ID   PI51B_HUMAN             Reviewed;         540 AA.
AC   O14986; A8K9L9; B4DIG7; P78518; P78519; Q5T5K6; Q5T5K8; Q5T5K9; Q5VZ00;
AC   Q7KYT5; Q8NHQ5; Q92749;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   22-APR-2020, entry version 150.
DE   RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase type-1 beta;
DE            Short=PIP5K1-beta;
DE            Short=PtdIns(4)P-5-kinase 1 beta;
DE            EC=2.7.1.68;
DE   AltName: Full=Phosphatidylinositol 4-phosphate 5-kinase type I beta;
DE            Short=PIP5KIbeta;
DE   AltName: Full=Protein STM-7;
DE   AltName: Full=Type I phosphatidylinositol 4-phosphate 5-kinase beta;
GN   Name=PIP5K1B; Synonyms=STM7;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=8841185; DOI=10.1038/ng1096-157;
RA   Carvajal J.J., Pook M.A., dos Santos M., Doudney K., Hillermann R.,
RA   Minogue S., Williamson R., Hsuan J.J., Chamberlain S.;
RT   "The Friedreich's ataxia gene encodes a novel phosphatidylinositol-4-
RT   phosphate 5-kinase.";
RL   Nat. Genet. 14:157-162(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-415, AND ALTERNATIVE
RP   SPLICING.
RX   PubMed=9177790; DOI=10.1006/geno.1997.4726;
RA   Pook M.A., Carvajal J.J., Doudney K., Hillermann R., Chamberlain S.;
RT   "Exon-intron structure of a 2.7-kb transcript of the STM7 gene with
RT   phosphatidylinositol-4-phosphate 5-kinase activity.";
RL   Genomics 42:170-172(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Kidney;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 340-540 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Fetal brain;
RX   PubMed=8955136; DOI=10.1074/jbc.271.51.32937;
RA   Loijens J.C., Anderson R.A.;
RT   "Type I phosphatidylinositol-4-phosphate 5-kinases are distinct members of
RT   this novel lipid kinase family.";
RL   J. Biol. Chem. 271:32937-32943(1996).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Participates in the biosynthesis of phosphatidylinositol 4,5-
CC       bisphosphate. Mediates RAC1-dependent reorganization of actin
CC       filaments. Contributes to the activation of PLD2. Together with PIP5K1A
CC       is required after stimulation of G-protein coupled receptors for stable
CC       platelet adhesion (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate)
CC         + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC         bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456,
CC         ChEBI:CHEBI:456216; EC=2.7.1.68;
CC   -!- SUBUNIT: Interacts with RAC1, AJUBA, PLD1, PLD2 and ARF1.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}.
CC       Note=Associated with membranes. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O14986-1; Sequence=Displayed;
CC       Name=2; Synonyms=Isoform 1;
CC         IsoId=O14986-2; Sequence=VSP_016010, VSP_016011;
CC       Name=3;
CC         IsoId=O14986-3; Sequence=VSP_054771;
CC   -!- TISSUE SPECIFICITY: Detected in heart, pancreas, brain, kidney,
CC       skeletal muscle and lung. {ECO:0000269|PubMed:8955136}.
CC   -!- CAUTION: There is confusion in the literature with phosphatidylinositol
CC       4-phosphate 5-kinase type I nomenclature due to the fact that
CC       frequently mouse PIP5K1B is named Phosphatidylinositol 4-phosphate 5-
CC       kinase type I alpha. {ECO:0000305}.
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DR   EMBL; X92493; CAA63224.1; -; mRNA.
DR   EMBL; U52387; AAC51327.1; -; Genomic_DNA.
DR   EMBL; U52376; AAC51327.1; JOINED; Genomic_DNA.
DR   EMBL; U52377; AAC51327.1; JOINED; Genomic_DNA.
DR   EMBL; U52378; AAC51327.1; JOINED; Genomic_DNA.
DR   EMBL; U52379; AAC51327.1; JOINED; Genomic_DNA.
DR   EMBL; U52380; AAC51327.1; JOINED; Genomic_DNA.
DR   EMBL; U52381; AAC51327.1; JOINED; Genomic_DNA.
