REPS1_MOUSE
ID REPS1_MOUSE Reviewed; 795 AA.
AC O54916; Q3UAM3; Q5PPQ9; Q8C9J9; Q99LR8;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=RalBP1-associated Eps domain-containing protein 1;
DE AltName: Full=RalBP1-interacting protein 1;
GN Name=Reps1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND CHARACTERIZATION.
RC TISSUE=Muscle;
RX PubMed=9395447; DOI=10.1074/jbc.272.50.31230;
RA Yamaguchi A., Urano T., Goi T., Feig L.A.;
RT "An eps homology (EH) domain protein that binds to the ral-GTPase target,
RT RalBP1.";
RL J. Biol. Chem. 272:31230-31234(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 39-795 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 499-795 (ISOFORM 1).
RC TISSUE=Embryo, and Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-708, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272; SER-273; SER-539 AND
RP THR-543, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP STRUCTURE BY NMR OF 279-370.
RX PubMed=11389591; DOI=10.1021/bi002700m;
RA Kim S., Cullis D.N., Feig L.A., Baleja J.D.;
RT "Solution structure of the Reps1 EH domain and characterization of its
RT binding to NPF target sequences.";
RL Biochemistry 40:6776-6785(2001).
CC -!- FUNCTION: May coordinate the cellular actions of activated EGF
CC receptors and Ral-GTPases.
CC -!- SUBUNIT: Homodimer (Potential). Interacts with RALBP1, CRK and GRB2.
CC Binding to RALBP1 does not affect its Ral-binding activity. Forms a
CC complex with the SH3 domains of CRK and GRB2 which may link it to an
CC EGF-responsive tyrosine kinase. Interacts with RAB11FIP2 (By
CC similarity). Interacts with AMPH, ITSN1 (via SH3 domains) and SGIP1;
CC may be involved in clathrin-mediated endocytosis (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}.
CC Note=Colocalize with ITSN1 at the plasma membrane in structures that
CC are most probably clathrin-coated pits. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O54916-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O54916-2; Sequence=VSP_038337, VSP_007956, VSP_007957;
CC Name=3;
CC IsoId=O54916-3; Sequence=VSP_038336, VSP_038338;
CC Name=4;
CC IsoId=O54916-4; Sequence=VSP_038336;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. The highest
CC level expression was found in the kidney and testis.
CC -!- PTM: EGF stimulates phosphorylation on Tyr-residues.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE29439.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE30291.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF031939; AAB94736.1; -; mRNA.
DR EMBL; AK150284; BAE29439.1; ALT_INIT; mRNA.
DR EMBL; AK151309; BAE30291.1; ALT_INIT; mRNA.
DR EMBL; AK041967; BAC31117.1; -; mRNA.
DR EMBL; AC153433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002256; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC087547; AAH87547.1; -; mRNA.
DR CCDS; CCDS23710.2; -. [O54916-1]
DR PIR; T09173; T09173.
DR RefSeq; NP_001104535.1; NM_001111065.1.
DR RefSeq; NP_033074.2; NM_009048.2. [O54916-1]
DR PDB; 1FI6; NMR; -; A=279-370.
DR PDBsum; 1FI6; -.
DR AlphaFoldDB; O54916; -.
DR BMRB; O54916; -.
DR SMR; O54916; -.
DR BioGRID; 202861; 13.
DR CORUM; O54916; -.
DR IntAct; O54916; 2.
DR STRING; 10090.ENSMUSP00000123238; -.
DR iPTMnet; O54916; -.
DR PhosphoSitePlus; O54916; -.
DR EPD; O54916; -.
DR jPOST; O54916; -.
DR MaxQB; O54916; -.
DR PaxDb; O54916; -.
DR PeptideAtlas; O54916; -.
DR PRIDE; O54916; -.
DR ProteomicsDB; 255283; -. [O54916-1]
DR ProteomicsDB; 255284; -. [O54916-2]
DR ProteomicsDB; 255285; -. [O54916-3]
DR ProteomicsDB; 255286; -. [O54916-4]
DR Antibodypedia; 33064; 119 antibodies from 25 providers.
DR Ensembl; ENSMUST00000126390; ENSMUSP00000123238; ENSMUSG00000019854. [O54916-1]
DR GeneID; 19707; -.
DR KEGG; mmu:19707; -.
DR UCSC; uc007ema.2; mouse. [O54916-1]
DR CTD; 85021; -.
DR MGI; MGI:1196373; Reps1.
DR VEuPathDB; HostDB:ENSMUSG00000019854; -.
DR eggNOG; KOG1955; Eukaryota.
