HMCN1_MOUSE
ID HMCN1_MOUSE Reviewed; 5634 AA.
AC D3YXG0; D3Z2Q7;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Hemicentin-1 {ECO:0000312|MGI:MGI:2685047};
DE AltName: Full=Fibulin-6 {ECO:0000303|PubMed:24951538};
DE Short=FIBL-6 {ECO:0000303|PubMed:24951538};
DE Flags: Precursor;
GN Name=Hmcn1 {ECO:0000312|MGI:MGI:2685047};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17015624; DOI=10.1369/jhc.6a6975.2006;
RA Xu X., Dong C., Vogel B.E.;
RT "Hemicentins assemble on diverse epithelia in the mouse.";
RL J. Histochem. Cytochem. 55:119-126(2007).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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 [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21215633; DOI=10.1016/j.cub.2010.12.006;
RA Xu X., Vogel B.E.;
RT "A secreted protein promotes cleavage furrow maturation during
RT cytokinesis.";
RL Curr. Biol. 21:114-119(2011).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY
RP MYOCARDIAL INFARCTION.
RX PubMed=24951538; DOI=10.1093/cvr/cvu161;
RA Chowdhury A., Herzog C., Hasselbach L., Khouzani H.L., Zhang J.,
RA Hammerschmidt M., Rudat C., Kispert A., Gaestel M., Menon M.B.,
RA Tudorache I., Hilfiker-Kleiner D., Muehlfeld C., Schmitto J.D., Mueller M.,
RA Theilmeier G.;
RT "Expression of fibulin-6 in failing hearts and its role for cardiac
RT fibroblast migration.";
RL Cardiovasc. Res. 103:509-520(2014).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RX PubMed=29488390; DOI=10.1152/ajprenal.00198.2017;
RA Toffoli B., Zennaro C., Winkler C., Giordano Attianese G.M.P., Bernardi S.,
RA Carraro M., Gilardi F., Desvergne B.;
RT "Hemicentin 1 influences podocyte dynamic changes in glomerular diseases.";
RL Am. J. Physiol. 314:F1154-F1165(2018).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=32035013; DOI=10.1002/dvdy.159;
RA Lin M.H., Pope B.D. III, Sasaki T., Keeley D.P., Sherwood D.R., Miner J.H.;
RT "Mammalian hemicentin 1 is assembled into tracks in the extracellular
RT matrix of multiple tissues.";
RL Dev. Dyn. 249:775-788(2020).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=34504132; DOI=10.1038/s41598-021-96824-4;
RA Welcker D., Stein C., Feitosa N.M., Armistead J., Zhang J.L., Luetke S.,
RA Kleinridders A., Bruening J.C., Eming S.A., Sengle G., Niehoff A.,
RA Bloch W., Hammerschmidt M.;
RT "Hemicentin-1 is an essential extracellular matrix component of the dermal-
RT epidermal and myotendinous junctions.";
RL Sci. Rep. 11:17926-17926(2021).
CC -!- FUNCTION: Involved in transforming growth factor beta-mediated
CC rearrangement of the podocyte cytoskeleton which includes reduction of
CC F-actin fibers and broadening, flattening and elongation of podocytes
CC (By similarity). Plays a role in basement membrane organization
CC (PubMed:34504132). May promote cleavage furrow maturation during
CC cytokinesis in preimplantation embryos (PubMed:21215633). May play a
CC role in the architecture of adhesive and flexible epithelial cell
CC junctions (PubMed:17015624). May play a role during myocardial
CC remodeling by imparting an effect on cardiac fibroblast migration
CC (PubMed:24951538). {ECO:0000250|UniProtKB:Q96RW7,
CC ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:21215633,
CC ECO:0000269|PubMed:24951538, ECO:0000269|PubMed:34504132}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:17015624,
CC ECO:0000269|PubMed:24951538, ECO:0000269|PubMed:29488390,
CC ECO:0000269|PubMed:32035013, ECO:0000269|PubMed:34504132}. Cytoplasm
CC {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:29488390}. Cell
CC junction {ECO:0000269|PubMed:17015624}. Cleavage furrow
CC {ECO:0000269|PubMed:21215633}. Note=Has been detected in the glomerular
CC basement membrane in one study (PubMed:29488390). However, another
CC study found expression in the glomerular mesangial matrix but not in
CC the glomerular basement membrane (PubMed:32035013). The antibody used
CC in PubMed:17015624 and PubMed:21215633 to determine subcellular
CC location does not distinguish between HMCN1 and HMCN2 (PubMed:17015624,
CC PubMed:21215633). {ECO:0000269|PubMed:17015624,
CC ECO:0000269|PubMed:21215633, ECO:0000269|PubMed:29488390,
CC ECO:0000269|PubMed:32035013}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=D3YXG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=D3YXG0-2; Sequence=VSP_058526;
CC -!- TISSUE SPECIFICITY: In the kidney, expressed in the glomerulus (at
CC protein level) (PubMed:29488390, PubMed:32035013). Expressed in whisker
CC and hair follicles, eye, tongue, and splenic and lymph node conduits
CC (at protein level) (PubMed:32035013). In the embryo, localizes to the
CC cleavage furrow at the two-cell stage (at protein level)
CC (PubMed:34504132). In neonatal skin, expressed throughout the dermis
CC (at protein level) (PubMed:34504132). In adult skin, strongly
CC concentrated at the dermal side of the basement membrane but not
CC detectable in the deeper dermis (PubMed:34504132). Shows tendon-
CC specific localization at the myotendinous junction and is also detected
CC in the perichondrium (at protein level) (PubMed:34504132). Expressed by
CC chondrocytes residing in articular cartilage and the femoral growth
CC plate of 52 week old mice (at protein level) (PubMed:34504132).
CC Expressed in vascular endothelial cells in coronary arteries and
CC sparsely in endocardial endothelium (at protein level)
CC (PubMed:24951538). Expressed in skin, tongue, lung and eye
CC (PubMed:17015624). At E14.5, expressed in the vibrissae, dermis,
CC forelimb, kidney, intestine, lung and iliac cartilage where expression
CC is found mainly in mesenchymal cells (PubMed:34504132).
CC {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:24951538,
CC ECO:0000269|PubMed:29488390, ECO:0000269|PubMed:32035013,
CC ECO:0000269|PubMed:34504132}.
CC -!- DEVELOPMENTAL STAGE: Expression increases with age from 3 weeks to 15-
CC 20 weeks (at protein level). {ECO:0000269|PubMed:29488390}.
CC -!- INDUCTION: Induced by high glucose and transforming growth factor beta
CC (at protein level) (PubMed:29488390). Following wounding, up-regulated
CC in the dermis adjacent to the epidermal tongues of closing wounds (at
CC protein level) (PubMed:34504132). Up-regulated following myocardial
CC infarction. {ECO:0000269|PubMed:24951538, ECO:0000269|PubMed:29488390,
CC ECO:0000269|PubMed:34504132}.
CC -!- DISRUPTION PHENOTYPE: Mutants are viable and fertile with no gross
CC phenotypes (PubMed:32035013, PubMed:34504132). Ultrastructural basement
CC membrane alterations are observed at dermal-epidermal and myotendinous
CC junctions (PubMed:34504132). However, another study showed that embryos
CC arrest between the one- and four-cell stages with cleavage furrows that
CC form but fail to ingress and often retract prior to completion,
CC resulting in multinucleate cells (PubMed:21215633). Double knockout of
CC Hmcn1 and Hmcn2 results in no overt phenotypes with mice being viable
CC and fertile (PubMed:32035013). {ECO:0000269|PubMed:21215633,
CC ECO:0000269|PubMed:32035013, ECO:0000269|PubMed:34504132}.
CC -!- CAUTION: Has been shown in one study to play a role in cleavage furrow
CC maturation during cytokinesis (PubMed:21215633). However, other studies
CC have shown no role in this process (PubMed:32035013, PubMed:34504132).
CC {ECO:0000269|PubMed:21215633, ECO:0000269|PubMed:32035013,
CC ECO:0000269|PubMed:34504132}.
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DR EMBL; AC111145; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC115051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS15357.2; -. [D3YXG0-1]
DR RefSeq; NP_001019891.2; NM_001024720.3. [D3YXG0-1]
DR STRING; 10090.ENSMUSP00000074340; -.
DR GlyGen; D3YXG0; 8 sites.
DR iPTMnet; D3YXG0; -.
DR PhosphoSitePlus; D3YXG0; -.
DR MaxQB; D3YXG0; -.
DR PaxDb; D3YXG0; -.
DR PRIDE; D3YXG0; -.
DR ProteomicsDB; 273181; -. [D3YXG0-1]
DR ProteomicsDB; 273182; -. [D3YXG0-2]
DR Antibodypedia; 63332; 22 antibodies from 11 providers.
DR Ensembl; ENSMUST00000074783; ENSMUSP00000074340; ENSMUSG00000066842. [D3YXG0-1]
DR Ensembl; ENSMUST00000137197; ENSMUSP00000121500; ENSMUSG00000066842. [D3YXG0-2]
DR GeneID; 545370; -.
DR KEGG; mmu:545370; -.
DR UCSC; uc007cyj.1; mouse. [D3YXG0-1]
DR CTD; 83872; -.
DR MGI; MGI:2685047; Hmcn1.
DR VEuPathDB; HostDB:ENSMUSG00000066842; -.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT00940000154614; -.
DR InParanoid; D3YXG0; -.
DR OMA; MIEIRNP; -.
DR OrthoDB; 38313at2759; -.
DR PhylomeDB; D3YXG0; -.
DR BioGRID-ORCS; 545370; 1 hit in 72 CRISPR screens.
DR PRO; PR:D3YXG0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; D3YXG0; protein.
DR Bgee; ENSMUSG00000066842; Expressed in manus and 176 other tissues.
DR ExpressionAtlas; D3YXG0; baseline and differential.
DR Genevisible; D3YXG0; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0030054; C:cell junction; IDA:MGI.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005927; C:muscle tendon junction; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0090527; P:actin filament reorganization; ISS:UniProtKB.
DR GO; GO:0071711; P:basement membrane organization; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR CDD; cd00255; nidG2; 1.
DR Gene3D; 2.20.100.10; -; 5.
DR Gene3D; 2.40.155.10; -; 1.
DR Gene3D; 2.60.40.10; -; 44.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR006605; G2_nidogen/fibulin_G2F.
DR InterPro; IPR009017; GFP.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 6.
DR Pfam; PF07474; G2F; 1.
DR Pfam; PF07679; I-set; 34.
DR Pfam; PF00090; TSP_1; 6.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 8.
DR SMART; SM00682; G2F; 1.
DR SMART; SM00409; IG; 44.
DR SMART; SM00408; IGc2; 44.
DR SMART; SM00406; IGv; 14.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF48726; SSF48726; 44.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF54511; SSF54511; 1.
DR SUPFAM; SSF57184; SSF57184; 3.
DR SUPFAM; SSF82895; SSF82895; 6.
DR PROSITE; PS00010; ASX_HYDROXYL; 5.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 8.
DR PROSITE; PS50835; IG_LIKE; 43.
DR PROSITE; PS50993; NIDOGEN_G2; 1.
DR PROSITE; PS50092; TSP1; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Calcium; Cell cycle;
KW Cell division; Cell junction; Cytoplasm; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..5634
FT /note="Hemicentin-1"
FT /evidence="ECO:0000255"
FT /id="PRO_5003053106"
FT DOMAIN 41..216
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 431..517
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 520..607
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 612..697
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 702..788
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 793..883
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 890..976
FT /note="Ig-like C2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 981..1067
FT /note="Ig-like C2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1072..1166
FT /note="Ig-like C2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1171..1254
FT /note="Ig-like C2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1261..1353
FT /note="Ig-like C2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1357..1446
FT /note="Ig-like C2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1451..1540
FT /note="Ig-like C2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1545..1633
FT /note="Ig-like C2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1638..1723
FT /note="Ig-like C2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1732..1820
