GON1_CAEEL
ID GON1_CAEEL Reviewed; 2150 AA.
AC Q19791; Q27524;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs gon-1 {ECO:0000305};
DE Short=ADAMTS gon-1 {ECO:0000305};
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q9P2N4};
DE AltName: Full=Abnormal gonad development protein 1 {ECO:0000312|WormBase:F25H8.3a};
DE Flags: Precursor;
GN Name=gon-1 {ECO:0000312|WormBase:F25H8.3a};
GN ORFNames=F25H8.3 {ECO:0000312|WormBase:F25H8.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=10588887; DOI=10.1006/dbio.1999.9491;
RA Blelloch R., Anna-Arriola S.S., Gao D., Li Y., Hodgkin J., Kimble J.;
RT "The gon-1 gene is required for gonadal morphogenesis in Caenorhabditis
RT elegans.";
RL Dev. Biol. 216:382-393(1999).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF GLU-425.
RX PubMed=10376599; DOI=10.1038/21196;
RA Blelloch R., Kimble J.;
RT "Control of organ shape by a secreted metalloprotease in the nematode
RT Caenorhabditis elegans.";
RL Nature 399:586-590(1999).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1432, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [5]
RP FUNCTION.
RX PubMed=15556862; DOI=10.1016/j.cub.2004.11.006;
RA Hesselson D., Newman C., Kim K.W., Kimble J.;
RT "GON-1 and fibulin have antagonistic roles in control of organ shape.";
RL Curr. Biol. 14:2005-2010(2004).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1432, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [7]
RP FUNCTION IN TRANSPORT, SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22419820; DOI=10.1091/mbc.e11-10-0857;
RA Yoshina S., Sakaki K., Yonezumi-Hayashi A., Gengyo-Ando K., Inoue H.,
RA Iino Y., Mitani S.;
RT "Identification of a novel ADAMTS9/GON-1 function for protein transport
RT from the ER to the Golgi.";
RL Mol. Biol. Cell 23:1728-1741(2012).
RN [8]
RP FUNCTION.
RX PubMed=25080592; DOI=10.1523/jneurosci.5128-13.2014;
RA Qin J., Liang J., Ding M.;
RT "Perlecan antagonizes collagen IV and ADAMTS9/GON-1 in restricting the
RT growth of presynaptic boutons.";
RL J. Neurosci. 34:10311-10324(2014).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25232106; DOI=10.1523/jneurosci.1183-14.2014;
RA Kurshan P.T., Phan A.Q., Wang G.J., Crane M.M., Lu H., Shen K.;
RT "Regulation of synaptic extracellular matrix composition is critical for
RT proper synapse morphology.";
RL J. Neurosci. 34:12678-12689(2014).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DOMAIN.
RX PubMed=26218657; DOI=10.1371/journal.pone.0133966;
RA Yoshina S., Mitani S.;
RT "Loss of C. elegans GON-1, an ADAMTS9 Homolog, decreases secretion
RT resulting in altered lifespan and dauer formation.";
RL PLoS ONE 10:E0133966-E0133966(2015).
CC -!- FUNCTION: Secreted metalloprotease required for distal tip cell (DTC)
CC migration along the body wall basement membranes, a key step that
CC promotes gonad morphogenesis (PubMed:10588887, PubMed:10376599,
CC PubMed:15556862). Probably acts by remodeling the basement membrane
CC during cell migration (PubMed:10376599). Required to restrict
CC presynaptic growth at the neuromuscular junctions (NMJ) in late larval
CC stage and in adult motor neurons, probably by controlling collagen IV
CC emb-9 degradation, a component of the synapse basement membrane
CC (PubMed:25080592, PubMed:25232106). Also involved in the organization
CC of adult muscle morphology (PubMed:25232106). Has a protease-
CC independent function in promoting the transport from the endoplasmic
CC reticulum to the Golgi apparatus of a variety of secretory cargos
CC (PubMed:22419820, PubMed:26218657). Required for the secretion of
CC insulin-like peptide ins-7, daf-28 and ins-18 and TGF beta-like protein
CC daf-7 (PubMed:26218657). In peripheral tissues, negatively regulates
CC insulin-mediated daf-16 translocation and thereby negatively regulates
CC lifespan and dauer formation (PubMed:26218657).
CC {ECO:0000269|PubMed:10376599, ECO:0000269|PubMed:10588887,
CC ECO:0000269|PubMed:15556862, ECO:0000269|PubMed:22419820,
CC ECO:0000269|PubMed:25080592, ECO:0000269|PubMed:25232106,
CC ECO:0000269|PubMed:26218657}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9UHI8};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UHI8};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:10376599}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:22419820}. Golgi apparatus
CC {ECO:0000269|PubMed:22419820}.
CC -!- TISSUE SPECIFICITY: Expressed by the gonadal distal tip cells (DTCs)
CC (PubMed:10376599). Expressed in muscles, including body wall, vulval
CC and anal depressor muscles (PubMed:10376599, PubMed:25232106,
CC PubMed:26218657). Expressed in motor neurons and in ASI and ASJ neurons
CC (PubMed:26218657). {ECO:0000269|PubMed:10376599,
CC ECO:0000269|PubMed:25232106, ECO:0000269|PubMed:26218657}.
