RABE1_MOUSE
ID RABE1_MOUSE Reviewed; 862 AA.
AC O35551; A1L322; Q5QNU3; Q99L08; Q9CRP3; Q9EQF9; Q9JI94;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Rab GTPase-binding effector protein 1;
DE AltName: Full=Rabaptin-5;
DE AltName: Full=Rabaptin-5alpha;
GN Name=Rabep1; Synonyms=Rab5ep, Rabpt5, Rabpt5a;
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 1).
RC STRAIN=ICR; TISSUE=Brain, and Muscle;
RX PubMed=9427343; DOI=10.1097/00001756-199711100-00045;
RA Nishimune H., Uyeda A., Nogawa M., Fujimori K., Taguchi T.;
RT "Neurocrescin: a novel neurite-outgrowth factor secreted by muscle after
RT denervation.";
RL NeuroReport 8:3649-3654(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=CBA/J; TISSUE=Embryo;
RX PubMed=11977240;
RA Korobko E.V., Smirnova E.V., Kiselev S.L., Georgiev G.P., Korobko I.V.;
RT "Identification of a new alternative-splicing transcript of rabaptin-5
RT interacting with protein kinase MAK-V.";
RL Dokl. Biochem. 370:1-3(2000).
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 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-316 (ISOFORMS 1/4/5).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-410, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407; THR-408 AND SER-410, AND
RP 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 [9]
RP INTERACTION WITH KCNH1.
RX PubMed=22841712; DOI=10.1016/j.febslet.2012.07.055;
RA Ninkovic M., Mitkovski M., Kohl T., Stuhmer W., Pardo L.A.;
RT "Physical and functional interaction of KV10.1 with Rabaptin-5 impacts ion
RT channel trafficking.";
RL FEBS Lett. 586:3077-3084(2012).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PKD1 AND GGA1.
RX PubMed=25405894; DOI=10.1038/ncomms6482;
RA Kim H., Xu H., Yao Q., Li W., Huang Q., Outeda P., Cebotaru V.,
RA Chiaravalli M., Boletta A., Piontek K., Germino G.G., Weinman E.J.,
RA Watnick T., Qian F.;
RT "Ciliary membrane proteins traffic through the Golgi via a
RT Rabep1/GGA1/Arl3-dependent mechanism.";
RL Nat. Commun. 5:5482-5482(2014).
CC -!- FUNCTION: Rab effector protein acting as linker between gamma-adaptin,
CC RAB4A and RAB5A. Involved in endocytic membrane fusion and membrane
CC trafficking of recycling endosomes. Involved in KCNH1 channels
CC trafficking to and from the cell membrane. Stimulates RABGEF1 mediated
CC nucleotide exchange on RAB5A. Mediates the traffic of PKD1:PKD2 complex
CC from the endoplasmic reticulum through the Golgi to the cilium
CC (PubMed:25405894). {ECO:0000250|UniProtKB:Q15276,
CC ECO:0000269|PubMed:25405894}.
CC -!- SUBUNIT: Heterodimer with RABGEF1. The heterodimer binds RAB4A and
CC RAB5A that have been activated by GTP-binding. Interacts with TSC2 (By
CC similarity). Interacts with GGA1 (via GAE domain), GGA2 (via GAE
CC domain) and GGA3 (via GAE domain) (By similarity). Interacts with AP1G1
CC (via GAE domain) (By similarity). Interacts with AP1G2 (via GAE domain)
CC (By similarity). Interacts with ECPAS (By similarity). Interacts with
CC KCNH1 (PubMed:22841712). Interacts with PKD1 (via C-terminal domain)
CC and GGA1; the interactions recruit PKD1:PKD2 complex to GGA1 and ARL3
CC at trans-Golgi network (PubMed:25405894). Interacts with KCNH1 (By
CC similarity). {ECO:0000250|UniProtKB:O35550,
CC ECO:0000250|UniProtKB:Q15276, ECO:0000269|PubMed:22841712,
CC ECO:0000269|PubMed:25405894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Early endosome
CC {ECO:0000250}. Recycling endosome {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=Rabaptin-5;
CC IsoId=O35551-1; Sequence=Displayed;
CC Name=2; Synonyms=Rabaptin-5gamma;
CC IsoId=O35551-2; Sequence=VSP_010452;
CC Name=3; Synonyms=Rabaptin-5delta;
CC IsoId=O35551-3; Sequence=VSP_010453;
CC Name=4;
CC IsoId=O35551-4; Sequence=VSP_010454, VSP_010455;
CC Name=5;
CC IsoId=O35551-5; Sequence=VSP_010456, VSP_010457;
CC Name=6;
CC IsoId=O35551-6; Sequence=VSP_025444;
CC -!- PTM: Proteolytic cleavage by caspases in apoptotic cells causes loss of
CC endosome fusion activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the rabaptin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH03921.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D86066; BAA21783.1; -; mRNA.