FT /note="Ig-like C2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1825..1913
FT /note="Ig-like C2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 1918..2006
FT /note="Ig-like C2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2011..2096
FT /note="Ig-like C2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2103..2189
FT /note="Ig-like C2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2194..2284
FT /note="Ig-like C2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2289..2378
FT /note="Ig-like C2-type 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2383..2472
FT /note="Ig-like C2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2477..2565
FT /note="Ig-like C2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2570..2661
FT /note="Ig-like C2-type 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2665..2762
FT /note="Ig-like C2-type 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2765..2863
FT /note="Ig-like C2-type 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2867..2958
FT /note="Ig-like C2-type 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 2962..3050
FT /note="Ig-like C2-type 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3055..3145
FT /note="Ig-like C2-type 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3155..3227
FT /note="Ig-like C2-type 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3244..3334
FT /note="Ig-like C2-type 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3339..3428
FT /note="Ig-like C2-type 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3433..3515
FT /note="Ig-like C2-type 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3526..3614
FT /note="Ig-like C2-type 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3619..3707
FT /note="Ig-like C2-type 35"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3712..3798
FT /note="Ig-like C2-type 36"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3803..3891
FT /note="Ig-like C2-type 37"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3896..3982
FT /note="Ig-like C2-type 38"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 3987..4073
FT /note="Ig-like C2-type 39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 4077..4163
FT /note="Ig-like C2-type 40"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 4168..4252
FT /note="Ig-like C2-type 41"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 4259..4332
FT /note="Ig-like C2-type 42"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 4347..4434
FT /note="Ig-like C2-type 43"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 4439..4526
FT /note="Ig-like C2-type 44"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 4528..4583
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 4585..4640
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 4642..4697
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 4699..4754
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 4756..4811
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 4813..4868
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 4870..5092
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00348"
FT DOMAIN 5106..5145
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 5146..5189
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 5191..5228
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 5229..5269
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 5271..5306
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 5314..5354
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 5431..5470
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 615
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1292
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1386
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1639
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1826