CC -!- DEVELOPMENTAL STAGE: Expressed in some cells at the embryonic stage
CC (260-280 min after the first cleavage) (PubMed:26218657). In
CC hermaphrodites, expression is first detected in gonads in L2 larvae and
CC is limited to the distal tip cells (DTCs), then continues in DTCs
CC throughout L4 larval stage and becomes faint or absent in adults
CC (PubMed:10376599). Also expressed in muscle cells throughout
CC development (PubMed:10376599). At the larval stages, expressed in some
CC head neurons, intestine and excretory cells (PubMed:26218657).
CC {ECO:0000269|PubMed:10376599, ECO:0000269|PubMed:26218657}.
CC -!- DOMAIN: The GON domain mediates protease-independent function in ER to
CC Golgi transport. {ECO:0000269|PubMed:22419820,
CC ECO:0000269|PubMed:26218657}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in distal tip cells
CC results in deformation of ER structure and inhibition of protein
CC secretion which are rescued upon GON-domain expression.
CC {ECO:0000269|PubMed:22419820}.
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DR EMBL; Z69360; CAA93287.2; -; Genomic_DNA.
DR EMBL; Z69361; CAA93287.2; JOINED; Genomic_DNA.
DR PIR; T21371; T21371.
DR RefSeq; NP_001255447.1; NM_001268518.1.
DR AlphaFoldDB; Q19791; -.
DR SMR; Q19791; -.
DR STRING; 6239.F25H8.3b; -.
DR MEROPS; M12.135; -.
DR iPTMnet; Q19791; -.
DR EPD; Q19791; -.
DR PaxDb; Q19791; -.
DR EnsemblMetazoa; F25H8.3a.1; F25H8.3a.1; WBGene00001650.
DR EnsemblMetazoa; F25H8.3a.2; F25H8.3a.2; WBGene00001650.
DR UCSC; F25H8.3; c. elegans.
DR WormBase; F25H8.3a; CE42668; WBGene00001650; gon-1.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000167121; -.
DR HOGENOM; CLU_000660_0_1_1; -.
DR InParanoid; Q19791; -.
DR PhylomeDB; Q19791; -.
DR Reactome; R-CEL-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-CEL-5173214; O-glycosylation of TSR domain-containing proteins.
DR PRO; PR:Q19791; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001650; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q19791; baseline and differential.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; IMP:WormBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016477; P:cell migration; IMP:WormBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:WormBase.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0008406; P:gonad development; IMP:WormBase.
DR GO; GO:0048644; P:muscle organ morphogenesis; IMP:UniProtKB.
DR GO; GO:1905607; P:negative regulation of presynapse assembly; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 16.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR012314; Pept_M12B_GON-ADAMTSs.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF08685; GON; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 18.
DR SUPFAM; SSF82895; SSF82895; 16.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS51046; GON; 1.
DR PROSITE; PS50092; TSP1; 15.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Developmental protein; Disulfide bond;
KW Endoplasmic reticulum; ER-Golgi transport; Extracellular matrix;
KW Glycoprotein; Golgi apparatus; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Protein transport; Reference proteome; Repeat; Secreted; Signal;
KW Transport; Zinc; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..273
FT /evidence="ECO:0000250|UniProtKB:Q9P2N4"
FT /id="PRO_0000440960"
FT CHAIN 274..2150
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs gon-1"
FT /id="PRO_0000250561"
FT DOMAIN 280..493
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 503..587
FT /note="Disintegrin"
FT DOMAIN 588..643
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 943..1003
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1004..1057
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1060..1115
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1116..1165
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1168..1227
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1228..1277
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1280..1339
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1352..1409
FT /note="TSP type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1410..1469
FT /note="TSP type-1 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1474..1524
FT /note="TSP type-1 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1527..1585
FT /note="TSP type-1 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1621..1675
FT /note="TSP type-1 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1678..1736
FT /note="TSP type-1 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1737..1793
FT /note="TSP type-1 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1794..1866
FT /note="TSP type-1 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1867..1924
FT /note="TSP type-1 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1924..2123
FT /note="GON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00383"
FT REGION 1590..1614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 1528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1654
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1960
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1997
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 402..488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 440..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 600..637
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 604..642
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 615..627
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1679..1718
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1690..1730
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1690..1694
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1694..1735
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1705..1718
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1730..1735
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT MUTAGEN 425
FT /note="E->A: Loss of function; abolishes DTCs migration or
FT gonad arm extension."
