PH-interacting protein (PHIP) (IRS-1 PH domain-binding protein) (Neuronal differentiation-related protein) (NDRP) (WD repeat-containing protein 11)

 PHIP_MOUSE              Reviewed;        1821 AA.
 Q8VDD9; Q3TS96; Q80VI6; Q9EPY1; Q9ESL6;
 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
 21-AUG-2007, sequence version 2.
 22-APR-2020, entry version 133.
 RecName: Full=PH-interacting protein;
          Short=PHIP;
 AltName: Full=IRS-1 PH domain-binding protein;
 AltName: Full=Neuronal differentiation-related protein;
          Short=NDRP;
 AltName: Full=WD repeat-containing protein 11;
 Name=Phip; Synonyms=Ndrp, Phip1, Wdr11;
 Mus musculus (Mouse).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
 Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
 Murinae; Mus; Mus.
 NCBI_TaxID=10090;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1-1779.
 Antonarakis S.;
 Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1-999, TISSUE SPECIFICITY, DEVELOPMENTAL
 STAGE, AND INDUCTION.
 STRAIN=Swiss Webster / NIH;
 PubMed=11098134; DOI=10.1093/oxfordjournals.jbchem.a022843;
 Kato H., Chen S., Kiyama H., Ikeda K., Kimura N., Nakashima K., Taga T.;
 "Identification of a novel WD repeat-containing gene predominantly
 expressed in developing and regenerating neurons.";
 J. Biochem. 128:923-932(2000).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-893.
 STRAIN=Czech II; TISSUE=Mammary tumor;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA project:
 the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 745-1458.
 STRAIN=C57BL/6J; TISSUE=Egg;
 PubMed=16141072; DOI=10.1126/science.1112014;
 Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
 Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
 Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
 Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
 Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
 Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
 Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
 Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
 Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
 Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
 Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
 Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
 Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
 Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
 Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
 Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
 Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
 Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
 Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
 Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
 Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
 Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
 Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
 Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
 Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
 van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
 Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
 Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
 Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
 Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
 Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
 Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
 Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
 Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
 "The transcriptional landscape of the mammalian genome.";
 Science 309:1559-1563(2005).
 [5]
 NUCLEOTIDE SEQUENCE [MRNA] OF 924-1821, FUNCTION, INTERACTION WITH IRS1 AND
 IRS2, AND TISSUE SPECIFICITY.
 PubMed=11018022; DOI=10.1074/jbc.c000611200;
 Farhang-Fallah J., Yin X., Trentin G., Cheng A.M., Rozakis-Adcock M.;
 "Cloning and characterization of PHIP, a novel insulin receptor substrate-1
 pleckstrin homology domain interacting protein.";
 J. Biol. Chem. 275:40492-40497(2000).
 [6]
 PROTEIN SEQUENCE OF 1589-1596, AND IDENTIFICATION BY MASS SPECTROMETRY.
 STRAIN=OF1; TISSUE=Hippocampus;
 Lubec G., Sunyer B., Chen W.-Q.;
 Submitted (JAN-2009) to UniProtKB.
 [7]
 FUNCTION.
 PubMed=12242307; DOI=10.1128/mcb.22.20.7325-7336.2002;
 Farhang-Fallah J., Randhawa V.K., Nimnual A., Klip A., Bar-Sagi D.,
 Rozakis-Adcock M.;
 "The pleckstrin homology (PH) domain-interacting protein couples the
 insulin receptor substrate 1 PH domain to insulin signaling pathways
 leading to mitogenesis and GLUT4 translocation.";
 Mol. Cell. Biol. 22:7325-7336(2002).
 [8]
 FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
 PubMed=17636024; DOI=10.1128/mcb.02409-06;
 Podcheko A., Northcott P., Bikopoulos G., Lee A., Bommareddi S.R.,
 Kushner J.A., Farhang-Fallah J., Rozakis-Adcock M.;
 "Identification of a WD40 repeat-containing isoform of PHIP as a novel
 regulator of beta-cell growth and survival.";
 Mol. Cell. Biol. 27:6484-6496(2007).
 [9]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281 AND SER-1283, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Liver;
 PubMed=17242355; DOI=10.1073/pnas.0609836104;
 Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
 "Large-scale phosphorylation analysis of mouse liver.";
 Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
 [10]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281 AND SER-1283, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
 Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
 Thibault P.;
 "The phagosomal proteome in interferon-gamma-activated macrophages.";
 Immunity 30:143-154(2009).
 [11]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281; SER-1283; SER-1315 AND
 SER-1783, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
 Testis;
 PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
 Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
 Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
 "A tissue-specific atlas of mouse protein phosphorylation and expression.";
 Cell 143:1174-1189(2010).