DR   EMBL; U52382; AAC51327.1; JOINED; Genomic_DNA.
DR   EMBL; U52383; AAC51327.1; JOINED; Genomic_DNA.
DR   EMBL; U52384; AAC51327.1; JOINED; Genomic_DNA.
DR   EMBL; U52385; AAC51327.1; JOINED; Genomic_DNA.
DR   EMBL; U52386; AAC51327.1; JOINED; Genomic_DNA.
DR   EMBL; AK292734; BAF85423.1; -; mRNA.
DR   EMBL; AK295587; BAG58479.1; -; mRNA.
DR   EMBL; AL162730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL354794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL356219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471089; EAW62465.1; -; Genomic_DNA.
DR   EMBL; BC030587; AAH30587.1; -; mRNA.
DR   EMBL; U78580; AAC50915.1; -; mRNA.
DR   CCDS; CCDS65063.1; -. [O14986-3]
DR   CCDS; CCDS6624.1; -. [O14986-1]
DR   RefSeq; NP_001265182.1; NM_001278253.1. [O14986-3]
DR   RefSeq; NP_003549.1; NM_003558.3. [O14986-1]
DR   RefSeq; XP_005252318.1; XM_005252261.3. [O14986-1]
DR   RefSeq; XP_005252319.1; XM_005252262.4. [O14986-1]
DR   RefSeq; XP_006717363.1; XM_006717300.2. [O14986-1]
DR   RefSeq; XP_006717364.1; XM_006717301.1. [O14986-3]
DR   RefSeq; XP_011517384.1; XM_011519082.2. [O14986-1]
DR   RefSeq; XP_011517385.1; XM_011519083.2. [O14986-1]
DR   RefSeq; XP_011517386.1; XM_011519084.2. [O14986-1]
DR   RefSeq; XP_016870677.1; XM_017015188.1. [O14986-1]
DR   RefSeq; XP_016870678.1; XM_017015189.1. [O14986-1]
DR   RefSeq; XP_016870679.1; XM_017015190.1. [O14986-1]
DR   RefSeq; XP_016870680.1; XM_017015191.1. [O14986-3]
DR   SMR; O14986; -.
DR   BioGrid; 113984; 6.
DR   CORUM; O14986; -.
DR   STRING; 9606.ENSP00000265382; -.
DR   iPTMnet; O14986; -.
DR   PhosphoSitePlus; O14986; -.
DR   SwissPalm; O14986; -.
DR   BioMuta; PIP5K1B; -.
DR   jPOST; O14986; -.
DR   MassIVE; O14986; -.
DR   MaxQB; O14986; -.
DR   PaxDb; O14986; -.
DR   PeptideAtlas; O14986; -.
DR   PRIDE; O14986; -.
DR   ProteomicsDB; 4304; -.
DR   ProteomicsDB; 48360; -. [O14986-1]
DR   ProteomicsDB; 48361; -. [O14986-2]
DR   Antibodypedia; 2767; 141 antibodies.
DR   DNASU; 8395; -.
DR   Ensembl; ENST00000265382; ENSP00000265382; ENSG00000107242. [O14986-1]
DR   Ensembl; ENST00000478500; ENSP00000435778; ENSG00000107242. [O14986-2]
DR   Ensembl; ENST00000541509; ENSP00000438082; ENSG00000107242. [O14986-3]
DR   GeneID; 8395; -.
DR   KEGG; hsa:8395; -.
DR   UCSC; uc004agu.5; human. [O14986-1]
DR   CTD; 8395; -.
DR   DisGeNET; 8395; -.
DR   GeneCards; PIP5K1B; -.
DR   HGNC; HGNC:8995; PIP5K1B.
DR   HPA; ENSG00000107242; Low tissue specificity.
DR   MIM; 602745; gene.
DR   neXtProt; NX_O14986; -.
DR   OpenTargets; ENSG00000107242; -.
DR   PharmGKB; PA33328; -.
DR   eggNOG; KOG0229; Eukaryota.
DR   eggNOG; COG5253; LUCA.
DR   GeneTree; ENSGT00940000156639; -.
