FUR2_DROME
ID FUR2_DROME Reviewed; 1679 AA.
AC P30432; A4V4M0; A4V4M2; Q24301; Q5BI10; Q8SZS2;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Furin-like protease 2;
DE Short=Furin-2;
DE EC=3.4.21.75;
DE Flags: Precursor;
GN Name=Fur2; ORFNames=CG18734;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
RC STRAIN=Iso-1, Oregon-R, and Tuebingen; TISSUE=Embryo;
RX PubMed=1512259; DOI=10.1016/s0021-9258(18)41914-x;
RA Roebroek A.J.M., Creemers J.W.M., Pauli I.G.L., Kurzik-Dumke U.,
RA Rentrop M., Gateff E.A.F., Leunissen J.A.M., van de Ven W.J.M.;
RT "Cloning and functional expression of Dfurin2, a subtilisin-like proprotein
RT processing enzyme of Drosophila melanogaster with multiple repeats of a
RT cysteine motif.";
RL J. Biol. Chem. 267:17208-17215(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Iso-1;
RX PubMed=7880443; DOI=10.1089/dna.1995.14.223;
RA Roebroek A.J.M., Ayoubi T.A.Y., Creemers J.W.M., Pauli I.G.L.,
RA van de Ven W.J.M.;
RT "The Dfur2 gene of Drosophila melanogaster: genetic organization,
RT expression during embryogenesis, and pro-protein processing activity of its
RT translational product Dfurin2.";
RL DNA Cell Biol. 14:223-234(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 305-1679 (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Furin is likely to represent the ubiquitous endoprotease
CC activity within constitutive secretory pathways and capable of cleavage
CC at the RX(K/R)R consensus motif. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of mature proteins from their proproteins by cleavage
CC of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and
CC Yaa is Arg or Lys. Releases albumin, complement component C3 and von
CC Willebrand factor from their respective precursors.; EC=3.4.21.75;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=D; Synonyms=E, F, G;
CC IsoId=P30432-1; Sequence=Displayed;
CC Name=A; Synonyms=B, C;
CC IsoId=P30432-2; Sequence=VSP_009365;
CC -!- TISSUE SPECIFICITY: Transient expression in a subset of central nervous
CC system neurons during embryonic stages 12-13. Expression in developing
CC tracheal tree from stage 13 to end of embryonic development.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48024.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAX33562.1; Type=Miscellaneous discrepancy; Note=Intron retention.; 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; M94375; AAA28551.1; -; mRNA.
DR EMBL; L33831; AAA69860.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48598.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF48599.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09399.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09400.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09401.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09402.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65387.1; -; Genomic_DNA.
DR EMBL; BT021414; AAX33562.1; ALT_SEQ; mRNA.
DR EMBL; AY070553; AAL48024.1; ALT_INIT; mRNA.
DR PIR; A43434; A43434.
DR RefSeq; NP_523368.2; NM_078644.4. [P30432-1]
DR RefSeq; NP_727963.1; NM_167506.3. [P30432-2]
DR RefSeq; NP_727964.1; NM_167507.3. [P30432-2]
DR RefSeq; NP_727965.1; NM_167508.2. [P30432-2]
DR RefSeq; NP_727966.1; NM_167509.3. [P30432-1]
DR RefSeq; NP_727967.1; NM_167510.3. [P30432-1]
DR RefSeq; NP_996486.1; NM_206763.2. [P30432-1]
DR AlphaFoldDB; P30432; -.
DR SMR; P30432; -.
DR BioGRID; 58944; 19.
DR IntAct; P30432; 6.
DR STRING; 7227.FBpp0074038; -.
DR MEROPS; S08.049; -.
DR GlyGen; P30432; 12 sites.
DR PaxDb; P30432; -.
DR EnsemblMetazoa; FBtr0074261; FBpp0074038; FBgn0004598. [P30432-2]
DR EnsemblMetazoa; FBtr0074262; FBpp0074039; FBgn0004598. [P30432-1]
DR EnsemblMetazoa; FBtr0074263; FBpp0074040; FBgn0004598. [P30432-2]
DR EnsemblMetazoa; FBtr0074264; FBpp0074041; FBgn0004598. [P30432-1]
DR EnsemblMetazoa; FBtr0074265; FBpp0074042; FBgn0004598. [P30432-2]
DR EnsemblMetazoa; FBtr0074266; FBpp0074043; FBgn0004598. [P30432-1]
DR EnsemblMetazoa; FBtr0074267; FBpp0089399; FBgn0004598. [P30432-1]
DR GeneID; 32604; -.
DR KEGG; dme:Dmel_CG18734; -.
DR CTD; 32604; -.
DR FlyBase; FBgn0004598; Fur2.
DR VEuPathDB; VectorBase:FBgn0004598; -.
DR eggNOG; KOG3525; Eukaryota.
DR GeneTree; ENSGT00940000167869; -.
DR InParanoid; P30432; -.
DR PhylomeDB; P30432; -.
DR BioGRID-ORCS; 32604; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32604; -.
DR PRO; PR:P30432; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004598; Expressed in cleaving embryo and 23 other tissues.
DR ExpressionAtlas; P30432; baseline and differential.
DR Genevisible; P30432; DM.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:FlyBase.
DR GO; GO:0051048; P:negative regulation of secretion; IGI:FlyBase.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0045464; P:R8 cell fate specification; IMP:FlyBase.
DR CDD; cd00064; FU; 9.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 3.30.70.850; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR032778; GF_recep_IV.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR032815; S8_pro-domain.
