EGFLA_HUMAN
ID EGFLA_HUMAN Reviewed; 1017 AA.
AC Q63HQ2; A8K6D7; Q5U643; Q6P3V1; Q8N124; Q8N197; Q8N7Y0; Q8N8N5; Q8NAL2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Pikachurin;
DE AltName: Full=Agrin-like protein;
DE AltName: Full=EGF-like, fibronectin type-III and laminin G-like domain-containing protein;
DE Flags: Precursor;
GN Name=EGFLAM; Synonyms=AGRINL, AGRNL, PIKA;
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 MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Placenta, Spleen, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5), AND VARIANT
RP MET-473.
RC TISSUE=Kidney, Lung, PNS, and Testis;
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 PROTEIN SEQUENCE OF 874-897, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
CC -!- FUNCTION: Involved in both the retinal photoreceptor ribbon synapse
CC formation and physiological functions of visual perception. Necessary
CC for proper bipolar dendritic tip apposition to the photoreceptor ribbon
CC synapse. Promotes matrix assembly and cell adhesiveness (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DAG1 alpha-dystroglycan. {ECO:0000250}.
CC -!- INTERACTION:
CC Q63HQ2; Q6PRD1: GPR179; NbExp=3; IntAct=EBI-21327031, EBI-20895185;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q4VBE4}. Synaptic cleft
CC {ECO:0000250|UniProtKB:Q4VBE4}. Presynaptic active zone
CC {ECO:0000250|UniProtKB:Q4VBE4}. Note=Detected in the synaptic cleft of
CC the ribbon synapse around the postsynaptic terminals of bipolar cells.
CC Colocalizes with BSN, CTBP2 and DAG1 in photoreceptor synaptic
CC terminals. {ECO:0000250|UniProtKB:Q4VBE4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q63HQ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63HQ2-2; Sequence=VSP_028481;
CC Name=3;
CC IsoId=Q63HQ2-3; Sequence=VSP_028476, VSP_028481;
CC Name=4;
CC IsoId=Q63HQ2-4; Sequence=VSP_028477, VSP_028478, VSP_028481;
CC Name=5;
CC IsoId=Q63HQ2-5; Sequence=VSP_028475;
CC -!- PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04800.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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; AK092479; BAC03900.1; -; mRNA.
DR EMBL; AK092994; BAC04013.1; -; mRNA.
DR EMBL; AK096474; BAC04800.1; ALT_SEQ; mRNA.
DR EMBL; AK097549; BAC05096.1; -; mRNA.
DR EMBL; AK291602; BAF84291.1; -; mRNA.
DR EMBL; BX647551; CAH56137.1; -; mRNA.
DR EMBL; AC010338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471119; EAW55968.1; -; Genomic_DNA.
DR EMBL; BC031251; AAH31251.1; -; mRNA.
DR EMBL; BC033177; AAH33177.1; -; mRNA.
DR EMBL; BC033188; AAH33188.1; -; mRNA.
DR EMBL; BC063822; AAH63822.1; -; mRNA.
DR CCDS; CCDS3924.1; -. [Q63HQ2-2]
DR CCDS; CCDS3925.1; -. [Q63HQ2-4]
DR CCDS; CCDS47199.1; -. [Q63HQ2-5]
DR CCDS; CCDS56363.1; -. [Q63HQ2-1]
DR RefSeq; NP_001192230.1; NM_001205301.1. [Q63HQ2-1]
DR RefSeq; NP_689616.2; NM_152403.3. [Q63HQ2-2]
DR RefSeq; NP_877950.1; NM_182798.2. [Q63HQ2-4]
DR RefSeq; NP_877953.1; NM_182801.2. [Q63HQ2-5]
DR AlphaFoldDB; Q63HQ2; -.
DR SMR; Q63HQ2; -.
DR BioGRID; 126364; 15.
DR IntAct; Q63HQ2; 6.
DR STRING; 9606.ENSP00000346964; -.
DR GlyGen; Q63HQ2; 3 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q63HQ2; -.
DR PhosphoSitePlus; Q63HQ2; -.
DR BioMuta; EGFLAM; -.
DR DMDM; 158705944; -.
DR jPOST; Q63HQ2; -.
DR MassIVE; Q63HQ2; -.
DR PaxDb; Q63HQ2; -.
DR PeptideAtlas; Q63HQ2; -.