DR   HOGENOM; CLU_004312_5_1_1; -.
DR   InParanoid; O14986; -.
DR   KO; K00889; -.
DR   OMA; RALKMHF; -.
DR   OrthoDB; 1562683at2759; -.
DR   PhylomeDB; O14986; -.
DR   TreeFam; TF319618; -.
DR   BioCyc; MetaCyc:HS02982-MONOMER; -.
DR   Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR   Reactome; R-HSA-201688; WNT mediated activation of DVL.
DR   Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   SABIO-RK; O14986; -.
DR   SIGNOR; O14986; -.
DR   ChiTaRS; PIP5K1B; human.
DR   GeneWiki; PIP5K1B; -.
DR   GenomeRNAi; 8395; -.
DR   Pharos; O14986; Tbio.
DR   PRO; PR:O14986; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; O14986; protein.
DR   Bgee; ENSG00000107242; Expressed in choroid plexus epithelium and 194 other tissues.
DR   ExpressionAtlas; O14986; baseline and differential.
DR   Genevisible; O14986; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001931; C:uropod; IDA:UniProtKB.
DR   GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; NAS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR   GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
DR   Gene3D; 3.30.800.10; -; 1.
DR   Gene3D; 3.30.810.10; -; 2.
DR   InterPro; IPR023610; PInositol-4-P-5-kinase.
DR   InterPro; IPR027483; PInositol-4-P-5-kinase_C.
DR   InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR   InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR   PANTHER; PTHR23086; PTHR23086; 1.
DR   Pfam; PF01504; PIP5K; 1.
DR   SMART; SM00330; PIPKc; 1.
DR   PROSITE; PS51455; PIPK; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Polymorphism; Reference proteome; Transferase.
FT   CHAIN           1..540
FT                   /note="Phosphatidylinositol 4-phosphate 5-kinase type-1
FT                   beta"
FT                   /id="PRO_0000185458"
FT   DOMAIN          25..395
FT                   /note="PIPK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT   MOD_RES         445
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70181"
FT   MOD_RES         447
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70181"
FT   MOD_RES         448
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70181"
FT   VAR_SEQ         24
FT                   /note="T -> TQVKNQILSRLPKIPCTFIQAWTNTEMITLLACYYFRSVST (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016010"
FT   VAR_SEQ         501..540
FT                   /note="SKGLPSSSTFTLEEGTIYLTAEPNTLEVQDDNASVLDVYL -> RFKMATSE
FT                   H (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016011"
FT   VAR_SEQ         503..540
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054771"
FT   VARIANT         415
FT                   /note="A -> T (in dbSNP:rs55897616)"
FT                   /evidence="ECO:0000269|PubMed:9177790"
FT                   /id="VAR_023712"
FT   CONFLICT        346
FT                   /note="M -> T (in Ref. 6; AAH30587)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   540 AA;  61036 MW;  7A683794A39A20B6 CRC64;
     MSSAAENGEA APGKQNEEKT YKKTASSAIK GAIQLGIGYT VGNLTSKPER DVLMQDFYVV
     ESVFLPSEGS NLTPAHHYPD FRFKTYAPLA FRYFRELFGI KPDDYLYSIC SEPLIELSNP
     GASGSLFFVT SDDEFIIKTV QHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCMQSGG
     INIRIVVMNN VLPRSMRMHF TYDLKGSTYK RRASRKEREK SNPTFKDLDF LQDMHEGLYF
     DTETYNALMK TLQRDCRVLE SFKIMDYSLL LGIHFLDHSL KEKEEETPQN VPDAKRTGMQ
     KVLYSTAMES IQGPGKSGDG IITENPDTMG GIPAKSHRGE KLLLFMGIID ILQSYRLMKK
     LEHSWKALVY DGDTVSVHRP SFYADRFLKF MNSRVFKKIQ ALKASPSKKR CNSIAALKAT
     SQEIVSSISQ EWKDEKRDLL TEGQSFSSLD EEALGSRHRP DLVPSTPSLF EAASLATTIS
     SSSLYVNEHY PHDRPTLYSN SKGLPSSSTF TLEEGTIYLT AEPNTLEVQD DNASVLDVYL
//