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3151
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3897
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4379
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT DISULFID 451..499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 541..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 633..681
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 723..772
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 814..867
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 911..960
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1002..1051
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1101..1150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1192..1240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1287..1337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1381..1430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1474..1524
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1568..1617
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1662..1711
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1755..1804
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1847..1897
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1941..1990
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2032..2082
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2124..2173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2217..2268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2313..2362
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2407..2456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2500..2549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2596..2645
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2695..2744
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2798..2847
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2893..2942
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 2985..3034
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3080..3129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3172..3223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3267..3318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3363..3412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3456..3505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3549..3598
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3642..3691
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3733..3782
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3824..3875
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 3917..3966
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4008..4057
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4099..4147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4189..4238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4280..4327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4370..4418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4460..4508
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 4540..4577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4544..4582
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4555..4567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4597..4634
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4601..4639
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4612..4624
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4654..4691
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4658..4696
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4669..4681
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4711..4748
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4715..4753
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4726..4738
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4768..4805
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4772..4810
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4783..4795
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4825..4862
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4829..4867
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 4840..4852
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 5110..5120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 5116..5129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 5131..5144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 5195..5205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 5201..5214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 5216..5227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 5275..5288
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 5282..5297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 5318..5329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 5325..5338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 5340..5353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 5435..5445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 5441..5454
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 5456..5469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 5316..5432
FT /note="Missing (in isoform 2)"
FT /id="VSP_058526"
SQ SEQUENCE 5634 AA; 611561 MW; 38F277C227773C1C CRC64;
MIAQEVVHTV FLVALFRSSL AGDGTPQSES RAEEIPEGAS TLAFVFDVTG SMYDDLVQVI
EGASKILETS LKRPKRPLYN FALVPFHDPE IGPVTITTDP KKFQYELREL YVQGGGDCPE
MSIGAIKIAL EISLPGSFIY VFTDARSKDY RLTHEVLQLI QQKQSQVVFV LTGDCDDRNH
IGYKVYEEIA STSSGQVFHL DKKQVNEVLK WVEEAVQASK VHLLSTDHLE HAVNTWKIPF
DPSLKEVTVS LSGPSPVIEI RNPFGKLIKK GFGLNELLNI HNSAKVVNVK EPEAGMWTVK
TSSSGRHSVR ITGLSTIDFR AGFSRKPTLD FKKTMSRPVQ GIPTYVLLNT SGISSPARVD
RLELLSISGG SLKTIPVKHY PDRKPYGIWN ISDFIPPDEA FFLKVTGYDK DGYLFQRVSS
VSFSSIVPDA PKVTMPTRTL GYYLQPGQIL CSVESFLPFT LSFMRDGIAL GVDQYLRESA
SVNWDFTKVT LSDEGFYDCI AVSSAGTGRA QTFFDVSEPP PIIQLPNNVT VTPGERAVLA
CLVISAVDYN LTWQRSGRDI RLADSARIRT LANLSLELRS VKIGDAGEYR CVVSSEGGSA
AASVFLTVQE KPKVTVMPKN QSFTGGSEIS IMCSATGYPK PKIVWTMNEM FIMGSHRYRM
TSEGTLFIKN AVPKDAGTYA CLASNAAGTD KQTSTLRYIE APKLVVEQSE LLVALGDTTV
MECKTSGIPP PQVKWFKGDL ELRPSTFLSI DPLVGLLKIQ ETQDLDAGDY TCVAINEAGR
ATGRLTLDVG SPPVFIQEPS DVAVEIGSNV TLPCYVQGYP EPKIKWRRLD NMPVFSRPFS
VSFISQLRTG ALFISNLWAS DKGTYICEAE NQFGKIQSQT TVTVTGLVAP LIGISPSMAS
VIEGQPLTLP CTLLAGNPIP ERRWMKNSAM LVQNPYITVR SDGSLHIERV RLQDGGKYTC
VASNVAGTNN KTTSVAVHVL PSIQHGQQIL STIEGVPVTL PCRASGIPKP SITWSKKGEL
ISTSSAKFSA GADGSLYVVS PGSEESGEYI CTATNAAGYA KRKVQLTVYV RPRVFGDQRG
LSQDKPVEIS VLAGEEAILP CEAKSLPPPI ITWAKDSQLI SPFSPRHTFL PSGSMKITET
RVSDSGMYLC VATNIAGNVT QSVKLSVHVP PKIQHGNRHI KVQVGQRVDI LCNAHGSPPP
VITWFKSGRP FLDGAQHPGS PDGTLSIEQA VISDAGVYTC AATNIAGSDE AEVTLHVQEP
PSVEDLQPPF NTPFQERLAN QRIEFPCPAK GTPKPTIKWL HNGREVTGQE PGVSILEDGA
LLVIASVTPH NNGEYICVAV NEAGTTERKY NLKVHVPPVI RDKEHVTNVS VLTSQLASLY
CEVEGTPSPV ITWYKDDIQV TESSTVQIVN NGKILKLFKV SAEDAGRYSC KAINIAGTSQ
KDFSVNVLVP PSILGASSPS EVSVVLNHNV TLQCPGTGVP FPAIHWFKDG KPLFLGDPNI
ELSDRGQSLH LRNARRSDKG RYQCTVSNAA GKQAKDIKLT VYVPPSIKGG NITTEISALL
NSIVKLECET RGLPVPAITW YKDGQVVTSS SQALYIDKGQ LLHIQRAQVS DSATYTCHAA
NVAGTAEKSF HVDIYVPPTI EGDLTAPSNK QVIIGQSLIL ECKAAGNPPP ILTWLKDGVP
VKASDNIHIE AGGKKLEILS ALEVDRGQYI CVATSVAGER EIKYEVDVLV PPAVEGGEET
SYFIVLANNL LELDCQVSGS PPPTIMWLKG GQLIDERDGF KILLNGRKLV IAQAQVSDTG
LYQCVATNIA GDHRKEFEVT VHVPPTIKSS DLPEKTVVRY KPVTLQCIAN GIPNPSITWL
KDDQPVNTAH GNLKIQSSGR VLQIAKALLE DAGRYTCVAT NAAGEAHQHT QLHVHEPPSL
DDAGKMRNET VVVNNPIQLE CKATGKPLPV ITWYKDSHPL SGSASAAFLK RGQVLEIGSA
QISDAGIYKC VAINSAGATE LFYSLQVHVP PSISGSSSMV EVVVNNLARL ECEARGIPAP
SLTWLKDGSP VSSFSNGIQI LSGGRILALT SAQMSDAGRY TCVAVNAAGE KQRDIDLRVY
APPNIMGEEQ NVSVLIGQAV ELFCQSDAVP PPTLMWLKDG RPLLKRPGLS ISENGSVLKI