DR InterPro; IPR038466; S8_pro-domain_sf.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16470; S8_pro-domain; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00261; FU; 10.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR SUPFAM; SSF57184; SSF57184; 3.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome; Repeat;
KW Serine protease; Signal; Transmembrane; Transmembrane helix; Zymogen.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT PROPEP ?..318
FT /evidence="ECO:0000255"
FT /id="PRO_0000027024"
FT CHAIN 319..1679
FT /note="Furin-like protease 2"
FT /id="PRO_0000027025"
FT TRANSMEM 1512..1532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1533..1679
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 383..705
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 714..852
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT REPEAT 961..1006
FT /note="FU 1"
FT REPEAT 1009..1056
FT /note="FU 2"
FT REPEAT 1060..1104
FT /note="FU 3"
FT REPEAT 1107..1152
FT /note="FU 4"
FT REPEAT 1156..1204
FT /note="FU 5"
FT REPEAT 1208..1253
FT /note="FU 6"
FT REPEAT 1256..1299
FT /note="FU 7"
FT REPEAT 1301..1346
FT /note="FU 8"
FT REPEAT 1348..1393
FT /note="FU 9"
FT REPEAT 1396..1443
FT /note="FU 10"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1660..1679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 456
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 637
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 927
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1060
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 473..629
FT /evidence="ECO:0000250"
FT DISULFID 565..595
FT /evidence="ECO:0000250"
FT DISULFID 720..748
FT /evidence="ECO:0000250"
FT VAR_SEQ 386
FT /note="L -> LVSK (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_009365"
FT CONFLICT 152..153
FT /note="Missing (in Ref. 1; AAA28551)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="V -> F (in Ref. 1; AAA28551)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="V -> VDQL (in Ref. 1; AAA28551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1679 AA; 183370 MW; 3F9E749F0B021CF6 CRC64;
MSNTTRSSRV TIGRIGTTPQ ITDPWSSGLE KQRPSRCGGP KSLAEPTYRK IGRRKMMLHM
RVHDPGTTVT QRAKETATAK LNRIYLCTFN RMAQSCIYFV LFLVILSPNT SCALRSSAGE
TQNYVGILSN DSATTTYDVS SLHSSRRTNP PSSSSSSSSN VDVDYRNDRE LHKVDLVGLG
GERAGQAETI SGGKYDYNYE NTHTNASAKD EIVERQSNSL DFDGVDMFGA FSIPEEAIYT
NEFAVNIPAG KQMADVIATK HGFINRGQIG SLDNYYLFQH HHVSKRSLRS SRKHQGALKS
ENEVKWMQQQ HEKVRRKRDG PYQDLPTYSP YNLLRQHGGY VVDPNPHLSF SPESISLASH
SQRMEYRDVS SHFIFPDPLF KEQWYLNGGA KDGLDMNVGP AWQKGYTGKG VVVSILDDGI
QTNHPDLAQN YDPEASFDIN GNDSDPTPQD NGDNKHGTRC AGEVAAVAFN NFCGVGVAYN
ASIGGVRMLD GKVNDVVEAQ ALSLNPSHID IYSASWGPED DGSTVDGPGP LARRAFIYGV
TSGRQGKGSI FVWASGNGGR YTDSCNCDGY TNSIFTLSIS SATQAGFKPW YLEECSSTLA
TTYSSGTPGH DKSVATVDMD GSLRPDHICT VEHTGTSASA PLAAGICALA LEANPELTWR
DMQYLVVYTS RPAPLEKENG WTLNGVKRKY SHKFGYGLMD AGAMVSLAEQ WTSVPPQHIC
KSRENNEDRK IDGAYGSTLS THMDVNGCAG TINEVRYLEH VQCRITLRFF PRGNLRILLT
SPMGTTSTLL FERPRDIVKS NFDDWPFLSV HFWGEKAEGR WTLQVINGGR RRVNQPGILS
KWQLIFYGTS TQPMRLKSEL LNSSPQLRSP SSSNPFLFPS ASNIGQPANE GGNFNTDSFA
SYLNYQNIFS SAGSDPEPAT ATLDGQNVTA AIAGGSSAES LGFTASAAQL VAAPETRDGD
KKILHSCDAE CDSSGCYGRG PTQCVACSHY RLDNTCVSRC PPRSFPNQVG ICWPCHDTCE
TCAGAGPDSC LTCAPAHLHV IDLAVCLQFC PDGYFENSRN RTCVPCEPNC ASCQDHPEYC
TSCDHHLVMH EHKCYSACPL DTYETEDNKC AFCHSTCATC NGPTDQDCIT CRSSRYAWQN
KCLISCPDGF YADKKRLECM PCQEGCKTCT SNGVCSECLQ NWTLNKRDKC IVSGSEGCSE
SEFYSQVEGQ CRPCHASCGS CNGPADTSCT SCPPNRLLEQ SRCVSGCREG FFVEAGSLCS
PCLHTCSQCV SRTNCSNCSK GLELQNGECR TTCADGYYSD RGICAKCYLS CHTCSGPRRN
QCVQCPAGWQ LAAGECHPEC PEGFYKSDFG CQKCHHYCKT CNDAGPLACT SCPPHSMLDG
GLCMECLSSQ YYDTTSATCK TCHDSCRSCF GPGQFSCKGC VPPLHLDQLN SQCVSCCQNQ
TLAEKTSSAA CCNCDGETGE CKATSTGGKR RTVVGSGSAY KSSESKHGSF ENDGNAREFV
LRLDSPLTAI TAIAVAICLL IITIFSIIFA VLQRNSNHVS RNSVRYRKIA NTSSGRRKNL
SAKPTSDARF IFNIGEDDDT DGDNSDDELD GNVGTDINNR IVYDRKGNDH GHEFYIESTN
DIDAIEFHCN GAGAQKAETQ LQRCNANGDD DDILHYDRHT NAERKNHPSS TTSRTNIRS
