FBN2_MOUSE
ID FBN2_MOUSE Reviewed; 2907 AA.
AC Q61555; E9QJZ4; Q63957;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Fibrillin-2 {ECO:0000303|PubMed:32329225};
DE Contains:
DE RecName: Full=Placensin {ECO:0000303|PubMed:32329225};
DE Flags: Precursor;
GN Name=Fbn2 {ECO:0000303|PubMed:32329225, ECO:0000312|MGI:MGI:95490};
GN Synonyms=Fbn-2;
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 [GENOMIC DNA].
RX PubMed=7744963; DOI=10.1083/jcb.129.4.1165;
RA Zhang H., Hu W., Ramirez F.;
RT "Developmental expression of fibrillin genes suggests heterogeneity of
RT extracellular microfibrils.";
RL J. Cell Biol. 129:1165-1176(1995).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 210-317.
RX PubMed=8307578; DOI=10.1016/s0888-7543(05)80371-4;
RA Li X., Pereira L., Zhang H., Sanguineti C., Ramirez F., Bonadio J.,
RA Francke U.;
RT "Fibrillin genes map to regions of conserved mouse/human synteny on mouse
RT chromosomes 2 and 18.";
RL Genomics 18:667-672(1993).
RN [4]
RP PROTEIN SEQUENCE OF 2429-2441, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=11470817; DOI=10.1083/jcb.200105046;
RA Arteaga-Solis E., Gayraud B., Lee S.Y., Shum L., Sakai L., Ramirez F.;
RT "Regulation of limb patterning by extracellular microfibrils.";
RL J. Cell Biol. 154:275-281(2001).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=16407178; DOI=10.1074/jbc.m511599200;
RA Carta L., Pereira L., Arteaga-Solis E., Lee-Arteaga S.Y., Lenart B.,
RA Starcher B., Merkel C.A., Sukoyan M., Kerkis A., Hazeki N., Keene D.R.,
RA Sakai L.Y., Ramirez F.;
RT "Fibrillins 1 and 2 perform partially overlapping functions during aortic
RT development.";
RL J. Biol. Chem. 281:8016-8023(2006).
RN [7]
RP FUNCTION (FIBRILLIN-2), AND DISRUPTION PHENOTYPE.
RX PubMed=20855508; DOI=10.1083/jcb.201003089;
RA Nistala H., Lee-Arteaga S., Smaldone S., Siciliano G., Carta L., Ono R.N.,
RA Sengle G., Arteaga-Solis E., Levasseur R., Ducy P., Sakai L.Y.,
RA Karsenty G., Ramirez F.;
RT "Fibrillin-1 and -2 differentially modulate endogenous TGF-{beta} and BMP
RT bioavailability during bone formation.";
RL J. Cell Biol. 190:1107-1121(2010).
RN [8]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=24039232; DOI=10.1242/jcs.127571;
RA Tiedemann K., Boraschi-Diaz I., Rajakumar I., Kaur J., Roughley P.,
RA Reinhardt D.P., Komarova S.V.;
RT "Fibrillin-1 directly regulates osteoclast formation and function by a dual
RT mechanism.";
RL J. Cell Sci. 126:4187-4194(2013).
RN [9]
RP FUNCTION (PLACENSIN), AND TISSUE SPECIFICITY.
RX PubMed=32329225; DOI=10.15252/embr.201949530;
RA Yu Y., He J.H., Hu L.L., Jiang L.L., Fang L., Yao G.D., Wang S.J., Yang Q.,
RA Guo Y., Liu L., Shang T., Sato Y., Kawamura K., Hsueh A.J., Sun Y.P.;
RT "Placensin is a glucogenic hormone secreted by human placenta.";
RL EMBO Rep. 21:e49530-e49530(2020).
CC -!- FUNCTION: [Fibrillin-2]: Fibrillins are structural components of 10-12
CC nm extracellular calcium-binding microfibrils, which occur either in
CC association with elastin or in elastin-free bundles (PubMed:20855508).