DR EMBL; AB001750; BAA23818.1; -; mRNA.
DR EMBL; AF248489; AAF78238.1; -; mRNA.
DR EMBL; AF248490; AAG44544.1; -; mRNA.
DR EMBL; AL596136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR933735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR936845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466596; EDL12625.1; -; Genomic_DNA.
DR EMBL; BC129854; AAI29855.1; -; mRNA.
DR EMBL; BC003921; AAH03921.1; ALT_INIT; mRNA.
DR EMBL; BC060166; AAH60166.1; -; mRNA.
DR EMBL; BC129853; AAI29854.1; -; mRNA.
DR EMBL; AK019413; BAB31710.3; -; mRNA.
DR CCDS; CCDS24968.1; -. [O35551-1]
DR CCDS; CCDS70232.1; -. [O35551-2]
DR CCDS; CCDS78984.1; -. [O35551-3]
DR RefSeq; NP_001278070.1; NM_001291141.1. [O35551-2]
DR RefSeq; NP_001278071.1; NM_001291142.1. [O35551-3]
DR RefSeq; NP_001278072.1; NM_001291143.1.
DR RefSeq; NP_062273.2; NM_019400.3. [O35551-1]
DR AlphaFoldDB; O35551; -.
DR SMR; O35551; -.
DR BioGRID; 207592; 15.
DR CORUM; O35551; -.
DR IntAct; O35551; 5.
DR MINT; O35551; -.
DR STRING; 10090.ENSMUSP00000075619; -.
DR iPTMnet; O35551; -.
DR PhosphoSitePlus; O35551; -.
DR EPD; O35551; -.
DR jPOST; O35551; -.
DR MaxQB; O35551; -.
DR PaxDb; O35551; -.
DR PeptideAtlas; O35551; -.
DR PRIDE; O35551; -.
DR ProteomicsDB; 253157; -. [O35551-1]
DR ProteomicsDB; 253158; -. [O35551-2]
DR ProteomicsDB; 253159; -. [O35551-3]
DR ProteomicsDB; 253160; -. [O35551-4]
DR ProteomicsDB; 253161; -. [O35551-5]
DR ProteomicsDB; 253162; -. [O35551-6]
DR Antibodypedia; 3875; 123 antibodies from 27 providers.
DR DNASU; 54189; -.
DR Ensembl; ENSMUST00000076270; ENSMUSP00000075619; ENSMUSG00000020817. [O35551-1]
DR Ensembl; ENSMUST00000081362; ENSMUSP00000080102; ENSMUSG00000020817. [O35551-3]
DR Ensembl; ENSMUST00000100928; ENSMUSP00000098488; ENSMUSG00000020817. [O35551-5]
DR Ensembl; ENSMUST00000108533; ENSMUSP00000104173; ENSMUSG00000020817. [O35551-6]
DR Ensembl; ENSMUST00000178245; ENSMUSP00000137267; ENSMUSG00000020817. [O35551-2]
DR GeneID; 54189; -.
DR KEGG; mmu:54189; -.
DR UCSC; uc007jwr.3; mouse. [O35551-1]
DR UCSC; uc007jwt.3; mouse. [O35551-2]
DR UCSC; uc007jwu.1; mouse. [O35551-5]
DR UCSC; uc011xyb.2; mouse. [O35551-3]
DR CTD; 9135; -.
DR MGI; MGI:1860236; Rabep1.
DR VEuPathDB; HostDB:ENSMUSG00000020817; -.
DR eggNOG; KOG0993; Eukaryota.
DR GeneTree; ENSGT00530000063743; -.
DR InParanoid; O35551; -.
DR OMA; MSPSGYR; -.
DR OrthoDB; 1495285at2759; -.
DR TreeFam; TF329365; -.
DR BioGRID-ORCS; 54189; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Rabep1; mouse.
DR PRO; PR:O35551; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O35551; protein.
DR Bgee; ENSMUSG00000020817; Expressed in dentate gyrus of hippocampal formation granule cell and 260 other tissues.
DR ExpressionAtlas; O35551; baseline and differential.
DR Genevisible; O35551; MM.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:UniProtKB.
DR GO; GO:1903441; P:protein localization to ciliary membrane; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR InterPro; IPR003914; Rabaptin.
DR InterPro; IPR029880; Rabaptin-5.
DR InterPro; IPR018514; Rabaptin_coiled-coil.
DR InterPro; IPR015390; Rabaptin_Rab5-bd_dom.
DR PANTHER; PTHR31179; PTHR31179; 1.
DR PANTHER; PTHR31179:SF5; PTHR31179:SF5; 1.
DR Pfam; PF09311; Rab5-bind; 1.
DR Pfam; PF03528; Rabaptin; 1.
DR PRINTS; PR01432; RABAPTIN.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Endocytosis; Endosome; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15276"
FT CHAIN 2..862
FT /note="Rab GTPase-binding effector protein 1"
FT /id="PRO_0000187557"
FT REGION 315..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 11..345
FT /evidence="ECO:0000255"
FT COILED 534..816
FT /evidence="ECO:0000255"
FT COMPBIAS 315..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15276"
FT MOD_RES 282
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15276"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15276"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15276"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..54
FT /note="MAQPGPAPQPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQKRAKFKELYLA
FT KE -> MAQPGPAPQPD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11977240"
FT /id="VSP_010452"
FT VAR_SEQ 176..215
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11977240"
FT /id="VSP_010453"
FT VAR_SEQ 366..367
FT /note="EH -> VK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010454"
FT VAR_SEQ 368..862
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010455"
FT VAR_SEQ 522..556
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010456"
FT VAR_SEQ 738
FT /note="I -> IVL (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025444"
FT VAR_SEQ 831..862
FT /note="QLERIRQADSLERIRAILNDTKLTDINQLPET -> RCLGNHHGPSVGGGTN
FT VAGGLGSPLSLPQIFA (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010457"
FT CONFLICT 68
FT /note="Q -> K (in Ref. 6; BAB31710)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="Q -> R (in Ref. 1; BAA23818/BAA21783 and 2;
FT AAF78238/AAG44544)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 862 AA; 99524 MW; 5796514BB94E7CE5 CRC64;
MAQPGPAPQP DVSLQQRVAE LEKINAEFLR AQQQLEQEFN QKRAKFKELY LAKEEDLKRQ
NAVLQAAQDD LGHLRTQLWE AQAEMENIKA IATVSENTKQ EAIDEVKRQW REEVASLQAI
MKETVRDYEH QFHLRLEQER AQWAQYRESA EREIADLRRR LSEGQEEENL ENEMKKAQED
AEKLRSVVMP MEKEIAALKD KLTEAEDKIK ELEASKVKEL NHYLEAEKSC RTDLEMYVAV
LNTQKSVLQE DAEKLRKELH EVCHLLEQER QQHNQLKHTW QKANDQFLES QRLLMRDMQR
MEIVLTSEQL RQVEELKKKD QEEDEQQRVN KRKDNKKTDT EEEVKIPVVC ALTQEESSTP
LSNEEEHLDS THGSVHSLDA DLMLPSGDPF SKSDNDMFKD GLRRAQSTDS LGTSSSLQSK
ALGYNYKAKS AGNLDESDFG PLVGADSVSE NFDTVSLGSL QMPSGFMLTK DQERAIKAMT
PEQEETASLL SSVTQGMESA YVSPSGYRLV SETEWNLLQK EVHNAGNKLG RRCDMCSNYE
KQLQGIQIQE AETRDQVKKL QLMLRQANDQ LEKTMKEKQE LEDFLKQSAE DSSHQISALV
LRAQASEVLL EELQQSFSQA KRDVQEQMAV LMQSREQVSE ELVRLQKDND SLQGKHSLHV
SLQLAEDFIL PDTVEVLREL VLKYRENIVH VRTAADHMEE KLKAEILFLK EQIQAEQCLK
ENLEETLQLE IENCKEEIAS ISSLKAELER IKVEKGQLES TLREKSQQLE SLQEMKVNLE
EQLKKETAAK ATVEQLMFEE KNKAQRLQTE LDVSEQVQRD FVKLSQTLQV QLERIRQADS
LERIRAILND TKLTDINQLP ET
