PALS1_RAT
ID PALS1_RAT Reviewed; 675 AA.
AC B4F7E7;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein PALS1 {ECO:0000305};
DE AltName: Full=MAGUK p55 subfamily member 5 {ECO:0000305};
DE AltName: Full=Protein associated with Lin-7 1;
GN Name=Pals1 {ECO:0000303|PubMed:20237282};
GN Synonyms=Mpp5 {ECO:0000312|RGD:1308071};
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 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000312|EMBL:EDM03700.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|EMBL:AAI68247.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate {ECO:0000312|EMBL:AAI68247.1};
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 [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=20237282; DOI=10.1523/jneurosci.5185-09.2010;
RA Ozcelik M., Cotter L., Jacob C., Pereira J.A., Relvas J.B., Suter U.,
RA Tricaud N.;
RT "Pals1 is a major regulator of the epithelial-like polarization and the
RT extension of the myelin sheath in peripheral nerves.";
RL J. Neurosci. 30:4120-4131(2010).
RN [5] {ECO:0007744|PubMed:22673903}
RP 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: Plays a role in tight junction biogenesis and in the
CC establishment of cell polarity in epithelial cells (By similarity).
CC Also involved in adherens junction biogenesis by ensuring correct
CC localization of the exocyst complex protein EXOC4/SEC8 which allows
CC trafficking of adherens junction structural component CDH1 to the cell
CC surface (By similarity). Plays a role through its interaction with CDH5
CC in vascular lumen formation and endothelial membrane polarity (By
CC similarity). Required during embryonic and postnatal retinal
CC development (By similarity). Required for the maintenance of cerebellar
CC progenitor cells in an undifferentiated proliferative state, preventing
CC premature differentiation, and is required for cerebellar histogenesis,
CC fissure formation, cerebellar layer organization and cortical
CC development (By similarity). Plays a role in neuronal progenitor cell
CC survival, potentially via promotion of mTOR signaling (By similarity).
CC Plays a role in the radial and longitudinal extension of the myelin
CC sheath in Schwann cells (By similarity). May modulate SC6A1/GAT1-
CC mediated GABA uptake by stabilizing the transporter (By similarity).
CC May play a role in the T-cell receptor-mediated activation of NF-kappa-
CC B (By similarity). Required for localization of EZR to the apical
CC membrane of parietal cells and may play a role in the dynamic
CC remodeling of the apical cytoskeleton (By similarity). Required for the
CC normal polarized localization of the vesicular marker STX4 (By
CC similarity). Required for the correct trafficking of the myelin
CC proteins PMP22 and MAG (PubMed:20237282). Involved in promoting
CC phosphorylation and cytoplasmic retention of transcriptional
CC coactivators YAP1 and WWTR1/TAZ which leads to suppression of TGFB1-
CC dependent transcription of target genes such as CCN2/CTGF,
CC SERPINE1/PAI1, SNAI1/SNAIL1 and SMAD7 (By similarity).
CC {ECO:0000250|UniProtKB:Q8N3R9, ECO:0000250|UniProtKB:Q9JLB2,
CC ECO:0000269|PubMed:20237282}.
CC -!- SUBUNIT: Heterodimer with MPP1 (By similarity). Forms a heterotrimeric
CC complex composed of PALS1, LIN7B and PATJ; the N-terminal L27 domain of
CC PALS1 interacts with the L27 domain of PATJ and the C-terminal L27
CC domain of PALS1 interacts with the L27 domain of LIN7B (By similarity).
CC Component of a complex composed of PALS1, CRB1 and MPP4 (By
CC similarity). Component of a complex whose core is composed of ARHGAP17,
CC AMOT, PALS1, PATJ and PARD3/PAR3 (By similarity). Component of a
CC complex composed of PALS1, CRB1 and EPB41L5. Within the complex,
CC interacts (via HOOK domain) with EPB41L5 (via FERM domain), and
CC interacts with CRB1 (via intracellular domain) (By similarity).
