PHAG1_HUMAN
ID PHAG1_HUMAN Reviewed; 432 AA.
AC Q9NWQ8; A8K1A3; Q2M1Z9; Q5BKU4; Q9NYK0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Phosphoprotein associated with glycosphingolipid-enriched microdomains 1;
DE AltName: Full=Csk-binding protein;
DE AltName: Full=Transmembrane adapter protein PAG;
DE AltName: Full=Transmembrane phosphoprotein Cbp;
GN Name=PAG1; Synonyms=CBP, PAG;
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], PROTEIN SEQUENCE OF 264-274, IDENTIFICATION BY
RP MASS SPECTROMETRY, PHOSPHORYLATION AT TYR-317, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-37 AND CYS-40, MUTAGENESIS OF
RP TYR-105; TYR-163; TYR-181; TYR-227; TYR-299; TYR-317; TYR-341; TYR-359;
RP TYR-387 AND TYR-417, INTERACTION WITH FYN AND CSK, AND FUNCTION.
RX PubMed=10790433; DOI=10.1084/jem.191.9.1591;
RA Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P.,
RA Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K.,
RA Kuramitsu Y., Horejsi V., Schraven B.;
RT "Phosphoprotein associated with glycosphingolipid-enriched microdomains
RT (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds
RT the protein tyrosine kinase csk and is involved in regulation of T cell
RT activation.";
RL J. Exp. Med. 191:1591-1604(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Ileal mucosa;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lymph;
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 [5]
RP INTERACTION WITH SLC9A3R1.
RX PubMed=11684085; DOI=10.1016/s0014-5793(01)02955-6;
RA Brdickova N., Brdicka T., Andera L., Spicka J., Angelisova P.,
RA Milgram S.L., Horejsi V.;
RT "Interaction between two adapter proteins, PAG and EBP50: a possible link
RT between membrane rafts and actin cytoskeleton.";
RL FEBS Lett. 507:133-136(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=16160011; DOI=10.1182/blood-2005-06-2273;
RA Tedoldi S., Paterson J.C., Hansmann M.-L., Natkunam Y., Rudiger T.,
RA Angelisova P., Du M.Q., Roberton H., Roncador G., Sanchez L., Pozzobon M.,
RA Masir N., Barry R., Pileri S., Mason D.Y., Marafioti T., Horejsi V.;
RT "Transmembrane adaptor molecules: a new category of lymphoid-cell
RT markers.";
RL Blood 107:213-221(2006).
RN [8]
RP PHOSPHORYLATION AT TYR-317, INTERACTION WITH LYN AND STAT3, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18070987; DOI=10.1182/blood-2007-05-090985;
RA Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D.,
RA van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U., Borisch B.,
RA Hoessli D.C.;
RT "Oncogenic association of the Cbp/PAG adaptor protein with the Lyn tyrosine
RT kinase in human B-NHL rafts.";
RL Blood 111:2310-2320(2008).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-227; SER-229; TYR-317;
RP TYR-359; TYR-387 AND TYR-417, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Negatively regulates TCR (T-cell antigen receptor)-mediated
CC signaling in T-cells and FCER1 (high affinity immunoglobulin epsilon
CC receptor)-mediated signaling in mast cells. Promotes CSK activation and
CC recruitment to lipid rafts, which results in LCK inhibition. Inhibits
CC immunological synapse formation by preventing dynamic arrangement of
CC lipid raft proteins. May be involved in cell adhesion signaling.
CC {ECO:0000269|PubMed:10790433}.
CC -!- SUBUNIT: Interacts with FYN. When phosphorylated, interacts with CSK.
CC Interacts with SLC9A3R1/EBP50. In resting T-cells, part of a PAG1-
CC SLC9A3R1-MSN complex which is disrupted upon TCR activation. Interacts
CC with LYN on plasma membrane lipid rafts. Identified in a complex with
CC LYN and STAT3. {ECO:0000269|PubMed:10790433,
CC ECO:0000269|PubMed:11684085, ECO:0000269|PubMed:18070987}.
CC -!- INTERACTION:
CC Q9NWQ8; P41240: CSK; NbExp=5; IntAct=EBI-2828115, EBI-1380630;
CC Q9NWQ8; P06241: FYN; NbExp=5; IntAct=EBI-2828115, EBI-515315;
CC Q9NWQ8; P07948: LYN; NbExp=16; IntAct=EBI-2828115, EBI-79452;
CC Q9NWQ8; P63244: RACK1; NbExp=2; IntAct=EBI-2828115, EBI-296739;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10790433,
CC ECO:0000269|PubMed:18070987}; Single-pass type III membrane protein
CC {ECO:0000269|PubMed:10790433, ECO:0000269|PubMed:18070987}.
CC Note=Present in lipid rafts.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Present in germinal center
CC B-cells, plasma cells, T-cells, monocytes and platelets (at protein
CC level). {ECO:0000269|PubMed:10790433, ECO:0000269|PubMed:16160011}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:10790433}.
CC -!- PTM: Phosphorylated by FYN on Tyr-317 in resting T-cells; which
CC promotes interaction with CSK. Dephosphorylated by PTPRC/CD45 upon TCR
CC activation; which leads to CSK dissociation. May also be
CC dephosphorylated by PTPN11. Hyperphosphorylated in mast cells upon
CC FCER1 activation. Phosphorylated by LYN. {ECO:0000269|PubMed:10790433,
CC ECO:0000269|PubMed:18070987}.
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DR EMBL; AF240634; AAF67343.1; -; mRNA.
DR EMBL; AK000680; BAA91321.1; -; mRNA.
DR EMBL; AK289818; BAF82507.1; -; mRNA.
DR EMBL; CH471068; EAW87086.1; -; Genomic_DNA.
DR EMBL; BC090931; AAH90931.1; -; mRNA.
DR EMBL; BC112159; AAI12160.1; -; mRNA.
DR CCDS; CCDS6227.1; -.
DR RefSeq; NP_060910.3; NM_018440.3.
DR RefSeq; XP_016869129.1; XM_017013640.1.
DR RefSeq; XP_016869130.1; XM_017013641.1.
DR RefSeq; XP_016869131.1; XM_017013642.1.
DR RefSeq; XP_016869132.1; XM_017013643.1.
DR AlphaFoldDB; Q9NWQ8; -.
DR SMR; Q9NWQ8; -.
DR BioGRID; 120931; 58.
DR CORUM; Q9NWQ8; -.
DR IntAct; Q9NWQ8; 51.
DR MINT; Q9NWQ8; -.
DR STRING; 9606.ENSP00000220597; -.
DR iPTMnet; Q9NWQ8; -.
DR PhosphoSitePlus; Q9NWQ8; -.
DR SwissPalm; Q9NWQ8; -.
DR BioMuta; PAG1; -.
DR DMDM; 84029384; -.
DR EPD; Q9NWQ8; -.
DR jPOST; Q9NWQ8; -.
DR MassIVE; Q9NWQ8; -.
DR MaxQB; Q9NWQ8; -.
DR PaxDb; Q9NWQ8; -.
DR PeptideAtlas; Q9NWQ8; -.
DR PRIDE; Q9NWQ8; -.
DR ProteomicsDB; 82961; -.
DR TopDownProteomics; Q9NWQ8; -.
DR Antibodypedia; 1175; 369 antibodies from 35 providers.
DR DNASU; 55824; -.
DR Ensembl; ENST00000220597.4; ENSP00000220597.3; ENSG00000076641.4.
DR GeneID; 55824; -.
DR KEGG; hsa:55824; -.
DR MANE-Select; ENST00000220597.4; ENSP00000220597.3; NM_018440.4; NP_060910.3.
DR UCSC; uc003ybz.4; human.
DR CTD; 55824; -.
DR DisGeNET; 55824; -.
DR GeneCards; PAG1; -.
DR HGNC; HGNC:30043; PAG1.
DR HPA; ENSG00000076641; Low tissue specificity.
DR MIM; 605767; gene.
DR neXtProt; NX_Q9NWQ8; -.
DR OpenTargets; ENSG00000076641; -.
DR PharmGKB; PA142671201; -.
DR VEuPathDB; HostDB:ENSG00000076641; -.
DR eggNOG; ENOG502QUCZ; Eukaryota.
DR GeneTree; ENSGT00390000002061; -.
DR HOGENOM; CLU_051189_1_0_1; -.
DR InParanoid; Q9NWQ8; -.
DR OMA; QCRDITR; -.
DR OrthoDB; 1104680at2759; -.
DR PhylomeDB; Q9NWQ8; -.
DR TreeFam; TF336170; -.
DR PathwayCommons; Q9NWQ8; -.
DR Reactome; R-HSA-180292; GAB1 signalosome.
DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
DR SignaLink; Q9NWQ8; -.
DR SIGNOR; Q9NWQ8; -.
DR BioGRID-ORCS; 55824; 23 hits in 1071 CRISPR screens.
DR ChiTaRS; PAG1; human.
DR GeneWiki; PAG1; -.
DR GenomeRNAi; 55824; -.
DR Pharos; Q9NWQ8; Tbio.
DR PRO; PR:Q9NWQ8; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NWQ8; protein.
DR Bgee; ENSG00000076641; Expressed in secondary oocyte and 187 other tissues.