DR PRIDE; Q63HQ2; -.
DR ProteomicsDB; 65890; -. [Q63HQ2-1]
DR ProteomicsDB; 65891; -. [Q63HQ2-2]
DR ProteomicsDB; 65892; -. [Q63HQ2-3]
DR ProteomicsDB; 65893; -. [Q63HQ2-4]
DR ProteomicsDB; 65894; -. [Q63HQ2-5]
DR Antibodypedia; 23033; 117 antibodies from 20 providers.
DR DNASU; 133584; -.
DR Ensembl; ENST00000322350.10; ENSP00000313084.5; ENSG00000164318.18. [Q63HQ2-2]
DR Ensembl; ENST00000336740.10; ENSP00000337607.6; ENSG00000164318.18. [Q63HQ2-4]
DR Ensembl; ENST00000354891.7; ENSP00000346964.3; ENSG00000164318.18. [Q63HQ2-1]
DR Ensembl; ENST00000397202.6; ENSP00000380385.2; ENSG00000164318.18. [Q63HQ2-3]
DR Ensembl; ENST00000397210.7; ENSP00000380393.3; ENSG00000164318.18. [Q63HQ2-5]
DR Ensembl; ENST00000506135.5; ENSP00000425579.1; ENSG00000164318.18. [Q63HQ2-5]
DR Ensembl; ENST00000514476.1; ENSP00000423228.1; ENSG00000164318.18. [Q63HQ2-5]
DR GeneID; 133584; -.
DR KEGG; hsa:133584; -.
DR MANE-Select; ENST00000322350.10; ENSP00000313084.5; NM_152403.4; NP_689616.2. [Q63HQ2-2]
DR UCSC; uc003jlb.3; human. [Q63HQ2-1]
DR CTD; 133584; -.
DR DisGeNET; 133584; -.
DR GeneCards; EGFLAM; -.
DR HGNC; HGNC:26810; EGFLAM.
DR HPA; ENSG00000164318; Tissue enhanced (tongue).
DR MIM; 617683; gene.
DR neXtProt; NX_Q63HQ2; -.
DR OpenTargets; ENSG00000164318; -.
DR PharmGKB; PA147358056; -.
DR VEuPathDB; HostDB:ENSG00000164318; -.
DR eggNOG; KOG0613; Eukaryota.
DR eggNOG; KOG3509; Eukaryota.
DR GeneTree; ENSGT00940000158504; -.
DR HOGENOM; CLU_013380_0_0_1; -.
DR InParanoid; Q63HQ2; -.
DR OMA; ISIQYPQ; -.
DR OrthoDB; 414294at2759; -.
DR PhylomeDB; Q63HQ2; -.
DR TreeFam; TF326548; -.
DR PathwayCommons; Q63HQ2; -.
DR SignaLink; Q63HQ2; -.
DR BioGRID-ORCS; 133584; 14 hits in 1069 CRISPR screens.
DR ChiTaRS; EGFLAM; human.
DR GeneWiki; Pikachurin; -.
DR GenomeRNAi; 133584; -.
DR Pharos; Q63HQ2; Tbio.
DR PRO; PR:Q63HQ2; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q63HQ2; protein.
DR Bgee; ENSG00000164318; Expressed in gastrocnemius and 121 other tissues.
DR ExpressionAtlas; Q63HQ2; baseline and differential.
DR Genevisible; Q63HQ2; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005614; C:interstitial matrix; IEA:Ensembl.
DR GO; GO:0048786; C:presynaptic active zone; IEA:UniProtKB-SubCell.