FT /evidence="ECO:0000269|PubMed:10376599"
SQ SEQUENCE 2150 AA; 242582 MW; B18051C284C29116 CRC64;
MRSIGGSFHL LQPVVAALIL LVVCLVYALQ SGSGTISEFS SDVLFSRAKY SGVPVHHSRW
RQDAGIHVID SHHIVRRDSY GRRGKRDVTS TDRRRRLQGV ARDCGHACHL RLRSDDAVYI
VHLHRWNQIP DSHNKSVPHF SNSNFAPMVL YLDSEEEVRG GMSRTDPDCI YRAHVKGVHQ
HSIVNLCDSE DGLYGMLALP SGIHTVEPII SGNGTEHDGA SRHRQHLVRK FDPMHFKSFD
HLNSTSVNET ETTVATWQDQ WEDVIERKAR SRRAANSWDH YVEVLVVADT KMYEYHGRSL
EDYVLTLFST VASIYRHQSL RASINVVVVK LIVLKTENAG PRITQNAQQT LQDFCRWQQY
YNDPDDSSVQ HHDVAILLTR KDICRSQGKC DTLGLAELGT MCDMQKSCAI IEDNGLSAAF
TIAHELGHVF SIPHDDERKC STYMPVNKNN FHIMAPTLEY NTHPWSWSPC SAGMLERFLE
NNRGQTQCLF DQPVERRYYE DVFVRDEPGK KYDAHQQCKF VFGPASELCP YMPTCRRLWC
ATFYGSQMGC RTQHMPWADG TPCDESRSMF CHHGACVRLA PESLTKIDGQ WGDWRSWGEC
SRTCGGGVQK GLRDCDSPKP RNGGKYCVGQ RERYRSCNTQ ECPWDTQPYR EVQCSEFNNK
DIGIQGVAST NTHWVPKYAN VAPNERCKLY CRLSGSAAFY LLRDKVVDGT PCDRNGDDIC
VAGACMPAGC DHQLHSTLRR DKCGVCGGDD SSCKVVKGTF NEQGTFGYNE VMKIPAGSAN
IDIRQKGYNN MKEDDNYLSL RAANGEFLLN GHFQVSLARQ QIAFQDTVLE YSGSDAIIER
INGTGPIRSD IYVHVLSVGS HPPDISYEYM TAAVPNAVIR PISSALYLWR VTDTWTECDR
ACRGQQSQKL MCLDMSTHRQ SHDRNCQNVL KPKQATRMCN IDCSTRWITE DVSSCSAKCG
SGQKRQRVSC VKMEGDRQTP ASEHLCDRNS KPSDIASCYI DCSGRKWNYG EWTSCSETCG
SNGKMHRKSY CVDDSNRRVD ESLCGREQKE ATERECNRIP CPRWVYGHWS ECSRSCDGGV
KMRHAQCLDA ADRETHTSRC GPAQTQEHCN EHACTWWQFG VWSDCSAKCG DGVQYRDANC
TDRHRSVLPE HRCLKMEKII TKPCHRESCP KYKLGEWSQC SVSCEDGWSS RRVSCVSGNG
TEVDMSLCGT ASDRPASHQT CNLGTCPFWR NTDWSACSVS CGIGHRERTT ECIYREQSVD
ASFCGDTKMP ETSQTCHLLP CTSWKPSHWS PCSVTCGSGI QTRSVSCTRG SEGTIVDEYF
CDRNTRPRLK KTCEKDTCDG PRVLQKLQAD VPPIRWATGP WTACSATCGN GTQRRLLKCR
DHVRDLPDEY CNHLDKEVST RNCRLRDCSY WKMAEWEECP ATCGTHVQQS RNVTCVSAED
GGRTILKDVD CDVQKRPTSA RNCRLEPCPK GEEHIGSWII GDWSKCSASC GGGWRRRSVS
CTSSSCDETR KPKMFDKCNE ELCPPLTNNS WQISPWTHCS VSCGGGVQRR KIWCEDVLSG
RKQDDIECSE IKPREQRDCE MPPCRSHYHN KTSSASMTSL SSSNSNTTSS ASASSLPILP
PVVSWQTSAW SACSAKCGRG TKRRVVECVN PSLNVTVAST ECDQTKKPVE EVRCRTKHCP
RWKTTTWSSC SVTCGRGIRR REVQCYRGRK NLVSDSECNP KTKLNSVANC FPVACPAYRW
NVTPWSKCKD ECARGQKQTR RVHCISTSGK RAAPRMCELA RAPTSIRECD TSNCPYEWVP
GDWQTCSKSC GEGVQTREVR CRRKINFNST IPIIFMLEDE PAVPKEKCEL FPKPNESQTC
ELNPCDSEFK WSFGPWGECS KNCGQGIRRR RVKCVANDGR RVERVKCTTK KPRRTQYCFE
RNCLPSTCQE LKSQNVKAKD GNYTILLDGF TIEIYCHRMN STIPKAYLNV NPRTNFAEVY
GKKLIYPHTC PFNGDRNDSC HCSEDGDASA GLTRFNKVRI DLLNRKFHLA DYTFAKREYG
VHVPYGTAGD CYSMKDCPQG IFSIDLKSAG LKLVDDLNWE DQGHRTSSRI DRFYNNAKVI
GHCGGFCGKC SPERYKGLIF EVNTKLLNHV KNGGHIDDEL DDDGFSGDMD
