LGR5_MOUSE
ID LGR5_MOUSE Reviewed; 907 AA.
AC Q9Z1P4; Q3V1L2;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Leucine-rich repeat-containing G-protein coupled receptor 5;
DE AltName: Full=G-protein coupled receptor 49;
DE AltName: Full=Orphan G-protein coupled receptor FEX {ECO:0000303|PubMed:9920770};
DE Flags: Precursor;
GN Name=Lgr5; Synonyms=Fex {ECO:0000303|PubMed:9920770}, Gpr49;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=9920770; DOI=10.1006/bbrc.1998.9882;
RA Hermey G., Methner A., Schaller H.C., Hermans-Borgmeyer I.;
RT "Identification of a novel seven-transmembrane receptor with homology to
RT glycoprotein receptors and its expression in the adult and developing
RT mouse.";
RL Biochem. Biophys. Res. Commun. 254:273-279(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 [3]
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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=15509778; DOI=10.1128/mcb.24.22.9736-9743.2004;
RA Morita H., Mazerbourg S., Bouley D.M., Luo C.W., Kawamura K., Kuwabara Y.,
RA Baribault H., Tian H., Hsueh A.J.;
RT "Neonatal lethality of LGR5 null mice is associated with ankyloglossia and
RT gastrointestinal distension.";
RL Mol. Cell. Biol. 24:9736-9743(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=17934449; DOI=10.1038/nature06196;
RA Barker N., van Es J.H., Kuipers J., Kujala P., van den Born M.,
RA Cozijnsen M., Haegebarth A., Korving J., Begthel H., Peters P.J.,
RA Clevers H.;
RT "Identification of stem cells in small intestine and colon by marker gene
RT Lgr5.";
RL Nature 449:1003-1007(2007).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=18849992; DOI=10.1038/ng.239;
RA Jaks V., Barker N., Kasper M., van Es J.H., Snippert H.J., Clevers H.,
RA Toftgard R.;
RT "Lgr5 marks cycling, yet long-lived, hair follicle stem cells.";
RL Nat. Genet. 40:1291-1299(2008).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21727895; DOI=10.1038/nature10337;
RA de Lau W., Barker N., Low T.Y., Koo B.K., Li V.S., Teunissen H., Kujala P.,
RA Haegebarth A., Peters P.J., van de Wetering M., Stange D.E., van Es J.E.,
RA Guardavaccaro D., Schasfoort R.B., Mohri Y., Nishimori K., Mohammed S.,
RA Heck A.J., Clevers H.;
RT "Lgr5 homologues associate with Wnt receptors and mediate R-spondin
RT signalling.";
RL Nature 476:293-297(2011).
RN [8]
RP DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=29769720; DOI=10.1038/s41586-018-0118-y;
RA Szenker-Ravi E., Altunoglu U., Leushacke M., Bosso-Lefevre C., Khatoo M.,
RA Thi Tran H., Naert T., Noelanders R., Hajamohideen A., Beneteau C.,
RA de Sousa S.B., Karaman B., Latypova X., Basaran S., Yuecel E.B., Tan T.T.,
RA Vlaminck L., Nayak S.S., Shukla A., Girisha K.M., Le Caignec C.,
RA Soshnikova N., Uyguner Z.O., Vleminckx K., Barker N., Kayserili H.,
RA Reversade B.;
RT "RSPO2 inhibition of RNF43 and ZNRF3 governs limb development independently
RT of LGR4/5/6.";
RL Nature 557:564-569(2018).
CC -!- FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt
CC signaling pathway and acts as a stem cell marker of the intestinal
CC epithelium and the hair follicle. Upon binding to R-spondins (RSPO1,
CC RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and
CC frizzled receptors that are activated by extracellular Wnt receptors,
CC triggering the canonical Wnt signaling pathway to increase expression
CC of target genes. In contrast to classical G-protein coupled receptors,
CC does not activate heterotrimeric G-proteins to transduce the signal.
CC Involved in the development and/or maintenance of the adult intestinal
CC stem cells during postembryonic development.
CC {ECO:0000269|PubMed:21727895}.
CC -!- SUBUNIT: Identified in a complex composed of RNF43, LGR5 and RSPO1 (By
CC similarity). Also interacts with other R-spondin ligands, including
CC RSPO2, RSPO3 and RSPO4 (By similarity). {ECO:0000250|UniProtKB:O75473}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Rapidly and constitutively
CC internalized to the trans-Golgi network at steady state. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the gonads, the adrenal gland, and in
CC the brain. In the central nervous system expression is restricted to
CC the olfactory bulb. In the adrenal gland detected only in the neural-
CC crest derived chromaffin cells of the medulla, but not in the cells of
CC the adrenal cortex. In the gonads, the expression is high in Graafian
CC follicle, but absent from primary and secondary follicles. In the
CC intestine, exclusively expressed in cycling crypt base columnar cells.
CC Expressed in the lower bulge and secondary germ area of telogen hair
CC follicles and in the lower outer root sheath of anagen hair follicle.