CC Fibrillin-2-containing microfibrils regulate the early process of
CC elastic fiber assembly. Regulates osteoblast maturation by controlling
CC TGF-beta bioavailability and calibrating TGF-beta and BMP levels,
CC respectively (PubMed:20855508). {ECO:0000269|PubMed:20855508}.
CC -!- FUNCTION: [Placensin]: Hormone secreted by trophoblasts that promotes
CC trophoblast invasiveness (By similarity). Has glucogenic activity: is
CC able to increase plasma glucose levels (PubMed:32329225).
CC {ECO:0000250|UniProtKB:P35556, ECO:0000269|PubMed:32329225}.
CC -!- SUBUNIT: Interacts with BMP2, BMP4, BMP7, BMP10 and GDF5. Interacts
CC with MFAP2 and MFAP5. Interacts with ADAMTSL5. Interacts with MFAP4.
CC {ECO:0000250|UniProtKB:P35556}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P35556}.
CC Note=Fibrillin-2 and Placensin chains are still linked together during
CC the secretion from cells, but are subsequently separated by furin.
CC {ECO:0000250|UniProtKB:P35556}.
CC -!- SUBCELLULAR LOCATION: [Fibrillin-2]: Secreted, extracellular space,
CC extracellular matrix {ECO:0000269|PubMed:24039232}.
CC -!- SUBCELLULAR LOCATION: [Placensin]: Secreted
CC {ECO:0000250|UniProtKB:P35556}. Note=Secreted by placental cells.
CC {ECO:0000250|UniProtKB:P35556}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:32329225}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed during the first week of
CC osteoblast differentiation. {ECO:0000269|PubMed:24039232}.
CC -!- PTM: [Placensin]: N-glycosylated. {ECO:0000250|UniProtKB:P35556}.
CC -!- PTM: O-glycosylated on serine residues by POGLUT2 and POGLUT3.
CC {ECO:0000250|UniProtKB:P35556}.
CC -!- DISRUPTION PHENOTYPE: Limb-patterning defects characterized by
CC bilateral syndactyly due to disorganized matrix (PubMed:11470817).
CC Digit fusion involves both soft and hard tissues and is associated with
CC reduced apoptosis at affected sites (PubMed:11470817). Mice show a well
CC developed and morphologically normal aortic wall (PubMed:16407178).
CC Mice display a low bone mass phenotype that is associated with reduced
CC bone formation (PubMed:20855508). {ECO:0000269|PubMed:11470817,
CC ECO:0000269|PubMed:16407178, ECO:0000269|PubMed:20855508}.
CC -!- SIMILARITY: Belongs to the fibrillin family. {ECO:0000305}.
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DR EMBL; L39790; AAA74908.1; -; Genomic_DNA.
DR EMBL; AC102317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S69359; AAC60685.1; -; Unassigned_DNA.
DR CCDS; CCDS37827.1; -.
DR PIR; A57278; A57278.
DR RefSeq; NP_034311.2; NM_010181.2.
DR SMR; Q61555; -.
DR BioGRID; 199608; 4.
DR STRING; 10090.ENSMUSP00000025497; -.
DR GlyGen; Q61555; 12 sites.
DR iPTMnet; Q61555; -.
DR PhosphoSitePlus; Q61555; -.
DR jPOST; Q61555; -.
DR MaxQB; Q61555; -.
DR PaxDb; Q61555; -.
DR PeptideAtlas; Q61555; -.
DR PRIDE; Q61555; -.
DR ProteomicsDB; 271877; -.
DR Antibodypedia; 2482; 168 antibodies from 28 providers.
DR DNASU; 14119; -.
DR Ensembl; ENSMUST00000025497; ENSMUSP00000025497; ENSMUSG00000024598.
DR GeneID; 14119; -.
DR KEGG; mmu:14119; -.
