARP ASDGESDT
//