CC Component of a complex composed of PALS1, MPP3 and CRB1; PALS1 acts as
CC a bridging protein between MPP3 (via guanylate kinase-like domain) and
CC CRB1 (By similarity). Component of a complex composed of CRB3, PALS1
CC and PATJ (By similarity). Interacts (via PDZ domain) with PATJ (via N-
CC terminus). Interacts with EZR (By similarity). Interacts (via PDZ
CC domain) with CRB1 (via C-terminal ERLI motif) (By similarity). While
CC the PDZ domain is sufficient for interaction with CRB1, the adjacent
CC SH3 and guanylate kinase-like domains are likely to contribute to a
CC high affinity interaction (By similarity). Interacts with WWTR1/TAZ
CC (via WW domain) (By similarity). Interacts with MPP7 (By similarity).
CC Interacts (via PDZ domain) with CRB3 (via C-terminus) (By similarity).
CC Interacts with LIN7C. Interacts with MPDZ. Interacts with PARD6B.
CC Interacts with SC6A1. Interacts with CDH5; the interaction promotes
CC PALS1 localization to cell junctions and is required for CDH5-mediated
CC vascular lumen formation and endothelial cell (By similarity).
CC Interacts with NPHP1 (via coiled coil and SH3 domains) (By similarity).
CC Interacts with NPHP4 (By similarity). Interacts with CRB2 (By
CC similarity). {ECO:0000250|UniProtKB:E2QY99,
CC ECO:0000250|UniProtKB:Q8N3R9, ECO:0000250|UniProtKB:Q9JLB2}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q8N3R9}.
CC Cell membrane {ECO:0000250|UniProtKB:Q9JLB2}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q9JLB2}. Endomembrane system
CC {ECO:0000250|UniProtKB:Q9JLB2}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9JLB2}. Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q8N3R9}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q8N3R9}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9JLB2}. Perikaryon
CC {ECO:0000250|UniProtKB:Q9JLB2}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q8N3R9}. Note=Localized to the tight junctions
CC of epithelial cells (By similarity). Localized to the Golgi apparatus
CC in T lymphocytes (By similarity). Localized to a subset of
CC intracellular vesicles (By similarity). Localized to the Purkinje cell
CC body and axon (By similarity). Localized to intercellular junctions in
CC vascular endothelial cells (By similarity). Localized to Schmidt-
CC Lanterman incisures, the adaxonal domain, and the inner part of
CC paranodal loops in myelinating Schwann cells of the sciatic nerve (By
CC similarity). Localized to apical membrane domains of the outer limiting
CC membrane (OLM) junctions in the retina (By similarity). Colocalizes
CC with CRB1 at the OLM, apical to the adherens junction (By similarity).
CC Colocalizes with MPP1 in the retina at the OLM (By similarity).
CC Colocalizes with MPP3 to the subapical region of adherens junctions in
CC the retina OLM (By similarity). {ECO:0000250|UniProtKB:Q8N3R9,
CC ECO:0000250|UniProtKB:Q9JLB2}.
CC -!- DOMAIN: The L27 domain 1 functions in targeting to the tight junctions
CC by binding to and stabilizing PATJ. {ECO:0000250|UniProtKB:Q9JLB2}.
CC -!- DOMAIN: The PDZ domain binds to the C-terminus of SC6A1.
CC {ECO:0000250|UniProtKB:Q9JLB2}.
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; AABR07073239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC120917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473947; EDM03700.1; -; Genomic_DNA.
DR EMBL; BC168247; AAI68247.1; -; mRNA.
DR RefSeq; NP_001101504.1; NM_001108034.1.
DR RefSeq; XP_006240320.1; XM_006240258.2.
DR RefSeq; XP_008762995.1; XM_008764773.2.
DR AlphaFoldDB; B4F7E7; -.
DR SMR; B4F7E7; -.
DR IntAct; B4F7E7; 3.
DR STRING; 10116.ENSRNOP00000012005; -.
DR iPTMnet; B4F7E7; -.
DR PhosphoSitePlus; B4F7E7; -.
DR jPOST; B4F7E7; -.
DR PaxDb; B4F7E7; -.
DR PeptideAtlas; B4F7E7; -.
DR Ensembl; ENSRNOT00000092157; ENSRNOP00000070368; ENSRNOG00000008788.
DR GeneID; 314259; -.