DR UCSC; uc008ezn.1; mouse.
DR CTD; 2201; -.
DR MGI; MGI:95490; Fbn2.
DR VEuPathDB; HostDB:ENSMUSG00000024598; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00950000183158; -.
DR HOGENOM; CLU_000233_0_0_1; -.
DR InParanoid; Q61555; -.
DR OMA; HQCVACP; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; Q61555; -.
DR TreeFam; TF316849; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1566948; Elastic fibre formation.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR BioGRID-ORCS; 14119; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Fbn2; mouse.
DR PRO; PR:Q61555; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q61555; protein.
DR Bgee; ENSMUSG00000024598; Expressed in ureter smooth muscle and 207 other tissues.
DR Genevisible; Q61555; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0001527; C:microfibril; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; TAS:MGI.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IDA:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0060346; P:bone trabecula formation; IMP:BHF-UCL.
DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR GO; GO:0048048; P:embryonic eye morphogenesis; IEA:Ensembl.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IDA:UniProtKB.
DR GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
DR GO; GO:0001890; P:placenta development; ISS:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
DR GO; GO:1901163; P:regulation of trophoblast cell migration; ISS:UniProtKB.
DR GO; GO:0035583; P:sequestering of TGFbeta in extracellular matrix; IMP:BHF-UCL.
DR Gene3D; 3.90.290.10; -; 9.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR011398; FBN.
DR InterPro; IPR040872; Fibrillin_U_N.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR017878; TB_dom.
DR InterPro; IPR036773; TB_dom_sf.
DR PANTHER; PTHR24039:SF26; PTHR24039:SF26; 5.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 38.
DR Pfam; PF18193; Fibrillin_U_N; 1.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00683; TB; 9.
DR SMART; SM00181; EGF; 46.
DR SMART; SM00179; EGF_CA; 44.
DR SUPFAM; SSF57184; SSF57184; 13.
DR SUPFAM; SSF57581; SSF57581; 9.
DR PROSITE; PS00010; ASX_HYDROXYL; 43.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 37.
DR PROSITE; PS50026; EGF_3; 45.
DR PROSITE; PS01187; EGF_CA; 43.
DR PROSITE; PS51364; TB; 9.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..77
FT /evidence="ECO:0000305"
FT /id="PRO_0000436889"
FT CHAIN 78..2773
FT /note="Fibrillin-2"
FT /id="PRO_0000007585"
FT CHAIN 2774..2907
FT /note="Placensin"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT /id="PRO_0000436890"
FT DOMAIN 111..142
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 145..176
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 176..208
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 214..266
FT /note="TB 1"
FT DOMAIN 276..317
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 318..359
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 364..417
FT /note="TB 2"
FT DOMAIN 487..527
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 528..567
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 568..609
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 610..650
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 651..691
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 697..749
FT /note="TB 3"
FT DOMAIN 761..802
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 803..844
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 845..883
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 889..940
FT /note="TB 4"
FT DOMAIN 948..989
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 994..1045
FT /note="TB 5"
FT DOMAIN 1066..1107
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1108..1150
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1151..1192
FT /note="EGF-like 17; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1193..1234
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1235..1275
FT /note="EGF-like 19; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1276..1317
FT /note="EGF-like 20; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1318..1359
FT /note="EGF-like 21; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1360..1400
FT /note="EGF-like 22; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1401..1441
FT /note="EGF-like 23; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1442..1483
FT /note="EGF-like 24; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1484..1524
FT /note="EGF-like 25; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1525..1565
FT /note="EGF-like 26; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1570..1626
FT /note="TB 6"
FT DOMAIN 1643..1684
FT /note="EGF-like 27; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1685..1726
FT /note="EGF-like 28; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1731..1784
FT /note="TB 7"
FT DOMAIN 1801..1842
FT /note="EGF-like 29; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1843..1884
FT /note="EGF-like 30; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1885..1926
FT /note="EGF-like 31; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1927..1965
FT /note="EGF-like 32; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1966..2008
FT /note="EGF-like 33; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2009..2048
FT /note="EGF-like 34; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2049..2090
FT /note="EGF-like 35; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2095..2148
FT /note="TB 8"
FT DOMAIN 2164..2205
FT /note="EGF-like 36; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2206..2245
