HMCN1_HUMAN
ID HMCN1_HUMAN Reviewed; 5635 AA.
AC Q96RW7; A6NGE3; Q5TYR7; Q96DN3; Q96DN8; Q96SC3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Hemicentin-1;
DE AltName: Full=Fibulin-6;
DE Short=FIBL-6;
DE Flags: Precursor;
GN Name=HMCN1; Synonyms=FIBL6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-2418.
RA Trent J.;
RT "Human hemicentin gene.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 892-2181.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2963-5635.
RC TISSUE=Melanoma;
RA Kostka G., Timpl R.;
RT "Partial sequence of fibulin-6 with a C-terminal region related to domain
RT II and III of the fibulin family.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND 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 [6]
RP TISSUE SPECIFICITY.
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 [7]
RP VARIANT ARMD1 ARG-5345, VARIANTS VAL-1624; ILE-2327; THR-2418; GLY-2893;
RP TYR-4084; THR-4720 AND VAL-5087, TISSUE SPECIFICITY, AND ALTERNATIVE
RP SPLICING (ISOFORM 2).
RX PubMed=14570714; DOI=10.1093/hmg/ddg348;
RA Schultz D.W., Klein M.L., Humpert A.J., Luzier C.W., Persun V., Schain M.,
RA Mahan A., Runckel C., Cassera M., Vittal V., Doyle T.M., Martin T.M.,
RA Weleber R.G., Francis P.J., Acott T.S.;
RT "Analysis of the ARMD1 locus: evidence that a mutation in hemicentin-1 is
RT associated with age-related macular degeneration in a large family.";
RL Hum. