REPS2_HUMAN
ID REPS2_HUMAN Reviewed; 660 AA.
AC Q8NFH8; A6PWZ6; O43428; Q5JNZ8; Q8NFI5;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=RalBP1-associated Eps domain-containing protein 2;
DE AltName: Full=Partner of RalBP1;
DE AltName: Full=RalBP1-interacting protein 2;
GN Name=REPS2; Synonyms=POB1;
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), FUNCTION, INTERACTION WITH GRB2 AND
RP RALPB1, PHOSPHORYLATION, AND REGION.
RC TISSUE=Brain;
RX PubMed=9422736; DOI=10.1074/jbc.273.2.814;
RA Ikeda M., Ishida O., Hinoi T., Kishida S., Kikuchi A.;
RT "Identification and characterization of a novel protein interacting with
RT Ral-binding protein 1, a putative effector protein of Ral.";
RL J. Biol. Chem. 273:814-821(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Hypothalamus;
RX PubMed=12771942; DOI=10.1038/sj.onc.1206397;
RA Oosterhoff J.K., Penninkhof F., Brinkmann A.O., Anton Grootegoed J.,
RA Blok L.J.;
RT "REPS2/POB1 is downregulated during human prostate cancer progression and
RT inhibits growth factor signalling in prostate cancer cells.";
RL Oncogene 22:2920-2925(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP FUNCTION, AND INTERACTION WITH EPN1; EPS15 AND EPS15L1.
RX PubMed=10393179; DOI=10.1093/emboj/18.13.3629;
RA Nakashima S., Morinaka K., Koyama S., Ikeda M., Kishida M., Okawa K.,
RA Iwamatsu A., Kishida S., Kikuchi A.;
RT "Small G protein Ral and its downstream molecules regulate endocytosis of
RT EGF and insulin receptors.";
RL EMBO J. 18:3629-3642(1999).
RN [5]
RP INTERACTION WITH EPN1.
RX PubMed=10557078; DOI=10.1038/sj.onc.1202974;
RA Morinaka K., Koyama S., Nakashima S., Hinoi T., Okawa K., Iwamatsu A.,
RA Kikuchi A.;
RT "Epsin binds to the EH domain of POB1 and regulates receptor-mediated
RT endocytosis.";
RL Oncogene 18:5915-5922(1999).
RN [6]
RP FUNCTION, INTERACTION WITH ASAP1, MUTAGENESIS OF PRO-562 AND PRO-565, AND
RP REGION.
RX PubMed=12149250; DOI=10.1074/jbc.m203453200;
RA Oshiro T., Koyama S., Sugiyama S., Kondo A., Onodera Y., Asahara T.,
RA Sabe H., Kikuchi A.;
RT "Interaction of POB1, a downstream molecule of small G protein Ral, with
RT PAG2, a paxillin-binding protein, is involved in cell migration.";
RL J. Biol. Chem. 277:38618-38626(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; THR-479 AND SER-493, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP STRUCTURE BY NMR OF 265-367.
RX PubMed=9928989; DOI=10.1016/s0014-5793(98)01644-5;
RA Koshiba S., Kigawa T., Iwahara J., Kikuchi A., Yokoyama S.;
RT "Solution structure of the Eps15 homology domain of a human POB1 (partner
RT of RalBP1).";
RL FEBS Lett. 442:138-142(1999).
RN [9]
RP VARIANT CYS-321.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: Involved in ligand-dependent receptor mediated endocytosis of
CC the EGF and insulin receptors as part of the Ral signaling pathway
CC (PubMed:9422736, PubMed:12771942, PubMed:10393179). By controlling
CC growth factor receptors endocytosis may regulate cell survival
CC (PubMed:12771942). Through ASAP1 may regulate cell adhesion and
CC migration (PubMed:12149250). {ECO:0000269|PubMed:10393179,
CC ECO:0000269|PubMed:12149250, ECO:0000269|PubMed:12771942,
CC ECO:0000269|PubMed:9422736}.
CC -!- SUBUNIT: Interacts with EPN1; the interaction is direct
CC (PubMed:10393179, PubMed:10557078). Interacts with EPS15; the
CC interaction is direct (PubMed:10393179). Interacts with EPS15L1
CC (PubMed:10393179). Interacts with RALBP1; can form a ternary complex
CC with activated Ral (RALA or RALB) (PubMed:9422736). Interacts with
CC ASAP1; the interaction is direct and this complex can bind paxillin
CC (PubMed:12149250). Also forms a ternary complex with RALBP1 and ASAP1
CC (PubMed:12149250). Interacts with GRB2 (PubMed:9422736).
