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PHIP_MOUSE Reviewed; 1821 AA.
Q8VDD9; Q3TS96; Q80VI6; Q9EPY1; Q9ESL6;
21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
21-AUG-2007, sequence version 2.
12-AUG-2020, entry version 134.
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.
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