ID EGFLA_MOUSE Reviewed; 1017 AA.
AC Q4VBE4; B2RWU6; B6JU28; Q80WX4; Q8BGP3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 136.
DE RecName: Full=Pikachurin {ECO:0000303|PubMed:18641643};
DE AltName: Full=EGF-like, fibronectin type-III and laminin G-like domain-containing protein;
DE AltName: Full=Nectican;
DE Flags: Precursor;
GN Name=Egflam;
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), FUNCTION, INTERACTION WITH DAG1
RP ALPHA-DYSTROGLYCAN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=18641643; DOI=10.1038/nn.2160;
RA Sato S., Omori Y., Katoh K., Kondo M., Kanagawa M., Miyata K., Funabiki K.,
RA Koyasu T., Kajimura N., Miyoshi T., Sawai H., Kobayashi K., Tani A.,
RA Toda T., Usukura J., Tano Y., Fujikado T., Furukawa T.;
RT "Pikachurin, a dystroglycan ligand, is essential for photoreceptor ribbon
RT synapse formation.";
RL Nat. Neurosci. 11:923-931(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Forelimb, Skin, Testis, 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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Eye, and Olfactory epithelium;
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 FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18757743; DOI=10.1073/pnas.0803640105;
RA Manabe R., Tsutsui K., Yamada T., Kimura M., Nakano I., Shimono C.,
RA Sanzen N., Furutani Y., Fukuda T., Oguri Y., Shimamoto K., Kiyozumi D.,
RA Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S., Kawai J., Sugiura N.,
RA Kimata K., Hayashizaki Y., Sekiguchi K.;
RT "Transcriptome-based systematic identification of extracellular matrix
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12849-12854(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP GPR158 AND GPR179.
RX PubMed=30282023; DOI=10.1016/j.celrep.2018.08.068;
RA Orlandi C., Omori Y., Wang Y., Cao Y., Ueno A., Roux M.J., Condomitti G.,
RA de Wit J., Kanagawa M., Furukawa T., Martemyanov K.A.;
RT "Transsynaptic binding of orphan receptor GPR179 to Dystroglycan-pikachurin
RT complex is essential for the synaptic organization of photoreceptors.";
RL Cell Rep. 25:130-145(2018).
CC -!- FUNCTION: Involved in both the retinal photoreceptor ribbon synapse
CC formation and physiological functions of visual perception
CC (PubMed:18641643, PubMed:18757743, PubMed:30282023). Plays a key role
CC in the synaptic organization of photoreceptors by mediating
CC transsynaptic interaction between alpha-dystroglycan and GPR179 on the
CC postsynaptic membrane (PubMed:30282023). Necessary for proper bipolar
CC dendritic tip apposition to the photoreceptor ribbon synapse
CC (PubMed:18641643, PubMed:18757743, PubMed:30282023). Promotes matrix
CC assembly and cell adhesiveness (PubMed:18641643, PubMed:18757743).
CC {ECO:0000269|PubMed:18641643, ECO:0000269|PubMed:18757743,
CC ECO:0000269|PubMed:30282023}.
CC -!- SUBUNIT: Interacts with DAG1 alpha-dystroglycan (PubMed:18641643).
CC Interacts with GPR158 and GPR179; transsynaptic interaction is required
CC for synaptic organization of photoreceptor cells (PubMed:30282023).
CC {ECO:0000269|PubMed:18641643, ECO:0000269|PubMed:30282023}.
CC -!- INTERACTION:
CC Q4VBE4; PRO_0000021067 [Q62165]: Dag1; NbExp=2; IntAct=EBI-2025048, EBI-2025154;
CC Q4VBE4; Q6PRD1: GPR179; Xeno; NbExp=4; IntAct=EBI-2025048, EBI-20895185;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:18757743}. Synaptic cleft
CC {ECO:0000269|PubMed:18641643, ECO:0000269|PubMed:30282023}. Presynaptic
CC active zone {ECO:0000269|PubMed:18641643}. Note=Detected in the
CC synaptic cleft of the ribbon synapse around the postsynaptic terminals
CC of bipolar cells (PubMed:18641643). Colocalizes with BSN, CTBP2 and
CC DAG1 in photoreceptor synaptic terminals (PubMed:18641643).