CC {ECO:0000269|PubMed:17934449, ECO:0000269|PubMed:18849992,
CC ECO:0000269|PubMed:9920770}.
CC -!- DEVELOPMENTAL STAGE: First expressed at 8.5 dpc in a few cells of the
CC ectoplacental cone and, at 9.5 dpc, in a greater number of cells in the
CC labyrinthine region of the forming placenta. In the embryo per se,
CC expression starts at 9.5 dpc. At 10.5 dpc, detected in the facial area
CC in the tissue overlaying the mandibular cleft and in the optic cup. In
CC the central nervous system, expressed in the neuroepithelium at the
CC roof of the mesencephalon and in the spinal cord. At 11.5 dpc, in the
CC central nervous system, expressed in the neuroepithelium at the border
CC between mes- and metencephalon and that lining the fourth ventricle and
CC the retina, as well as in the spinal cord. Outside the nervous system,
CC at 11.5 dpc, expressed in the mesenchyme over-laying the mandibular
CC cleft, in the distal limb buds, especially the hind limb buds, as well
CC as in the perichordal mesenchyme in the rostral region of the embryo.
CC At 12.5 dpc, in the central nervous system, highly expressed in the
CC rhombencephalic isthmus. In the facial area, expressed in the
CC mesenchyme surrounding the olfactory epithelium and the forming
CC vibrissae. Expression in the hind and front limb buds increases and
CC spreads to more proximal directions, but is restricted to the area were
CC the digits develop. At 13.5 dpc, the expression in the brain becomes
CC restricted to the border between mes- and diencephalon. Also detected
CC in the pituitary. Strongly expressed in the mesenchyme adjacent to the
CC mandibular cleft, as well as in the most lateral aspects of the tongue
CC and the teeth anlagen. Weak expression in the body wall and mesenchyme
CC surrounding internal organs. At 14.5 dpc, becomes hardly detectable in
CC the nervous system. In the body, expressed in the perichondrium, but
CC levels decrease with ongoing age (PubMed:9920770). In the limbs, at
CC 14.5 dpc, expressed in the mesenchyme, but not in the overlying
CC ectoderm of the limb bud. In developing lungs, at 14.5 dpc, expressed
CC at low levels in both the epithelium and mesenchyme lineages
CC (PubMed:29769720). {ECO:0000269|PubMed:29769720,
CC ECO:0000269|PubMed:9920770}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit malformation of the tongue and of
CC lower jam causing newborns to swallow air leading to 100% neonatal
CC lethality. Conditional knockout of both Lgr4 and Lgr5 in the gut
CC results in Wnt signaling inhibition and results in the rapid demise of
CC intestinal crypts (PubMed:21727895). Simultaneous knockdown of LGR4,
CC LGR5 and LGR6 results in developmental phenotypes, such as cleft palate
CC and ankyloglossia, but not in tetra-amelia with lung agenesis
CC (PubMed:29769720). {ECO:0000269|PubMed:15509778,
CC ECO:0000269|PubMed:21727895, ECO:0000269|PubMed:29769720}.
CC -!- MISCELLANEOUS: LGR5 is used as a marker of adult tissue stem cells in
CC the intestine, stomach, hair follicle, and mammary epithelium.
CC {ECO:0000305|PubMed:17934449}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF110818; AAD14684.1; -; mRNA.
DR EMBL; AK132387; BAE21138.1; -; mRNA.
DR EMBL; CH466539; EDL21773.1; -; Genomic_DNA.
DR CCDS; CCDS24180.1; -.
DR PIR; JG0193; JG0193.
DR RefSeq; NP_034325.2; NM_010195.2.
DR AlphaFoldDB; Q9Z1P4; -.
DR SMR; Q9Z1P4; -.
DR BioGRID; 199635; 3.
DR STRING; 10090.ENSMUSP00000020350; -.
DR GlyGen; Q9Z1P4; 4 sites.
DR iPTMnet; Q9Z1P4; -.
DR PhosphoSitePlus; Q9Z1P4; -.
DR MaxQB; Q9Z1P4; -.
DR PaxDb; Q9Z1P4; -.
DR PRIDE; Q9Z1P4; -.
DR ProteomicsDB; 252468; -.
DR Antibodypedia; 1987; 895 antibodies from 42 providers.
DR DNASU; 14160; -.
DR Ensembl; ENSMUST00000020350; ENSMUSP00000020350; ENSMUSG00000020140.
DR GeneID; 14160; -.
DR KEGG; mmu:14160; -.
DR UCSC; uc007hbi.1; mouse.
DR CTD; 8549; -.
DR MGI; MGI:1341817; Lgr5.
DR VEuPathDB; HostDB:ENSMUSG00000020140; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2087; Eukaryota.
DR GeneTree; ENSGT00940000160214; -.
DR HOGENOM; CLU_006843_0_0_1; -.
DR InParanoid; Q9Z1P4; -.
DR OMA; LHHNEIY; -.