DR KEGG; rno:314259; -.
DR UCSC; RGD:1308071; rat.
DR CTD; 64398; -.
DR RGD; 1308071; Mpp5.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000156087; -.
DR HOGENOM; CLU_001715_5_4_1; -.
DR InParanoid; B4F7E7; -.
DR OMA; LKHIQHV; -.
DR OrthoDB; 531106at2759; -.
DR PhylomeDB; B4F7E7; -.
DR TreeFam; TF314263; -.
DR PRO; PR:B4F7E7; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Proteomes; UP000234681; Chromosome 6.
DR Bgee; ENSRNOG00000008788; Expressed in lung and 19 other tissues.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043219; C:lateral loop; ISO:RGD.
DR GO; GO:0035749; C:myelin sheath adaxonal region; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0021954; P:central nervous system neuron development; ISS:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0048699; P:generation of neurons; IBA:GO_Central.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; ISO:RGD.
DR GO; GO:0032288; P:myelin assembly; IMP:BHF-UCL.
DR GO; GO:0032287; P:peripheral nervous system myelin maintenance; ISO:RGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007009; P:plasma membrane organization; ISO:RGD.
DR GO; GO:0035750; P:protein localization to myelin sheath abaxonal region; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR CDD; cd12036; SH3_MPP5; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR015145; L27_N.
DR InterPro; IPR035601; MPP5_SH3.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 1.
DR Pfam; PF09060; L27_N; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; SSF101288; 2.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell junction; Cell membrane; Cell projection;
KW Golgi apparatus; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Tight junction; Transferase.
FT CHAIN 1..675
FT /note="Protein PALS1"
FT /id="PRO_0000447580"
FT DOMAIN 120..177
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 179..235
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 256..336
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 345..417
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 479..660
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 1..345
FT /note="Required for the correct localization of PALS1 and
FT PATJ at cell-cell contacts and the normal formation of
FT tight junctions and adherens junctions"
FT /evidence="ECO:0000250|UniProtKB:Q9JLB2"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 21..140
FT /note="Interaction with PARD6B"
FT /evidence="ECO:0000250|UniProtKB:Q9JLB2"
FT REGION 52..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..243
FT /note="Interaction with LIN7C"
FT /evidence="ECO:0000250|UniProtKB:Q9JLB2"
FT COMPBIAS 57..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 486..493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3R9"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLB2"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3R9"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3R9"
SQ SEQUENCE 675 AA; 77152 MW; 7F212741A8454B14 CRC64;
MTTSYMNGHV TEESDSGIKN LGLASPEEHP KHREMAVDCP GDLGTRLMPV RRSAQLERIR
QQQEDMRRRR EEEGKKQELD LNSSMRLKKL AQIPPKTGID NPIFDTEEGI VLESPHYAVK
ILEVEDLFSS LKHIQHTLVD SQSQEDISLL LQLVQNRDFQ NAFKIHNAVT VHMNKASPPF
PLIANVQDLV QEVQTVLKPV HQKEGQELTA LLNAPHIQAL LLAHDKVAEQ EMQLEPITDE
RVYESIGHYG GETVKIVRIE KARDIPLGAT VRNEMDSVII SRIVKGGAAE KSGLLHEGDE
VLEINGIEIR GKDVNEVFDL LSDMHGTLTF VLIPSQQIKP PPAKETVIHV KAHFDYDPSD
DPYVPCRELG LSFQKGDILH VISQEDPNWW QAYREGDEDN QPLAGLVPGK SFQQQREAMK
QTIEEDKEPE KSGKLWCAKK NKKKRKKVLY NANKNDDYDN EEILTYEEMS LYHQPANRKR
PIILIGPQNC GQNELRQRLM NKEKDRFASA VPHTTRNRRD HEVAGRDYHF VSRQAFEADI
AAGKFIEHGE FEKNLYGTSI DSVRQVINSG KICLLSLRAQ SLKTLRNSDL KPYIIFIAPP
SQERLRALLA KEGKNPKPEE LREIIEKTRE MEQNNGHYFD TAIVNSDLDK AYQELLRLIN
KLDTEPQWVP STWLR