 [12]
 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1533, AND IDENTIFICATION BY MASS
 SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Embryonic fibroblast;
 PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
 Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
 Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
 "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
 pathways.";
 Mol. Cell 50:919-930(2013).
 -!- FUNCTION: Probable regulator of the insulin and insulin-like growth
     factor signaling pathways. Stimulates cell proliferation through
     regulation of cyclin transcription and has an anti-apoptotic activity
     through AKT1 phosphorylation and activation. Plays a role in the
     regulation of cell morphology and cytoskeletal organization.
     {ECO:0000269|PubMed:11018022, ECO:0000269|PubMed:12242307,
     ECO:0000269|PubMed:17636024}.
 -!- SUBUNIT: Interacts (via bromo domain) with acetylated lysine residues
     on histone H1.4, histone H3 and H4 (in vitro) (By similarity).
     Interacts with IRS1 and IRS2. {ECO:0000250,
     ECO:0000269|PubMed:11018022}.
 -!- INTERACTION:
     Q8VDD9; P35570: Irs1; Xeno; NbExp=2; IntAct=EBI-1369766, EBI-520230;
 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17636024}.
 -!- TISSUE SPECIFICITY: Widely expressed with most abundant expression
     detected in pancreatic islets, brain and skeletal muscle. Predominantly
     expressed in developing and regenerating neurons. Expressed in adult
     brain (granular layer of the olfactorium bulb, hippocampus, dentate
     gyrus and cerebellum internal granular layer). Expressed in the CA3
     region of adult hippocampus, adult and fetal retina, perinatal dorsal
     root ganglion and embryonal olfactory epithelia (at protein level).
     {ECO:0000269|PubMed:11018022, ECO:0000269|PubMed:11098134,
     ECO:0000269|PubMed:17636024}.
 -!- DEVELOPMENTAL STAGE: Expressed at highest levels at 17.5 dpc in the
     neural layer of the retina and olfactory epithelia.
     {ECO:0000269|PubMed:11098134}.
 -!- INDUCTION: In motor neurons after injury.
     {ECO:0000269|PubMed:11098134}.
 -!- SEQUENCE CAUTION:
     Sequence=AAG45146.1; Type=Miscellaneous discrepancy; Note=Intron retention. This sequence is incomplete at the 5' end and extensively differs from that shown.; Evidence={ECO:0000305};
     Sequence=AAH49950.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
     Sequence=BAB16299.1; Type=Miscellaneous discrepancy; Note=Intron retention. This sequence is incomplete at the 3' end and extensively differs from that shown.; Evidence={ECO:0000305};
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 EMBL; AJ303103; CAC83119.1; -; mRNA.
 EMBL; AB049460; BAB16299.1; ALT_SEQ; mRNA.
 EMBL; BC049950; AAH49950.1; ALT_TERM; mRNA.
 EMBL; AK162189; BAE36779.1; -; mRNA.
 EMBL; AF310251; AAG45146.1; ALT_SEQ; mRNA.
 CCDS; CCDS40706.1; -.
 IntAct; Q8VDD9; 6.
 MINT; Q8VDD9; -.
 STRING; 10090.ENSMUSP00000034787; -.
 iPTMnet; Q8VDD9; -.
 PhosphoSitePlus; Q8VDD9; -.
 EPD; Q8VDD9; -.
 jPOST; Q8VDD9; -.
 MaxQB; Q8VDD9; -.
 PaxDb; Q8VDD9; -.
 PRIDE; Q8VDD9; -.
 UCSC; uc009qvw.1; mouse.
 MGI; MGI:1932404; Phip.
 eggNOG; KOG0644; Eukaryota.
 eggNOG; ENOG410YCD8; LUCA.
 InParanoid; Q8VDD9; -.
 PhylomeDB; Q8VDD9; -.
 ChiTaRS; Phip; mouse.
 PRO; PR:Q8VDD9; -.
 Proteomes; UP000000589; Unplaced.
 RNAct; Q8VDD9; protein.
 GO; GO:0005634; C:nucleus; IDA:UniProtKB.
 GO; GO:0005158; F:insulin receptor binding; IEA:InterPro.
 GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
 GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
 GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
 GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
 GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
 GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
 GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IDA:UniProtKB.
 GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:UniProtKB.
 GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:MGI.
 GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:MGI.
 GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
 GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
 GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
 GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
 GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
 GO; GO:0040008; P:regulation of growth; IMP:MGI.
 GO; GO:0001932; P:regulation of protein phosphorylation; IDA:UniProtKB.
 GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
 Gene3D; 1.20.920.10; -; 2.
 Gene3D; 2.130.10.10; -; 2.
 InterPro; IPR001487; Bromodomain.