EDAQAGDTGR YTCEATNVAG KTEKNYNVNV WVPPSIYGSD ELVQLTAIEG NLITLLCESS
GIPPPDLTWK KKGSLVLADS AGRVHILSGG RRLQISIAEK ADAGLYTCVA SNVAGVAKKE
YNLQVYIRPS ITNSGGHRPE ITVIRGKSIS LECEVQGIPQ PTVTWMKDGR PLTKGKGVEI
LDEGRILQLK NVHVSDTGRY VCVAVNVAGM TDKRYDLSVH APPSIIGNHG VPENVSVVEK
SSVSLTCEAS GIPLPSITWL KDGWPVNLGS SVKILSGGRM LRLMQTRPED AGQYTCIVRN
AAGEDRKMFG LSVLVPPHIV GENTLEDVKI KEKQSVTLTC EVRGNPVPQI TWHKDGQLLQ
EDEAHHMMSG GRFLQITNAQ VSHTGRYTCL ASNIAGDKSK SFRLNVFVSP TIAGVDSDGS
PEDVIVILNS PTSLVCEAYS YPPATITWFK DGTPLESNRN IRILPGGRTL QILNAQEDNA
GRYSCVATNE AGEKIKHYEV KVYIPPIIKK GDLLGPGLSP KEVKIRVNSS LTLECEAYAI
PSASLRWYKD GQPLKSDDHV TIAASGHTLQ IKEAQISDTG RYTCVASNLA GEDELDFDVN
IQVPPSFQKL WEIGNMLDTG RSGEAKDVII NNPLSLHCET NAAPPPTLTW YKDGRPLTSS
DRVLILPGGR VLQIPRAKVE DAGRYTCVAV NEAGEDSLRY DVHVLLPPVI KGANSDLPEE
VTVLVNKSTQ MECSSSGNPA PRNYWQKDGQ ILLEDEHHKF QSDGRSLQIL NAQITDTGRY
VCVAENTAGS AKKYFNLNVH VPPSVIGPNH EHLSVVVNHF ISLNCEVSGF PPPDLSWLKN
EEPIKPNTNV LTVPGGRTLQ IIRAKISDGG DYTCIAINQA GESKKKVSLT VHVPPSIKDH
GSQSLSIVNV REGTSVSLEC ESNAVPPPVI TWSKNGRMIP DSTNVEILTG GQTLHIRRAE
VSDTGQYVCR AINVAGRDDK NFHLNVYVPP TIEGPETEVI VETISNPVTL TCDATGIPPP
TITWLKNHKP IENSDPLEVH ILSGGSKLQI ARPQRSNSGN YTCVASNMEG KAQKNFILFI
QVPPSVAGAE VPSEVSVLLG ENVELVCNAD GIPTPHLQWL RDGKPIVNGE TERVRVTTDG
STLNIYRALT SDMGKYTCVA TNPAGEEDRI FNLNVYVPPK IRGNKEEAEK LMALVDTSIN
IECKATGTPP PQINWLKNGL PLPISSHIRL LSAGQVVRIV RAQVSDIAVY TCVASNRAGV
DSKHYSLQVF VPPNMDNAMG TEEITIVKGS STSMTCFTDG TPAPSMSWLR DGQPLAPDAH
LTVSTQGMVL QLIKAETEDT GKYTCVATNE AGEVSKHFVL KVLEPPHING SEGPGEVSVI
VNNPLELSCI ASGIPAPKIS WMKDGRPFLQ TEQVQTLEGG AILRVSSAQV EDTGRYTCLA
SSPAGDDDKE YLVRVHVPPN IAGMDEAQDF TVLRNRQVTL ECKSDAVPPP VIMWLKNREQ
LQATPRVRIL SGGRYLQINN ADLGDTANYT CVASNIAGKT TREFNLTVNV PPSIGGGPQS
LVTLLNKSIA LECRAEGVPA PRITWRKDGV VLAESHARYS ILENGFLHIE SAHVTDTGRY
LCMATNVAGT DRRRIDLQVH VPPSIAMGPT NVTVTVNVQT TLACEATGIP KPSVTWRKNG
HLLNVDQNQN SYRLLSSGSL VIISPSVDDT ASYECTVTSD AGEDKRAVDL TVQVPPTIAD
EPMDFLVTRQ APAVMTCSAS GVPVPSIHWT KNGLRLLPRG DGYRILSSGA IEIPTTQLNH
AGRYTCVARN AAGSAHRHVT LRVQEPPVIQ PQPSELDVIL NNPILLPCEA TGIPTPFITW
QKEGINVITS GKSLAILPSG SLQISRAVRG DAGTYMCVAQ NPAGTALGKV KLNVQVPPVI
SSHQKEYVVT MDKPVSLLCE TEGSPPPDIT WHKDGHALTE SIRQRILNSG ALQIAFAQPD
DAGQYTCMAA NMAGSSSVSS TLTVHVPPRI QSTEVHFTVN ENSQAVLPCV ADGIPTPAIH
WEKDGVLIAN LLGKYTAQPY GELILENVVL EDSGTYTCVA NNAAGEDTRI VTLAVHTLPT
FTELPGDLSL NKGEQLRLSC KAVGIPLPKL TWTFNNNIIP AHFDSINGHS ELVIEKVSKE
DSGTYVCTAE NSVGFVKAIG FVYVKEPPVF KGDYPSNWIE PLGGNAILNC EVKGDPAPTI
QWSRKGADIE ISHRIRQLGN GSLAIYGTVN EDAGDYTCVA ANEAGMVERS MSLTLQSSPI
ITLEPVETVV DAGGRVILDC QAAGEPQPTI TWSRQGQPIS WDNRLSMLPN SSLYIAAARK
EDTSEYECVA RNLMGSVLVR VPVIVQVHGG FSLWSAWRPC SVTCGKGIQK RSRLCDNPPP
ANGGRPCQGA DSEARHCHNK LCPVDGHWSE WSFWEDCSRS CGHGNQTRTR TCSNPPAQHG
GRPCEGHAVE TIMCNIRPCP VHGVWNAWQP WSACSKSCGK GSQTRMRLCN NPPPSFGGAH
CSGAETQMQV CNERHCPVDG RWATWSSWSA CTVSCGGGAR KRTRDCSDPV PQYGGNKCEG
TGVQSDFCNS DPCPTHGNWS PWSGWGTCSR TCNGGQMRRY RTCDNPRPSN GGRACGGPDT
QIQRCNTDMC PVDGSWGTWH SWSHCSVSCG GGERTRKRLC DNPVPTKGGR SCPGDATQVS
RCNMQACPGG PQRARGSVIG NINDIEFGIA FLNATITDSP NTDTRVIQAK ITNVPRSLGP
AMRKIISILN PIYWTTAKEI GEAVNGFTLT NAVFKRETQV EFATGEVLRM THVARGLDSD
GALLLDVIVS GQVLQLHSPA EVGVKDYTED YIQTGPGQLY AYSTRLFTID GISIPYTWNH
TIFYDQAWGK MPFLVETLHA SSIESDYNQL EETLGFKIHA SISKGDRSNQ CPSGFILDSV
GPFCADEDEC TAGNPCSHTC HNAIGAYYCS CPKGLTIAAD GRTCQDIDEC ALGGHTCRAG
QDCDNTIGSY RCVVHCGTGF RRTSDGLSCQ DINECQESSP CHQRCFNVIG SFHCGCEAGY
QLKGRKCIDV NECRQNVCRP DQHCKNTRGG YKCIDLCPSG MTKAENGTCI DIDECKDGTH
QCRYNQICEN TRGSYRCACP RGYRSQGVGR PCIDINECEQ VPKPCAHQCS NSPGSFKCIC
LPGQQLLGDG KSCAGLERLS NYGTQYSSYT LERFSPVRSD YQPSQHYRQY SQLYSSYSEY
RNSRASFSRN RRTIRKTCPE GSEANHETCV DIDECQNRDT CQHECKNTIG SYQCVCPPGY
RLMLNGKTCQ DVDECLEQNV RCGPNRMCFN MRGSYQCIDT PCPPNYQRDP VLGFCLKNCP
PNDLECTLSP YALEYKLVSL PFGIAANQDL IRLVAYTQDG VMHPRTTFLM IDEEPAVPFA
LRDENLKGVV YTTRPLREAE TYRMKVGALS YSANGTIEYQ TTFIVYIAVS AYPY