DR GeneTree; ENSGT00940000158749; -.
DR HOGENOM; CLU_014864_0_0_1; -.
DR InParanoid; O54916; -.
DR OMA; QCCDVEN; -.
DR OrthoDB; 1319710at2759; -.
DR PhylomeDB; O54916; -.
DR TreeFam; TF316546; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 19707; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Reps1; mouse.
DR EvolutionaryTrace; O54916; -.
DR PRO; PR:O54916; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O54916; protein.
DR Bgee; ENSMUSG00000019854; Expressed in undifferentiated genital tubercle and 260 other tissues.
DR ExpressionAtlas; O54916; baseline and differential.
DR Genevisible; O54916; MM.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:InterPro.
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 InterPro; IPR026814; Reps1.
DR PANTHER; PTHR11216:SF63; PTHR11216:SF63; 1.
DR Pfam; PF12763; EF-hand_4; 1.
DR SMART; SM00027; EH; 2.
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; Coated pit; Coiled coil;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..795
FT /note="RalBP1-associated Eps domain-containing protein 1"
FT /id="PRO_0000073830"
FT DOMAIN 10..113
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 285..374
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 318..353
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 112..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..795
FT /note="Interaction with RALBP1"
FT COILED 750..790
FT /evidence="ECO:0000255"
FT COMPBIAS 112..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..597
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 333
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 342
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96D71"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96D71"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96D71"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96D71"
FT MOD_RES 173
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96D71"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 288
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96D71"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96D71"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96D71"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96D71"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 543
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96D71"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96D71"
FT VAR_SEQ 1..244
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038337"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9395447"
FT /id="VSP_038336"
FT VAR_SEQ 420..454
FT /note="QWETFSERSSSSQTLTQFDSNIAPADPDTAIVHPV -> VSKTSLSLLEISL
FT FTGRSFKQDRFTAGYLQYAHTP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007956"
FT VAR_SEQ 420..446
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038338"
FT VAR_SEQ 455..795
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007957"
FT CONFLICT 161
FT /note="V -> A (in Ref. 1; AAB94736)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="D -> N (in Ref. 2; BAE29439)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="P -> T (in Ref. 2; BAE29439)"
FT /evidence="ECO:0000305"
FT HELIX 283..293
FT /evidence="ECO:0007829|PDB:1FI6"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:1FI6"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:1FI6"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:1FI6"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:1FI6"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:1FI6"
FT HELIX 340..355
FT /evidence="ECO:0007829|PDB:1FI6"
SQ SEQUENCE 795 AA; 86519 MW; 98D788160F560509 CRC64;
MEGLTLSDAE QKYYSDLFSY CDIESTKKVV VNGRVLELFR AAQLPNDVVL QIMELCGATR
LGYFGRSQFY IALKLVAVAQ SGFPLRVESI NTVKDLPLPR FVASKNEQES RLAASYSSDS
ENQGSYSGVI PPPPGRGQVK KGPGSHDAVQ PRPSAEQQEP VSPVVSPQQS PPTSPHTWRK
HSRHPSGGNS ERPLTGPGPF WSPFGDAQAG SSAGDAVWSG QSPPPPQDNW VSFADTPPTS
ALLTMHPASV QDQTTVRTVA SAATANEIRR QSSSYEDPWK ITDEQRQYYV NQFKTIQPDL
NGFIPGSAAK EFFTKSKLPI LELSHIWELS DFDKDGALTL DEFCAAFHLV VARKNGYDLP
EKLPESLMPK LIDLEDSADV GEQPGEVGYS GSPAEAPPSK SPSMPSLNQT WPELNQSSEQ
WETFSERSSS SQTLTQFDSN IAPADPDTAI VHPVPIRMTP SKIHMQEMEL KRTSSDHTNP
TSPLLVKPSD LSEENKINSS VKFPSGNTVD GYSSSDSFPS DPEQIGSSVT RQRSHSGTSP
DNTAPPPPPP RPQPSHSRSS SLDMNRTFAV TTGQQQAGVV AHPPAVPPRP QPSQAPGPSV
HRPVDADGLI THTSTSPQQI PEQPNFADFS QFEVFAASNV SEEQDSEAEK HPEVLPAEKA
SDPSSSLRAA QADSKAEEKT ATNVPANVSK GTTPLAPPPK PVRRRLKSED ELRPDVDEHT
QKTGVLAAVL TSQPSIPRSV GKDKKAIQAS IRRNKETNTV LARLNSELQQ QLKDVLEERI
SLEVQLEQLR PFSHL