CC {ECO:0000269|PubMed:18641643}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4VBE4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4VBE4-2; Sequence=VSP_028482;
CC -!- TISSUE SPECIFICITY: Expressed in the outer plexiform layer (first
CC synaptic region) but not in the inner plexiform layer (second synaptic
CC region) of the retina (at protein level). Strongly expressed in the
CC photoreceptor layer of the retina. Moderately expressed in pineal gland
CC and brain. Weakly expressed in lung and ovary.
CC {ECO:0000269|PubMed:18641643}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the apical side of the neuroblastic
CC layer (NBL) of the retina at 14.5 dpc and 17.5 dpc. At 16.5 dpc,
CC present in rib cartilage and hair follicle (at protein level).
CC {ECO:0000269|PubMed:18641643, ECO:0000269|PubMed:18757743}.
CC -!- PTM: O-glycosylated; contains chondroitin sulfate and heparan sulfate.
CC {ECO:0000269|PubMed:18757743}.
CC -!- DISRUPTION PHENOTYPE: No morphological abnormalities (PubMed:18641643).
CC Knockout mice are viable and fertile (PubMed:18641643). However, the
CC terminal of bipolar cells do not appose to the synapse terminals in the
CC rod photoreceptor ribbon synapses (PubMed:18641643). The signal
CC transmission from the rod photoreceptor to the rod bipolar cells is
CC less sensitive and is delayed compared to the wild type mouse
CC (PubMed:18641643). The signal transmission from cone photoreceptors to
CC the cone bipolar cells is also impaired (PubMed:18641643). These mice
CC show reduced visual function (PubMed:18641643). Impaired stability and
CC postsynaptic targeting of GPR179 (PubMed:30282023).
CC {ECO:0000269|PubMed:18641643, ECO:0000269|PubMed:30282023}.
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DR EMBL; DQ223720; ABB48431.1; -; mRNA.
DR EMBL; AK031136; BAC27271.1; -; mRNA.
DR EMBL; AK033332; BAC28235.1; -; mRNA.
DR EMBL; AK037223; BAC29762.1; -; mRNA.
DR EMBL; AK041546; BAC30982.1; -; mRNA.
DR EMBL; AC105969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051455; AAH51455.1; -; mRNA.
DR EMBL; BC095994; AAH95994.1; -; mRNA.
DR EMBL; BC150710; AAI50711.1; -; mRNA.
DR CCDS; CCDS27370.1; -. [Q4VBE4-2]
DR CCDS; CCDS79359.1; -. [Q4VBE4-1]
DR RefSeq; NP_001276425.1; NM_001289496.1. [Q4VBE4-1]
DR RefSeq; NP_848863.1; NM_178748.6. [Q4VBE4-2]
DR RefSeq; XP_017172117.1; XM_017316628.1.
DR AlphaFoldDB; Q4VBE4; -.
DR SMR; Q4VBE4; -.
DR BioGRID; 234554; 1.
DR IntAct; Q4VBE4; 6.
DR STRING; 10090.ENSMUSP00000094238; -.
DR GlyCosmos; Q4VBE4; 1 site, No reported glycans.
DR GlyGen; Q4VBE4; 1 site.
DR PhosphoSitePlus; Q4VBE4; -.
DR MaxQB; Q4VBE4; -.
DR PaxDb; 10090-ENSMUSP00000055599; -.
DR ProteomicsDB; 277561; -. [Q4VBE4-1]
DR ProteomicsDB; 277562; -. [Q4VBE4-2]
DR Antibodypedia; 23033; 125 antibodies from 20 providers.
DR DNASU; 268780; -.
DR Ensembl; ENSMUST00000058593.10; ENSMUSP00000055599.4; ENSMUSG00000042961.14. [Q4VBE4-2]
DR Ensembl; ENSMUST00000096494.5; ENSMUSP00000094238.5; ENSMUSG00000042961.14. [Q4VBE4-1]
DR GeneID; 268780; -.
DR KEGG; mmu:268780; -.
DR UCSC; uc007vea.2; mouse. [Q4VBE4-2]
DR UCSC; uc007veb.2; mouse. [Q4VBE4-1]
DR AGR; MGI:2146149; -.