DR Genevisible; Q9NWQ8; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:HGNC-UCL.
DR GO; GO:0042169; F:SH2 domain binding; IDA:HGNC-UCL.
DR GO; GO:0035591; F:signaling adaptor activity; NAS:HGNC-UCL.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:HGNC-UCL.
DR GO; GO:0050868; P:negative regulation of T cell activation; IBA:GO_Central.
DR GO; GO:0050863; P:regulation of T cell activation; IDA:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR032748; PAG.
DR PANTHER; PTHR16322; PTHR16322; 1.
DR Pfam; PF15347; PAG; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell membrane; Direct protein sequencing; Immunity;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..432
FT /note="Phosphoprotein associated with glycosphingolipid-
FT enriched microdomains 1"
FT /id="PRO_0000083338"
FT TOPO_DOM 1..16
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 110..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..320
FT /note="Interaction with CSK"
FT /evidence="ECO:0000269|PubMed:10790433"
FT REGION 430..432
FT /note="Interaction with SLC9A3R1"
FT /evidence="ECO:0000269|PubMed:11684085"
FT COMPBIAS 267..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM80"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM80"
FT MOD_RES 105
FT /note="Phosphotyrosine; by LYN"
FT /evidence="ECO:0000250|UniProtKB:Q9JM80"
FT MOD_RES 163
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3U1F9"
FT MOD_RES 181
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3U1F9"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 317
FT /note="Phosphotyrosine; by FYN and LYN"
FT /evidence="ECO:0000269|PubMed:10790433,
FT ECO:0000269|PubMed:18070987, ECO:0007744|PubMed:19690332"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U1F9"
FT MOD_RES 359
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U1F9"
FT MOD_RES 387
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 417
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT LIPID 37
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:10790433"
FT LIPID 40
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:10790433"
FT MUTAGEN 105
FT /note="Y->F: No effect on interaction with FYN or CSK."
FT /evidence="ECO:0000269|PubMed:10790433"
FT MUTAGEN 163
FT /note="Y->F: No effect on interaction with FYN or CSK."
FT /evidence="ECO:0000269|PubMed:10790433"
FT MUTAGEN 181
FT /note="Y->F: No effect on interaction with FYN or CSK."
FT /evidence="ECO:0000269|PubMed:10790433"
FT MUTAGEN 227
FT /note="Y->F: No effect on interaction with FYN or CSK."
FT /evidence="ECO:0000269|PubMed:10790433"
FT MUTAGEN 299
FT /note="Y->F: No effect on interaction with FYN or CSK."
FT /evidence="ECO:0000269|PubMed:10790433"
FT MUTAGEN 317
FT /note="Y->F: No effect on interaction with FYN. Abolishes
FT interaction with CSK."
FT /evidence="ECO:0000269|PubMed:10790433"
FT MUTAGEN 341
FT /note="Y->F: No effect on interaction with FYN or CSK."
FT /evidence="ECO:0000269|PubMed:10790433"
FT MUTAGEN 359
FT /note="Y->F: No effect on interaction with FYN or CSK."
FT /evidence="ECO:0000269|PubMed:10790433"
FT MUTAGEN 387
FT /note="Y->F: No effect on interaction with FYN or CSK."
FT /evidence="ECO:0000269|PubMed:10790433"
FT MUTAGEN 417
FT /note="Y->F: No effect on interaction with FYN or CSK."
FT /evidence="ECO:0000269|PubMed:10790433"
FT CONFLICT 4
FT /note="A -> V (in Ref. 4; AAH90931)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="L -> P (in Ref. 2; BAA91321)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 46981 MW; E86272A0B7E3328C CRC64;
MGPAGSLLGS GQMQITLWGS LAAVAIFFVI TFLIFLCSSC DREKKPRQHS GDHENLMNVP
SDKEMFSRSV TSLATDAPAS SEQNGALTNG DILSEDSTLT CMQHYEEVQT SASDLLDSQD
STGKPKCHQS RELPRIPPES AVDTMLTARS VDGDQGLGME GPYEVLKDSS SQENMVEDCL
YETVKEIKEV AAAAHLEKGH SGKAKSTSAS KELPGPQTEG KAEFAEYASV DRNKKCRQSV
NVESILGNSC DPEEEAPPPV PVKLLDENEN LQEKEGGEAE ESATDTTSET NKRFSSLSYK
SREEDPTLTE EEISAMYSSV NKPGQLVNKS GQSLTVPEST YTSIQGDPQR SPSSCNDLYA
TVKDFEKTPN STLPPAGRPS EEPEPDYEAI QTLNREEEKA TLGTNGHHGL VPKENDYESI
SDLQQGRDIT RL