DR OrthoDB; 340670at2759; -.
DR PhylomeDB; Q9Z1P4; -.
DR TreeFam; TF316814; -.
DR Reactome; R-MMU-4641263; Regulation of FZD by ubiquitination.
DR BioGRID-ORCS; 14160; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Lgr5; mouse.
DR PRO; PR:Q9Z1P4; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9Z1P4; protein.
DR Bgee; ENSMUSG00000020140; Expressed in crypt of Lieberkuhn of small intestine and 164 other tissues.
DR ExpressionAtlas; Q9Z1P4; baseline and differential.
DR Genevisible; Q9Z1P4; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR GO; GO:0016500; F:protein-hormone receptor activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:UniProtKB.
DR GO; GO:2001013; P:epithelial cell proliferation involved in renal tubule morphogenesis; IGI:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0001942; P:hair follicle development; IGI:MGI.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0009994; P:oocyte differentiation; IMP:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR002131; Gphrmn_rcpt_fam.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF01462; LRRNT; 1.
DR PRINTS; PR00373; GLYCHORMONER.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM00369; LRR_TYP; 13.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS51450; LRR; 15.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Golgi apparatus; Leucine-rich repeat; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..907
FT /note="Leucine-rich repeat-containing G-protein coupled
FT receptor 5"
FT /id="PRO_0000012795"
FT TOPO_DOM 22..561
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..638
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..682
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 683..703
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 704..723
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 745..767
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..788
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 789..802
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..823
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 824..907
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..66
FT /note="LRRNT"
FT REPEAT 67..88
FT /note="LRR 1"
FT REPEAT 91..112
FT /note="LRR 2"
FT REPEAT 115..136
FT /note="LRR 3"
FT REPEAT 139..160
FT /note="LRR 4"
FT REPEAT 163..184
FT /note="LRR 5"
FT REPEAT 187..208
FT /note="LRR 6"
FT REPEAT 211..232
FT /note="LRR 7"
FT REPEAT 235..256
FT /note="LRR 8"
FT REPEAT 258..279
FT /note="LRR 9"
FT REPEAT 282..303
FT /note="LRR 10"
FT REPEAT 306..325
FT /note="LRR 11"
FT REPEAT 329..350
FT /note="LRR 12"
FT REPEAT 353..374
FT /note="LRR 13"
FT REPEAT 375..396
FT /note="LRR 14"
FT REPEAT 399..420
FT /note="LRR 15"
FT REPEAT 423..446
FT /note="LRR 16"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 38..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 348..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 479..541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 637..712
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 128
FT /note="Q -> K (in Ref. 1; AAD14684)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="K -> N (in Ref. 1; AAD14684)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="A -> T (in Ref. 1; AAD14684)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 907 AA; 99666 MW; 5E202CB356DB12CF CRC64;
MDTSCVHMLL SLLALLQLVA AGSSPGPDAI PRGCPSHCHC ELDGRMLLRV DCSDLGLSEL
PSNLSVFTSY LDLSMNNISQ LPASLLHRLC FLEELRLAGN ALTHIPKGAF TGLHSLKVLM
LQNNQLRQVP EEALQNLRSL QSLRLDANHI SYVPPSCFSG LHSLRHLWLD DNALTDVPVQ
AFRSLSALQA MTLALNKIHH IADYAFGNLS SLVVLHLHNN RIHSLGKKCF DGLHSLETLD
LNYNNLDEFP TAIKTLSNLK ELGFHSNNIR SIPERAFVGN PSLITIHFYD NPIQFVGVSA
FQHLPELRTL TLNGASHITE FPHLTGTATL ESLTLTGAKI SSLPQAVCDQ LPNLQVLDLS
YNLLEDLPSL SGCQKLQKID LRHNEIYEIK GSTFQQLFNL RSLNLAWNKI AIIHPNAFST
LPSLIKLDLS SNLLSSFPVT GLHGLTHLKL TGNRALQSLI PSANFPELKI IEMPSAYQCC
AFGGCENVYK ISNQWNKDDG NSVDDLHKKD AGLFQVQDER DLEDFLLDFE EDLKALHSVQ
CSPSPGPFKP CEHLFGSWLI RIGVWTTAVL ALSCNALVAL TVFRTPLYIS SIKLLIGVIA
VVDILMGVSS AVLAAVDAFT FGRFAQHGAW WEDGIGCQIV GFLSIFASES SIFLLTLAAL
ERGFSVKCSS KFEVKAPLFS LRAIVLLCVL LALTIATIPL LGGSKYNASP LCLPLPFGEP
STTGYMVALV LLNSLCFLIM TIAYTKLYCS LEKGELENLW DCSMVKHIAL LLFANCILYC
PVAFLSFSSL LNLTFISPDV IKFILLVIVP LPSCLNPLLY IVFNPHFKED MGSLGKHTRF
WMRSKHASLL SINSDDVEKR SCESTQALVS FTHASIAYDL PSTSGASPAY PMTESCHLSS
VAFVPCL