FT /note="EGF-like 37; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2246..2286
FT /note="EGF-like 38; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2287..2330
FT /note="EGF-like 39; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2331..2372
FT /note="EGF-like 40; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2377..2430
FT /note="TB 9"
FT DOMAIN 2442..2483
FT /note="EGF-like 41; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2484..2524
FT /note="EGF-like 42; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2525..2563
FT /note="EGF-like 43; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2564..2606
FT /note="EGF-like 44; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2607..2646
FT /note="EGF-like 45; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2647..2687
FT /note="EGF-like 46; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2688..2727
FT /note="EGF-like 47; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 26..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..359
FT /note="Interaction with MFAP4"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT REGION 1728..2164
FT /note="Interaction with MFAP4"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT COMPBIAS 28..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 298
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 340
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 548
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 590
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 631
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 672
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 825
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 865
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 970
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 1088
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 1105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1173
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 1215
FT /note="O-linked (Glc) threonine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 1256
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 1340
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 1383
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 1407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1665
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 1707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1738
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1866
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 1938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1947
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 1989
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 2113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2186
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 2218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2267
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 2353
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 2464
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 2505
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 2587
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 2668
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35556"
FT CARBOHYD 2803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 119..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 132..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 149..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 153..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 166..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 180..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 184..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 198..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 280..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 287..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 303..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 322..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 329..343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 345..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 491..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 498..512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 514..526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 532..542
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 537..551
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 553..566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 572..584
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 579..593
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 595..608
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 614..625
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 620..634
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 636..649
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 655..666
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 661..675
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 677..690
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 765..777
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 772..786
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 788..801
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 807..819
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 814..828
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 830..843
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 849..859
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 854..868
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 870..883