CC {ECO:0000269|PubMed:10393179, ECO:0000269|PubMed:10557078,
CC ECO:0000269|PubMed:12149250, ECO:0000269|PubMed:9422736}.
CC -!- INTERACTION:
CC Q8NFH8; O00499: BIN1; NbExp=6; IntAct=EBI-7067016, EBI-719094;
CC Q8NFH8; P62993: GRB2; NbExp=8; IntAct=EBI-7067016, EBI-401755;
CC Q8NFH8; P31947: SFN; NbExp=2; IntAct=EBI-7067016, EBI-476295;
CC Q8NFH8; P63104: YWHAZ; NbExp=2; IntAct=EBI-7067016, EBI-347088;
CC Q8NFH8; P42567: Eps15; Xeno; NbExp=10; IntAct=EBI-7067016, EBI-443923;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12771942}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=REPS2a, Long;
CC IsoId=Q8NFH8-1; Sequence=Displayed;
CC Name=2; Synonyms=REPS2b, Short;
CC IsoId=Q8NFH8-4; Sequence=VSP_040086;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the cerebrum,
CC cerebellum, lung, kidney, and testis. Weakly expressed in the kidney.
CC Isoform 2 is down-regulated during progression of prostate cancer.
CC {ECO:0000269|PubMed:12771942}.
CC -!- PTM: Tyrosine-phosphorylated upon stimulation of cells with EGF.
CC Phosphorylation on Tyr-residues induces its association with the EGF
CC receptor probably indirectly through an adapter like GRB2.
CC {ECO:0000269|PubMed:9422736}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC02901.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM43953.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/REPS2ID44120chXp22.html";
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DR EMBL; AF010233; AAC02901.1; ALT_INIT; mRNA.
DR EMBL; AF511533; AAM43933.1; -; mRNA.
DR EMBL; AF512951; AAM43953.1; ALT_INIT; mRNA.
DR EMBL; AL732371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS14180.2; -. [Q8NFH8-1]
DR CCDS; CCDS43919.1; -. [Q8NFH8-4]
DR RefSeq; NP_001074444.1; NM_001080975.1. [Q8NFH8-4]
DR RefSeq; NP_004717.2; NM_004726.2. [Q8NFH8-1]
DR PDB; 1IQ3; NMR; -; A=265-367.
DR PDBsum; 1IQ3; -.
DR AlphaFoldDB; Q8NFH8; -.
DR SMR; Q8NFH8; -.
DR BioGRID; 114622; 27.
DR IntAct; Q8NFH8; 24.
DR MINT; Q8NFH8; -.
DR STRING; 9606.ENSP00000349824; -.
DR GlyGen; Q8NFH8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NFH8; -.
DR PhosphoSitePlus; Q8NFH8; -.
DR BioMuta; REPS2; -.
DR DMDM; 34098575; -.
DR EPD; Q8NFH8; -.
DR jPOST; Q8NFH8; -.
DR MassIVE; Q8NFH8; -.
DR MaxQB; Q8NFH8; -.
DR PaxDb; Q8NFH8; -.
DR PeptideAtlas; Q8NFH8; -.
DR PRIDE; Q8NFH8; -.
DR ProteomicsDB; 73308; -. [Q8NFH8-1]
DR ProteomicsDB; 73311; -. [Q8NFH8-4]
DR Antibodypedia; 434; 118 antibodies from 27 providers.
DR DNASU; 9185; -.
DR Ensembl; ENST00000303843.7; ENSP00000306033.7; ENSG00000169891.18. [Q8NFH8-4]
DR Ensembl; ENST00000357277.8; ENSP00000349824.3; ENSG00000169891.18. [Q8NFH8-1]
DR GeneID; 9185; -.
DR KEGG; hsa:9185; -.
DR MANE-Select; ENST00000357277.8; ENSP00000349824.3; NM_004726.3; NP_004717.2.
DR UCSC; uc004cxv.1; human. [Q8NFH8-1]
DR CTD; 9185; -.
DR DisGeNET; 9185; -.
DR GeneCards; REPS2; -.
DR HGNC; HGNC:9963; REPS2.
DR HPA; ENSG00000169891; Tissue enhanced (brain).
DR MIM; 300317; gene.
DR neXtProt; NX_Q8NFH8; -.
DR OpenTargets; ENSG00000169891; -.
DR PharmGKB; PA34330; -.
DR VEuPathDB; HostDB:ENSG00000169891; -.