DR GO; GO:0043083; C:synaptic cleft; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IEA:Ensembl.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00054; Laminin_G_1; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 3.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Synapse.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1017
FT /note="Pikachurin"
FT /id="PRO_0000306803"
FT DOMAIN 37..136
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 144..239
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 343..381
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 386..564
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 565..602
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 609..788
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 784..820
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 835..1014
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 347..358
FT /evidence="ECO:0000250"
FT DISULFID 352..369
FT /evidence="ECO:0000250"
FT DISULFID 371..380
FT /evidence="ECO:0000250"
FT DISULFID 534..564
FT /evidence="ECO:0000250"
FT DISULFID 569..580
FT /evidence="ECO:0000250"
FT DISULFID 574..590
FT /evidence="ECO:0000250"
FT DISULFID 592..601
FT /evidence="ECO:0000250"
FT DISULFID 788..799
FT /evidence="ECO:0000250"
FT DISULFID 793..808
FT /evidence="ECO:0000250"
FT DISULFID 810..819
FT /evidence="ECO:0000250"
FT DISULFID 987..1014
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..865
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028475"
FT VAR_SEQ 1..634
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028476"
FT VAR_SEQ 1..234
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028477"
FT VAR_SEQ 235..238
FT /note="RTLC -> MHPG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028478"
FT VAR_SEQ 822..830
FT /note="ECGNYCLNT -> A (in isoform 2, isoform 3 and isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028481"
FT VARIANT 26
FT /note="R -> P (in dbSNP:rs12522205)"
FT /id="VAR_055718"
FT VARIANT 111
FT /note="R -> H (in dbSNP:rs2561111)"
FT /id="VAR_035302"
FT VARIANT 229
FT /note="W -> R (in dbSNP:rs1465567)"
FT /id="VAR_035303"
FT VARIANT 473
FT /note="T -> M (in dbSNP:rs16903965)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035304"
FT VARIANT 576
FT /note="H -> N (in dbSNP:rs6897179)"
FT /id="VAR_035305"
FT VARIANT 745
FT /note="V -> M (in dbSNP:rs2561818)"
FT /id="VAR_055719"
FT CONFLICT 546
FT /note="D -> G (in Ref. 2; CAH56137)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="E -> G (in Ref. 2; CAH56137)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="F -> L (in Ref. 1; BAF84291)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="F -> L (in Ref. 2; CAH56137)"
FT /evidence="ECO:0000305"
FT CONFLICT 1005
FT /note="A -> S (in Ref. 5; AAH33177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1017 AA; 111271 MW; AF251212507A57EB CRC64;
MDLIRGVLLR LLLLASSLGP GAVSLRAAIR KPGKVGPPLD IKLGALNCTA FSIQWKMPRH
PGSPILGYTV FYSEVGADKS LQEQLHSVPL SRDIPTTEEV IGDLKPGTEY RVSIAAYSQA
GKGRLSSPRH VTTLSQDSCL PPAAPQQPHV IVVSDSEVAL SWKPGASEGS APIQYYSVEF
IRPDFDKKWT SIHERIQMDS MVIKGLDPDT NYQFAVRAMN SHGPSPRSWP SDIIRTLCPE
EAGSGRYGPR YITDMGAGED DEGFEDDLDL DISFEEVKPL PATKGGNKKF LVESKKMSIS
NPKTISRLIP PTSASLPVTT VAPQPIPIQR KGKNGVAIMS RLFDMPCDET LCSADSFCVN
DYTWGGSRCQ CTLGKGGESC SEDIVIQYPQ FFGHSYVTFE PLKNSYQAFQ ITLEFRAEAE
DGLLLYCGEN EHGRGDFMSL AIIRRSLQFR FNCGTGVAII VSETKIKLGG WHTVMLYRDG
LNGLLQLNNG TPVTGQSQGQ YSKITFRTPL YLGGAPSAYW LVRATGTNRG FQGCVQSLAV
NGRRIDMRPW PLGKALSGAD VGECSSGICD EASCIHGGTC TAIKADSYIC LCPLGFKGRH
CEDAFTLTIP QFRESLRSYA ATPWPLEPQH YLSFMEFEIT FRPDSGDGVL LYSYDTGSKD
FLSINLAGGH VEFRFDCGSG TGVLRSEDPL TLGNWHELRV SRTAKNGILQ VDKQKIVEGM
AEGGFTQIKC NTDIFIGGVP NYDDVKKNSG VLKPFSGSIQ KIILNDRTIH VKHDFTSGVN
VENAAHPCVR APCAHGGSCR PRKEGYDCDC PLGFEGLHCQ KECGNYCLNT IIEAIEIPQF
IGRSYLTYDN PDILKRVSGS RSNVFMRFKT TAKDGLLLWR GDSPMRPNSD FISLGLRDGA
LVFSYNLGSG VASIMVNGSF NDGRWHRVKA VRDGQSGKIT VDDYGARTGK SPGMMRQLNI
NGALYVGGMK EIALHTNRQY MRGLVGCISH FTLSTDYHIS LVEDAVDGKN INTCGAK