 InterPro; IPR036427; Bromodomain-like_sf.
 InterPro; IPR018359; Bromodomain_CS.
 InterPro; IPR028738; PHIP.
 InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
 InterPro; IPR001680; WD40_repeat.
 InterPro; IPR019775; WD40_repeat_CS.
 InterPro; IPR017986; WD40_repeat_dom.
 InterPro; IPR036322; WD40_repeat_dom_sf.
 PANTHER; PTHR16266:SF4; PTHR16266:SF4; 1.
 Pfam; PF00439; Bromodomain; 2.
 Pfam; PF00400; WD40; 5.
 PRINTS; PR00503; BROMODOMAIN.
 SMART; SM00297; BROMO; 2.
 SMART; SM00320; WD40; 8.
 SUPFAM; SSF47370; SSF47370; 2.
 SUPFAM; SSF50978; SSF50978; 1.
 PROSITE; PS00633; BROMODOMAIN_1; 1.
 PROSITE; PS50014; BROMODOMAIN_2; 2.
 PROSITE; PS00678; WD_REPEATS_1; 2.
 PROSITE; PS50082; WD_REPEATS_2; 5.
 PROSITE; PS50294; WD_REPEATS_REGION; 1.
 1: Evidence at protein level;
 Acetylation; Bromodomain; Direct protein sequencing; Isopeptide bond;
 Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation;
 WD repeat.
 CHAIN           1..1821
                 /note="PH-interacting protein"
                 /id="PRO_0000297758"
 REPEAT          181..222
                 /note="WD 1"
 REPEAT          224..262
                 /note="WD 2"
 REPEAT          265..310
                 /note="WD 3"
 REPEAT          319..360
                 /note="WD 4"
 REPEAT          363..402
                 /note="WD 5"
 REPEAT          422..461
                 /note="WD 6"
 REPEAT          464..504
                 /note="WD 7"
 REPEAT          512..551
                 /note="WD 8"
 DOMAIN          1176..1246
                 /note="Bromo 1"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
 DOMAIN          1333..1403
                 /note="Bromo 2"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
 REGION          924..1129
                 /note="Mediates interaction with IRS1"
                 /evidence="ECO:0000269|PubMed:11018022"
 COMPBIAS        867..923
                 /note="Lys-rich"
 COMPBIAS        1752..1758
                 /note="Poly-Glu"
 MOD_RES         136
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         641
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         659
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         674
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         677
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         683
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         692
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         879
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         880
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         881
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         911
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         1281
                 /note="Phosphoserine"
                 /evidence="ECO:0000244|PubMed:17242355,
                 ECO:0000244|PubMed:19144319, ECO:0000244|PubMed:21183079"
 MOD_RES         1283
                 /note="Phosphoserine"
                 /evidence="ECO:0000244|PubMed:17242355,
                 ECO:0000244|PubMed:19144319, ECO:0000244|PubMed:21183079"
 MOD_RES         1296
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         1315
                 /note="Phosphoserine"
                 /evidence="ECO:0000244|PubMed:21183079"
 MOD_RES         1359
                 /note="Phosphothreonine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         1405
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         1479
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         1497
                 /note="N6-acetyllysine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         1525
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         1533
                 /note="N6-acetyllysine"
                 /evidence="ECO:0000244|PubMed:23806337"
 MOD_RES         1560
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         1651
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         1762