DR eggNOG; KOG1955; Eukaryota.
DR GeneTree; ENSGT00940000158080; -.
DR HOGENOM; CLU_014864_1_0_1; -.
DR InParanoid; Q8NFH8; -.
DR OMA; QMHAAPY; -.
DR OrthoDB; 1319710at2759; -.
DR PhylomeDB; Q8NFH8; -.
DR TreeFam; TF316546; -.
DR PathwayCommons; Q8NFH8; -.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; Q8NFH8; -.
DR SIGNOR; Q8NFH8; -.
DR BioGRID-ORCS; 9185; 9 hits in 699 CRISPR screens.
DR ChiTaRS; REPS2; human.
DR EvolutionaryTrace; Q8NFH8; -.
DR GeneWiki; REPS2; -.
DR GenomeRNAi; 9185; -.
DR Pharos; Q8NFH8; Tbio.
DR PRO; PR:Q8NFH8; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8NFH8; protein.
DR Bgee; ENSG00000169891; Expressed in middle temporal gyrus and 157 other tissues.
DR Genevisible; Q8NFH8; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR CDD; cd00052; EH; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR Pfam; PF12763; EF-hand_4; 1.
DR SMART; SM00027; EH; 1.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Coiled coil; Cytoplasm;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..660
FT /note="RalBP1-associated Eps domain-containing protein 2"
FT /id="PRO_0000073831"
FT DOMAIN 34..147
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 282..373
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 315..350
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 169..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..660
FT /note="Interaction with RALBP1"
FT /evidence="ECO:0000269|PubMed:9422736"
FT REGION 561..660
FT /note="Interaction with ASAP1"
FT /evidence="ECO:0000269|PubMed:12149250"
FT COILED 601..657
FT /evidence="ECO:0000255"
FT COMPBIAS 486..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..523
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 328
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 182
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12771942"
FT /id="VSP_040086"
FT VARIANT 321
FT /note="S -> C"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069419"
FT MUTAGEN 562
FT /note="P->A: Abolishes interaction with ASAP1."
FT /evidence="ECO:0000269|PubMed:12149250"
FT MUTAGEN 565
FT /note="P->A: Abolishes interaction with ASAP1."
FT /evidence="ECO:0000269|PubMed:12149250"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:1IQ3"
FT HELIX 283..293
FT /evidence="ECO:0007829|PDB:1IQ3"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:1IQ3"
FT HELIX 303..309
FT /evidence="ECO:0007829|PDB:1IQ3"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:1IQ3"
FT HELIX 320..327
FT /evidence="ECO:0007829|PDB:1IQ3"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:1IQ3"
FT STRAND 333..336
FT /evidence="ECO:0007829|PDB:1IQ3"
FT HELIX 337..352
FT /evidence="ECO:0007829|PDB:1IQ3"
SQ SEQUENCE 660 AA; 71534 MW; AACB3B8B8A9C2E3A CRC64;
MEAAAAAAAA AAAAAAAGGG CGSGPPPLLL SEGEQQCYSE LFARCAGAAG GGPGSGPPEA
ARVAPGTATA AAGPVADLFR ASQLPAETLH QITELCGAKR VGYFGPTQFY IALKLIAAAQ
SGLPVRIESI KCELPLPRFM MSKNDGEIRF GNPAELHGTK VQIPYLTTEK NSFKRMDDED
KQQETQSPTM SPLASPPSSP PHYQRVPLSH GYSKLRSSAE QMHPAPYEAR QPLVQPEGSS
SGGPGTKPLR HQASLIRSFS VERELQDNSS YPDEPWRITE EQREYYVNQF RSLQPDPSSF
ISGSVAKNFF TKSKLSIPEL SYIWELSDAD CDGALTLPEF CAAFHLIVAR KNGYPLPEGL
PPTLQPEYLQ AAFPKPKWDC QLFDSYSESL PANQQPRDLN RMEKTSVKDM ADLPVPNQDV
TSDDKQALKS TINEALPKDV SEDPATPKDS NSLKARPRSR SYSSTSIEEA MKRGEDPPTP
PPRPQKTHSR ASSLDLNKVF QPSVPATKSG LLPPPPALPP RPCPSQSEQV SEAELLPQLS
RAPSQAAESS PAKKDVLYSQ PPSKPIRRKF RPENQATENQ EPSTAASGPA SAATMKPHPT
VQKQSSKQKK AIQTAIRKNK EANAVLARLN SELQQQLKEV HQERIALENQ LEQLRPVTVL