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 952..964
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 959..973
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 975..988
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1070..1082
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1077..1091
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1093..1106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1112..1124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1119..1133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1135..1149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1155..1167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1162..1176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1178..1191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1197..1209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1204..1218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1220..1233
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1239..1250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1246..1259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1261..1274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1280..1292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1287..1301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1303..1316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1322..1334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1329..1343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1345..1358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1364..1377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1371..1386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1388..1399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1405..1418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1412..1427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1429..1440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1446..1458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1453..1467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1469..1482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1488..1499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1494..1508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1510..1523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1529..1540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1535..1549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1551..1564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1647..1659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1654..1668
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1670..1683
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1689..1701
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1696..1710
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1712..1725
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1805..1817
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1812..1826
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1828..1841
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1847..1860
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1854..1869
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1871..1883
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1889..1901
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1896..1910
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1912..1925
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1931..1941
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1936..1950
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1952..1964
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1970..1983
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1978..1992
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1994..2007
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2013..2025
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2020..2034
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2036..2047
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2053..2065
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2060..2074
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2076..2089
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2168..2180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2175..2189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2191..2204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2210..2221
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2216..2230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2232..2244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2250..2261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2257..2270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2272..2285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2291..2305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2298..2314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2316..2329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2335..2347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2342..2356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2358..2371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2446..2458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2453..2467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2469..2482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2488..2499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2495..2508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2510..2523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2529..2540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2536..2549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2551..2562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2568..2581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2575..2590