                 /note="Phosphoserine"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 MOD_RES         1783
                 /note="Phosphoserine"
                 /evidence="ECO:0000244|PubMed:21183079"
 CROSSLNK        421
                 /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                 G-Cter in SUMO2)"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 CROSSLNK        1470
                 /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                 G-Cter in SUMO1); alternate"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 CROSSLNK        1470
                 /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                 G-Cter in SUMO2); alternate"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 CROSSLNK        1644
                 /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                 G-Cter in SUMO2)"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 CROSSLNK        1670
                 /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
                 G-Cter in SUMO2)"
                 /evidence="ECO:0000250|UniProtKB:Q8WWQ0"
 CONFLICT        672
                 /note="R -> G (in Ref. 3; AAH49950)"
                 /evidence="ECO:0000305"
 CONFLICT        1065
                 /note="P -> R (in Ref. 4; BAE36779 and 5; AAG45146)"
                 /evidence="ECO:0000305"
 CONFLICT        1155
                 /note="E -> D (in Ref. 5; AAG45146)"
                 /evidence="ECO:0000305"
 CONFLICT        1392
                 /note="F -> S (in Ref. 4; BAE36779 and 5; AAG45146)"
                 /evidence="ECO:0000305"
 CONFLICT        1776
                 /note="A -> T (in Ref. 5; AAG45146)"
                 /evidence="ECO:0000305"
 SEQUENCE   1821 AA;  206726 MW;  92E8DF0833F60FFA CRC64;
 MSRERKGLSE LRSELYFLIA RFLEDGPCQQ AAQVLIREVA EKELLPRRTD WTGKEHPRTY
 QNLVKYYRHL APDHLLQICH RLGPLLEQEI PQSVPGVQTL LGAGRQSLLR TNKSCKHVVW
 KGSALAALHC GRPPESPVNY GSPPSIADTL FSRKLNGKYR LERLVPTAVY QHMKMHKRIL
 GHLSSVYCVT FDRTGRRIFT GSDDCLVKIW ATDDGRLLAT LRGHAAEISD MAVNYENTMI
 AAGSCDKMIR VWCLRTCAPL AVLQGHSASI TSLQFSPLCS GSKRYLSSTG ADGTICFWLW
 DAGTLKINPR PTKFTERPRP GVQMICSSFS AGGMFLATGS TDHIIRVYFF GSGQPEKISE
 LEFHTDKVDS IQFSNTSNRF VSGSRDGTAR IWQFKRREWK SILLDMATRP AGQNLQGIED
 KITKMKVTMV AWDRHDNTVI TAVNNMTLKV WNSYTGQLIH VLMGHEDEVF VLEPHPFDPR
 VLFSAGHDGN VIVWDLARGV KVRSYFNMIE GQGHGAVFDC KCSPDGQHFA CTDSHGHLLI
 FGFGSSSKYD KIADQMFFHS DYRPLIRDAN NFVLDEQTQQ APHLMPPPFL VDVDGNPHPS
 RYQRLVPGRE NCREEQLIPQ MGVTSSGLNQ VLSQQANQDI SPLDSMIQRL QQEQDLRRSG
 EAGVSNASRV NRGSVSSTSE VHSPPNIGLR RSGQIEGVRQ MHSNAPRSEI ATERDLVAWS
 RRVVVPELSA GVASRQEEWR TAKGEEEIKS YRSEEKRKHL TVAKENKILT VSKNHAHEHF
 LDLGDSKKQQ ANQHNYRTRS ALEETPRPLE ELENGTSSSD EGEVLAVSGG TSEEEERAWH
 SDGSSSDYSS DYSDWTADAG INLQPPKKVP KHKTKKPESS SDEEEESENQ KQKHIKKERK
 KANEEKDGPT SPKKKKPKER KQKRLAVGEL TENGLTLEEW LPSAWITDTL PRRCPFVPQM
 GDEVYYFRQG HEAYVEMARK NKIYSINPKK QPWHKMELRE QELMKIVGIK YEVGLPTLCC
 LKLAFLDPDT GKLTGGSFTM KYHDMPDVID FLVLRQQFDD AKYRPWNIGD RFRSVIDDAW
 WFGTIESQEP LQPEYPDSLF QCYNVCWDNG DTEKMSPWDM ELIPNNAVFP EELGTSVPLT
 DVECRSLIYK PLDGEWGANP RDEECERIVG GINQLMTLDI ASAFVAPVDL QAYPMYCTVV
 AYPTDLSTIK QRLENRFYRR FSSLMWEVRY IEHNTRTFNE PGSPIVKSAK FVTDLLLHFI
 KDQTCYNIIP LYNSMKKKVL SDSEEEEKDA DVPGTSTRKR KDHQPRRRLR NRAQSYDIQA
 WKKQCQELLN LIFQCEDSEP FRQPVDLLEY PDYRDIIDTP MDFATVRETL EAGNYESPME
 LCKDVRLIFS NFKAYTPSKR SRIYSMSLRL SAFFEEHISS VLSDYKSALR FHKRNTISKK
 RKKRNRSSSL SSSAASSPER KKRILKPQLK SEVSTSPFSI PTRSVLPRHN AAQMNGKPES
 SSVVRTRSNR VAVDPVVTEQ PSTSSATKAF VSKTNTSAMP GKAMLENSVR HSKALSTLSS
 PDPLTFSHAT KNNSAKENME KEKPVKRKMK SSVFSKASPL PKSAAVIEQG ECKNNVLIPG
 TIQVNGHGGQ PSKLVKRGPG RKPKVEVNTS SGEVTHKKRG RKPKNLQCAK QENSEQNNMH
 PIRADVLPSS TCNFLSETNA VKEDLLQKKS RGGRKPKRKM KTHNLDSELI VPTNVKVLRR
 SNRKKTDDPI DEEEEFEELK GSEPHMRTRN QGRRTAFYNE DDSEEEQRQL LFEDTSLTFG
 TSSRGRVRKL TEKAKANLIG W

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