LRC47_HUMAN
ID LRC47_HUMAN Reviewed; 583 AA.
AC Q8N1G4; Q9ULN5;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Leucine-rich repeat-containing protein 47;
GN Name=LRRC47; Synonyms=KIAA1185;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [3]
RP PROTEIN SEQUENCE OF 2-18; 23-34; 65-83; 85-102; 371-381 AND 494-502,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-583.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-509 AND SER-520, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431 AND SER-520, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-518 AND SER-520, 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 [14]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-193.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- INTERACTION:
CC Q8N1G4; PRO_0000038596 [P04591]: gag; Xeno; NbExp=2; IntAct=EBI-2509921, EBI-6179727;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL365330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031301; AAH31301.1; -; mRNA.
DR EMBL; AB033011; BAA86499.1; -; mRNA.
DR CCDS; CCDS51.1; -.
DR RefSeq; NP_065761.1; NM_020710.2.
DR PDB; 6ZXD; EM; 3.20 A; k=1-583.
DR PDB; 6ZXE; EM; 3.00 A; k=1-583.
DR PDB; 6ZXF; EM; 3.70 A; k=1-583.
DR PDB; 6ZXG; EM; 2.60 A; k=1-583.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR AlphaFoldDB; Q8N1G4; -.
DR SMR; Q8N1G4; -.
DR BioGRID; 121540; 84.
DR IntAct; Q8N1G4; 26.
DR MINT; Q8N1G4; -.
DR STRING; 9606.ENSP00000367498; -.
DR GlyGen; Q8N1G4; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8N1G4; -.
DR PhosphoSitePlus; Q8N1G4; -.
DR SwissPalm; Q8N1G4; -.
DR BioMuta; LRRC47; -.
DR DMDM; 74750895; -.
DR EPD; Q8N1G4; -.
DR jPOST; Q8N1G4; -.
DR MassIVE; Q8N1G4; -.
DR MaxQB; Q8N1G4; -.
DR PaxDb; Q8N1G4; -.
DR PeptideAtlas; Q8N1G4; -.
DR PRIDE; Q8N1G4; -.
DR ProteomicsDB; 71601; -.
DR Antibodypedia; 1623; 32 antibodies from 13 providers.
DR DNASU; 57470; -.
DR Ensembl; ENST00000378251.3; ENSP00000367498.1; ENSG00000130764.10.
DR GeneID; 57470; -.
DR KEGG; hsa:57470; -.
DR MANE-Select; ENST00000378251.3; ENSP00000367498.1; NM_020710.3; NP_065761.1.
DR UCSC; uc001akx.2; human.
DR CTD; 57470; -.
DR DisGeNET; 57470; -.
DR GeneCards; LRRC47; -.
DR HGNC; HGNC:29207; LRRC47.
DR HPA; ENSG00000130764; Tissue enhanced (skeletal).
DR MIM; 619154; gene.
DR neXtProt; NX_Q8N1G4; -.
DR OpenTargets; ENSG00000130764; -.
DR PharmGKB; PA142671507; -.
DR VEuPathDB; HostDB:ENSG00000130764; -.
DR eggNOG; KOG2472; Eukaryota.
DR GeneTree; ENSGT00530000063489; -.
DR HOGENOM; CLU_034522_0_0_1; -.
DR InParanoid; Q8N1G4; -.
DR OMA; YDVKPPT; -.
DR OrthoDB; 1021451at2759; -.
DR PhylomeDB; Q8N1G4; -.
DR TreeFam; TF315742; -.
DR PathwayCommons; Q8N1G4; -.
DR SignaLink; Q8N1G4; -.
DR BioGRID-ORCS; 57470; 17 hits in 1080 CRISPR screens.
DR ChiTaRS; LRRC47; human.
DR GenomeRNAi; 57470; -.
DR Pharos; Q8N1G4; Tdark.
DR PRO; PR:Q8N1G4; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N1G4; protein.
DR Bgee; ENSG00000130764; Expressed in middle temporal gyrus and 210 other tissues.
DR ExpressionAtlas; Q8N1G4; baseline and differential.
DR Genevisible; Q8N1G4; HS.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 3.50.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR005146; B3/B4_tRNA-bd.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR045060; Phe-tRNA-ligase_IIc_bsu.
DR InterPro; IPR020825; Phe-tRNA_synthase-like_B3/B4.
DR PANTHER; PTHR10947; PTHR10947; 1.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Direct protein sequencing;
KW Leucine-rich repeat; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22223895"
FT CHAIN 2..583
FT /note="Leucine-rich repeat-containing protein 47"
FT /id="PRO_0000223926"
FT REPEAT 76..95
FT /note="LRR 1"
FT REPEAT 100..121
FT /note="LRR 2"
FT REPEAT 130..152
FT /note="LRR 3"
FT REPEAT 154..175
FT /note="LRR 4"
FT REPEAT 180..202
FT /note="LRR 5"
FT REPEAT 203..225
FT /note="LRR 6"
FT REPEAT 226..246
FT /note="LRR 7"
FT REGION 260..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 402..437
FT /evidence="ECO:0000255"
FT COMPBIAS 269..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22223895"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 509
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT VARIANT 193
FT /note="E -> D (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035471"
FT VARIANT 545
FT /note="P -> L (in dbSNP:rs11547614)"
FT /id="VAR_051118"
FT VARIANT 581
FT /note="V -> I (in dbSNP:rs11547615)"
FT /id="VAR_051119"
FT HELIX 13..18
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:6ZXG"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6ZXG"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:6ZXD"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 251..259
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 348..366
FT /evidence="ECO:0007829|PDB:6ZXG"
FT TURN 367..371
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:6ZXG"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:6ZXG"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 411..420
FT /evidence="ECO:0007829|PDB:6ZXG"
FT TURN 425..428
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 447..452
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:6ZXE"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 479..484
FT /evidence="ECO:0007829|PDB:6ZXG"
FT HELIX 491..503
FT /evidence="ECO:0007829|PDB:6ZXG"
SQ SEQUENCE 583 AA; 63473 MW; BCCFAE89BCD46031 CRC64;
MAAAAVSESW PELELAERER RRELLLTGPG LEERVRAAGG QLPPRLFTLP LLHYLEVSGC
GSLRAPGPGL AQGLPQLHSL VLRRNALGPG LSPELGPLPA LRVLDLSGNA LEALPPGQGL
GPAEPPGLPQ LQSLNLSGNR LRELPADLAR CAPRLQSLNL TGNCLDSFPA ELFRPGALPL
LSELAAADNC LRELSPDIAH LASLKTLDLS NNQLSEIPAE LADCPKLKEI NFRGNKLRDK
RLEKMVSGCQ TRSILEYLRV GGRGGGKGKG RAEGSEKEES RRKRRERKQR REGGDGEEQD
VGDAGRLLLR VLHVSENPVP LTVRVSPEVR DVRPYIVGAV VRGMDLQPGN ALKRFLTSQT
KLHEDLCEKR TAATLATHEL RAVKGPLLYC ARPPQDLKIV PLGRKEAKAK ELVRQLQLEA
EEQRKQKKRQ SVSGLHRYLH LLDGNENYPC LVDADGDVIS FPPITNSEKT KVKKTTSDLF
LEVTSATSLQ ICKDVMDALI LKMAEMKKYT LENKEEGSLS DTEADAVSGQ LPDPTTNPSA
GKDGPSLLVV EQVRVVDLEG SLKVVYPSKA DLATAPPHVT VVR
