FUR11_DROME
ID FUR11_DROME Reviewed; 1269 AA.
AC P26016; A4V3E2; Q05817; Q27436;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Furin-like protease 1, isoforms 1/1-X/2;
DE Short=Furin-1;
DE EC=3.4.21.75;
DE AltName: Full=Kex2-like endoprotease 1;
DE AltName: Full=dKLIP-1;
DE Flags: Precursor;
GN Name=Fur1; ORFNames=CG10772;
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 1).
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=1915835; DOI=10.1016/0014-5793(91)81052-a;
RA Roebroek A.J.M., Pauli I.G.L., Zhang Y., van de Ven W.J.M.;
RT "cDNA sequence of a Drosophila melanogaster gene, Dfur1, encoding a protein
RT structurally related to the subtilisin-like proprotein processing enzyme
RT furin.";
RL FEBS Lett. 289:133-137(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1-X AND
RP 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R, and Tuebingen; TISSUE=Embryo;
RX PubMed=8491178; DOI=10.1002/j.1460-2075.1993.tb05834.x;
RA Roebroek A.J.M., Creemers J.W.M., Pauli I.G.L., Bogaert T.,
RA Van de Ven W.J.M.;
RT "Generation of structural and functional diversity in furin-like proteins
RT in Drosophila melanogaster by alternative splicing of the DFur1 gene.";
RL EMBO J. 12:1853-1870(1993).
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 2).
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: Golgi apparatus membrane
CC {ECO:0000269|PubMed:8491178}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:8491178}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1-X; Synonyms=E;
CC IsoId=P26016-1; Sequence=Displayed;
CC Name=1; Synonyms=F;
CC IsoId=P26016-2; Sequence=VSP_005424, VSP_008042;
CC Name=2; Synonyms=C, D, F;
CC IsoId=P26016-3; Sequence=VSP_005424;
CC Name=1-CRR; Synonyms=A;
CC IsoId=P30430-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: In adults, isoform 1-X is expressed in CNS, fat
CC body and female reproductive tissues, and in embryos, in CNS, tracheal
CC pits, hindgut, posterior spiracles and anal pads.
CC {ECO:0000269|PubMed:8491178}.
CC -!- DEVELOPMENTAL STAGE: Isoforms 1-X and 2 are expressed in embryos,
CC larvae, pupae and adults. Highest expression is in late embryos.
CC {ECO:0000269|PubMed:8491178}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000305}.
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DR EMBL; X59384; CAA42027.1; -; mRNA.
DR EMBL; L12370; AAA28546.1; -; Genomic_DNA.
DR EMBL; L12369; AAA28546.1; JOINED; Genomic_DNA.
DR EMBL; L12370; AAA28547.1; -; Genomic_DNA.
DR EMBL; L12369; AAA28547.1; JOINED; Genomic_DNA.
DR EMBL; L12375; AAA28550.1; -; mRNA.
DR EMBL; L12376; AAA28549.1; -; mRNA.
DR EMBL; AE014297; AAF56463.2; -; Genomic_DNA.
DR EMBL; AE014297; AAF56464.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14052.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65215.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65216.1; -; Genomic_DNA.
DR EMBL; AY069590; AAL39735.1; -; mRNA.
DR PIR; S17546; S17546.
DR PIR; S35366; S35366.
DR RefSeq; NP_524885.1; NM_080146.3. [P26016-1]
DR RefSeq; NP_733103.1; NM_170655.2. [P26016-3]
DR RefSeq; NP_733104.1; NM_170656.2. [P26016-3]
DR RefSeq; NP_996293.1; NM_206570.2. [P26016-3]
DR RefSeq; NP_996294.2; NM_206571.2. [P26016-3]
DR AlphaFoldDB; P26016; -.
DR SMR; P26016; -.
DR BioGRID; 70692; 5.
DR IntAct; P26016; 4.
DR STRING; 7227.FBpp0089026; -.
DR MEROPS; S08.048; -.
DR GlyGen; P26016; 13 sites.
DR PaxDb; P26016; -.
DR PRIDE; P26016; -.
DR DNASU; 47220; -.
DR EnsemblMetazoa; FBtr0089983; FBpp0089026; FBgn0004509. [P26016-1]
DR EnsemblMetazoa; FBtr0089984; FBpp0089027; FBgn0004509. [P26016-3]
DR EnsemblMetazoa; FBtr0089985; FBpp0089028; FBgn0004509. [P26016-3]
DR EnsemblMetazoa; FBtr0089987; FBpp0089030; FBgn0004509. [P26016-3]
DR EnsemblMetazoa; FBtr0336805; FBpp0307776; FBgn0004509. [P26016-3]
DR GeneID; 47220; -.
DR KEGG; dme:Dmel_CG10772; -.
DR CTD; 47220; -.
DR FlyBase; FBgn0004509; Fur1.
DR VEuPathDB; VectorBase:FBgn0004509; -.
DR eggNOG; KOG3525; Eukaryota.
DR HOGENOM; CLU_002976_0_3_1; -.
DR InParanoid; P26016; -.
DR PhylomeDB; P26016; -.
DR BRENDA; 3.4.21.75; 1994.