DR CTD; 133584; -.
DR MGI; MGI:2146149; Egflam.
DR VEuPathDB; HostDB:ENSMUSG00000042961; -.
DR eggNOG; KOG0613; Eukaryota.
DR eggNOG; KOG3509; Eukaryota.
DR GeneTree; ENSGT00940000158504; -.
DR HOGENOM; CLU_013380_0_0_1; -.
DR InParanoid; Q4VBE4; -.
DR OMA; CGEGTIE; -.
DR OrthoDB; 2878505at2759; -.
DR PhylomeDB; Q4VBE4; -.
DR TreeFam; TF326548; -.
DR BioGRID-ORCS; 268780; 3 hits in 78 CRISPR screens.
DR ChiTaRS; Egflam; mouse.
DR PRO; PR:Q4VBE4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q4VBE4; Protein.
DR Bgee; ENSMUSG00000042961; Expressed in retinal neural layer and 157 other cell types or tissues.
DR ExpressionAtlas; Q4VBE4; baseline and differential.
DR Genevisible; Q4VBE4; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005614; C:interstitial matrix; IDA:MGI.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00110; LamG; 3.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.10.25.10; Laminin; 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 PANTHER; PTHR15036:SF88; PIKACHURIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00282; LamG; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
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; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Heparan sulfate; Proteoglycan;
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_0000306804"
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 822..830
FT /note="ECGNHCLNT -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_028482"
FT CONFLICT 45
FT /note="A -> T (in Ref. 4; AAI50711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1017 AA; 110735 MW; F8A21D89B251D455 CRC64;
MDLISTFSLH FLLLACSLPP GAVSLRTALR KSGKVGPPLD IKLGALNCTA FSIQWKTPKR
SGSSIIGYTV FYSEVGSDKS LRERSHNVPV GQDTLITEEV IGDLKPGTEY QVSVAAYSQT
GKGRLSFPRH VTTLSQDSCL PPAAPQQPHV LVVSDSEVAL SWRPGENEGS APIQSYSVEF
IRPDFDKSWT IIQERLQMDS MVIKGLDPDT NYQFAVKAMN AHGFSPRSWP SNTVRTLGPG
EAGSGHYGPG YITNPGVSED DDGSEDELDL DVSFEEVKPL PATKVGNKKF SVESKKTSVS
NSVMGSRLAQ PTSASLHETT VAIPPTPAQR KGKNSVAMMS RLFDMSCDET LCSADSFCVN
DYAWGGSRCH CNLGKGGEAC SEDIFIQYPQ FFGHSYVTFE PLKNSYQAFQ VTLEFRAEAE
DGLLLYCGES EHGRGDFMSL ALIRRSLHFR FNCGTGIAII ISETKIKLGA WHTVTLYRDG
LNGMLQLNNG TPVTGQSQGQ YSKITFRTPL YLGGAPSAYW LVRATGTNRG FQGCVQSLSV
NGKKIDMRPW PLGKALNGAD VGECSSGICD EASCIHGGTC AAIKADSYIC LCPLGFRGRH
CEDAFALTIP QFRESLRSYA ATPWPLEPQH YLSFTEFEIT FRPDSGDGVL LYSYDTGSKD
FLSINMAAGH VEFRFDCGSG TGVLRSEAPL TLGQWHDLRV SRTAKNGILQ VDKQKVVEGM
AEGGFTQIKC NTDIFIGGVP NYDDVKKNSG ILHPFSGSIQ KIILNDRTIH VKHDFTSGVN
VENAAHPCVG APCAHGGSCR PRKEGYECDC PLGFEGLNCQ KECGNHCLNT IIEAIEIPQF
IGRSYLTYDN PNILKRVSGS RSNAFMRFKT TAKDGLLLWR GDSPMRPNSD FISLGLRDGA
LIFSYNLGSG VASIMVNGSF SDGRWHRVKA VRDGQSGKIT VDDYGARTGK SPGLMRQLNI
NGALYVGGMK EIALHTNRQY LRGLVGCISH FTLSTDYHIS LVEDAVDGKN INTCGAK
//