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2592..2605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2611..2621
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2617..2630
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2632..2645
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2651..2662
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2657..2671
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2673..2686
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2692..2703
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2699..2712
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2714..2726
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 39
FT /note="R -> W (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="A -> R (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="A -> R (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="R -> P (in Ref. 1; AAA74908 and 3; AAC60685)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="T -> N (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="E -> R (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 587
FT /note="T -> S (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 783
FT /note="S -> T (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 836..837
FT /note="FR -> LP (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 919
FT /note="A -> G (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 1064
FT /note="Y -> C (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 1559
FT /note="P -> A (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 1590
FT /note="V -> A (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 1622
FT /note="Y -> H (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 1765
FT /note="W -> G (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 1937
FT /note="G -> A (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 2227
FT /note="S -> C (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 2277
FT /note="A -> G (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 2475
FT /note="T -> M (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
FT CONFLICT 2634..2636
FT /note="QGY -> HGD (in Ref. 1; AAA74908)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2907 AA; 313818 MW; 57FCD5188B1D63FF CRC64;
MGRRRRLCLQ PYFVWLGCVA LWAQGTDGQP QPPPPKTLRP QPPPQQVRPA VAGSEGGFMG
PEYRDEGAVA ASRVRRRGQQ EILRGPNVCG SRFHSYCCPG WKTLPGGNQC IVPICRNSCG
DGFCSRPNMC TCSSGQISPT CGAKSIQQCS VRCMNGGTCA DDHCQCQKGY IGTYCGQPVC
ENGCQNGGRC IGPNRCACVY GFTGPQCERD YRTGPCFTQV NNQMCQGQLT GIVCTKTLCC
ATIGRAWGHP CEMCPAQPQP CRRGFIPNIR TGACQDVDEC QAIPGLCQGG NCINTVGSFE
CRCPAGHKQS ETTQKCEDID ECSVIPGVCE TGDCSNTVGS YFCLCPRGFV TSTDGSRCID
QRAGTCFSGL VNGRCAQELP GRMAKAQCCC EPGRCWSIGT IPEACPVRGS EEYRRLCLDG
LPMGGIPGSS VSRPGGTGST GNGYGPGGTG FLPIPGDNGF SPGVGGAGVG AGGQGPIITG
LTILNQTIDI CKHHANLCLN GRCIPTVSSY RCECNMGYKQ DANGDCIDVD ECTSNPCSNG
DCVNTPGSYY CKCHAGFQRT PTKQACIDID ECIQNGVLCK NGRCVNTDGS FQCICNAGFE
LTTDGKNCVD HDECTTTNMC LNGMCINEDG SFKCVCKPGF ILAPNGRYCT DVDECQTPGI
CMNGHCINNE GSFRCDCPPG LAVGVDGRVC VDTHMRSTCY GEIKKGVCVR PFPGAVTKSE
CCCANPDYGF GEPCQPCPAK NSAEFHGLCS SGIGITVDGR DINECALDPD ICANGICENL
RGSYRCNCNS GYEPDASGRN CIDIDECLVN RLLCDNGLCR NTPGSYSCTC PPGYVFRTET
ETCEDVNECE SNPCVNGACR NNLGSFHCEC SPGSKLSSTG LICIDSLKGT CWLNIQDNRC
EVNINGATLK SECCATLGAA WGSPCERCEL DAACPRGFAR IKGVTCEDVN ECEVFPGVCP
NGRCVNSKGS FHCECPEGLT LDGTGRVCLD IRMEHCFLKW DEDECIHPVP GKFRMDACCC
AVGAAWGTEC EECPKPGTKE YETLCPRGPG FANRGDILTG RPFYKDINEC KAFPGMCTYG
KCRNTIGSFK CRCNNGFALD MEERNCTDID ECRISPDLCG SGICVNTPGS FECECFEGYE
SGFMMMKNCM DIDECERNPL LCRGGTCVNT EGSFQCDCPL GHELSPSRED CVDINECSLS
DNLCRNGKCV NMIGTYQCSC NPGYQATPDR QGCTDIDECM IMNGGCDTQC TNSEGSYECS
CSEGYALMPD GRSCADIDEC ENNPDICDGG QCTNIPGEYR CLCYDGFMAS MDMKTCIDVN
ECDLNPNICM FGECENTKGS FICHCQLGYS VKKGTTGCTD VDECEIGAHN CDMHASCLNV
PGSFKCSCRE GWVGNGIKCI DLDECANGTH QCSINAQCVN TPGSYRCACS EGFTGDGFTC
SDVDECAENT NLCENGQCLN VPGAYRCECE MGFTPASDSR SCQDIDECSF QNICVFGTCN
NLPGMFHCIC DDGYELDRTG GNCTDIDECA DPINCVNGLC VNTPGRYECN CPPDFQLNPT
GVGCVDNRVG NCYLKFGPRG DGSLSCNTEV GVGVSRSSCC CSLGKAWGNP CETCPPVNST
EYYTLCPGGE GFRPNPITII LEDIDECQEL PGLCQGGNCI NTFGSFQCEC PQGYYLSEET
RICEDIDECF AHPGVCGPGT CYNTLGNYTC ICPPEYMQVN GGHNCMDMRK SFCYRSYNGT
TCENELPFNV TKRMCCCTYN VGKAWNKPCE PCPTPGTADF KTICGNIPGF TFDIHTGKAV
DIDECKEIPG ICANGVCINQ IGSFRCECPT GFSYNDLLLV CEDIDECSNG DNLCQRNADC
INSPGSYRCE CAAGFKLSPN GACVDRNECL EIPNVCSHGL CVDLQGSYQC ICNNGFKASQ
DQTMCMDVDE CERHPCGNGT CKNTVGSYNC LCYPGFELTH NNDCLDIDEC SSFFGQVCRN
GRCFNEIGSF KCLCNEGYEL TPDGKNCIDT NECVALPGSC SPGTCQNLEG SFRCICPPGY
EVRSENCIDI NECDEDPNIC LFGSCTNTPG GFQCICPPGF VLSDNGRRCF DTRQSFCFTN
FENGKCSVPK AFNTTKAKCC CSKMPGEGWG DPCELCPKDD EVAFQDLCPY GHGTVPSLHD
TREDVNECLE SPGICSNGQC INTDGSFRCE CPMGYNLDYT GVRCVDTDEC SIGNPCGNGT
CTNVIGSFEC TCNEGFEPGP MMNCEDINEC AQNPLLCAFR CMNTFGSYEC TCPVGYALRE
DQKMCKDLDE CAEGLHDCES RGMMCKNLIG TFMCICPPGM ARRPDGEGCV DENECRTKPG
ICENGRCVNI IGSYRCECNE GFQSSSSGTE CLDNRQGLCF AEVLQTMCQM ASSSRNLVTK
SECCCDGGRG WGHQCELCPL PGTAQYKKIC PHGPGYATDG RDIDECKVMP SLCTNGQCVN
TMGSFRCFCK VGYTTDISGT ACVDLDECSQ SPKPCNFICK NTKGSYQCSC PRGYVLQEDG
KTCKDLDECQ TKQHNCQFLC VNTLGGFTCK CPPGFTQHHT ACIDNNECGS QPSLCGAKGI
CQNTPGSFSC ECQRGFSLDA SGLNCEDVDE CDGNHRCQHG CQNILGGYRC GCPQGYVQHY
QWNQCVDENE CSNPGACGSA SCYNTLGSYK CACPSGFSFD QFSSACHDVN ECSSSKNPCS
YGCSNTEGGY LCGCPPGYFR VGQGHCVSGM GFNKGQYLSV DAEAEDDENA LSPEACYECK
INGYTKKDGR RKRSAQEPEP ASAEEQISLE SVAMDSPVNM KFNLSGLGSK EHILELVPAI
EPLNNHIRYV ISQGNEDGVF RIHQRNGLSY LHTAKKKLAP GTYTLEITSI PLYGKKELRK
LEEHNEDDYL LGVLGEALRM RLQIQLY