DR Reactome; R-DME-1592389; Activation of Matrix Metalloproteinases.
DR Reactome; R-DME-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR Reactome; R-DME-186797; Signaling by PDGF.
DR Reactome; R-DME-2173789; TGF-beta receptor signaling activates SMADs.
DR BioGRID-ORCS; 47220; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Fur1; fly.
DR GenomeRNAi; 47220; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004509; Expressed in oviduct (Drosophila) and 46 other tissues.
DR ExpressionAtlas; P26016; baseline and differential.
DR Genevisible; P26016; 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; IDA: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:0097688; P:glutamate receptor clustering; IMP:FlyBase.
DR GO; GO:0016486; P:peptide hormone processing; IBA:GO_Central.
DR GO; GO:0001941; P:postsynaptic membrane organization; IMP:FlyBase.
DR GO; GO:0097090; P:presynaptic membrane organization; IMP:FlyBase.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0008039; P:synaptic target recognition; IMP:FlyBase.
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; IPR008979; Galactose-bd-like_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; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF16470; S8_pro-domain; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
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; Golgi apparatus; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Signal; Transmembrane;
KW Transmembrane helix; Zymogen.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT PROPEP ?..309
FT /evidence="ECO:0000255"
FT /id="PRO_0000027020"
FT CHAIN 310..1269
FT /note="Furin-like protease 1, isoforms 1/1-X/2"
FT /id="PRO_0000027021"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1233..1253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 340..654
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 662..793
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..181
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 413
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 587
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 814
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 857
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 908
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 994
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 430..579
FT /evidence="ECO:0000250"
FT DISULFID 522..552
FT /evidence="ECO:0000250"
FT DISULFID 669..695
FT /evidence="ECO:0000250"
FT VAR_SEQ 776..1152
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:1915835"
FT /id="VSP_005424"
FT VAR_SEQ 1208
FT /note="Q -> QQYPFPFQ (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:1915835"
FT /id="VSP_008042"
SQ SEQUENCE 1269 AA; 138627 MW; 594E641CFB024C82 CRC64;
MKNDVVRWSR QPTSNTTNSS SSSRSDSNST HKHRSKSNKL NARQLGSNAA RSCQQRSSVA
TTLEDEQQTI IECDIGNFNF DCNLFKTSFL TQHKQKRSGK SSSKSKSNRS RPLAKTKAVF
LLALQFSAVV FLCNINVGFV AGSVATAASS AGGSSPAAPS SAPSSPPTVA VPPPPPPSSA
LKVDPNGQSP VLPPYVLDYE TGGKAKLTPN NGKFGQSGSS GSNNNHIVGH YTHTWAVHIP
NGDNGMADAV AKDHGFVNLG KIFDDHYHFA HHKVSKRSLS PATHHQTRLD DDDRVHWAKQ
QRAKSRSKRD FIRMRPSRTS SRAMSMVDAM SFNDSKWPQM WYLNRGGGLD MNVIPAWKMG
ITGKGVVVTI LDDGLESDHP DIQDNYDPKA SYDVNSHDDD PMPHYDMTDS NRHGTRCAGE
VAATANNSFC AVGIAYGASV GGVRMLDGDV TDAVEARSLS LNPQHIDIYS ASWGPDDDGK
TVDGPGELAS RAFIEGTTKG RGGKGSIFIW ASGNGGREQD NCNCDGYTNS IWTLSISSAT
EEGHVPWYSE KCSSTLATTY SSGGQGEKQV VTTDLHHSCT VSHTGTSASA PLAAGIAALV
LQSNQNLTWR DLQHIVVRTA KPANLKDPSW SRNGVGRRVS HSFGYGLMDA AEMVRVARNW
KAVPEQQRCE INAPHVDKVI PPRTHITLQL TVNHCRSVNY LEHVQAKITL TSQRRGDIQL
FLRSPANTSV TLLTPRIHDN SRSGFNQWPF MSVHTWGESP QGNWQLEIHN EGRYMGHALL
REWSLIFYGT TQSIGPNDPI SVPKPSGSEA TTPNSSSTTS NLHQAYSPQY PRIPPNNFGS
SPSGGSKLPL GKVPPPNKSS YVTNNPLLNS APPKQGYQQI SATYGVILGK ANGKSNNNSK
EKTNNKGNKS NNGNKGKSGG SSGNRKEQTT QSTIIQTSTS KNKYYRISQQ QQQKNNKQDR
NGVQTQRPKA NSGEKSYDEK SRKVVGEITT NSGNGSIKAA KQVKESTTTS SNSRIPKLFE
RYEKIQAIFP ELEPYENSSP KGKPKQAKQG KQFEVDLFKP TNGGNSRQGN TKKSPSVPPP
SQTMATLSIL PILPAGGSSF LPDQKILKKQ QLLMAAAGVM APAQVEVEME EVHATPDYEA
RKDQRKEVNG PNAQITQWDM IFYGTETPAQ PDDVANPSQS NQFNLYGNDM AHNDVEYDST
GQWRNMQQVG EVGMTRDHSN TAACLKWSDR KCLGLSLLFF MIMQVFFLNF KHANDNNNKN
KNNIIKCIR
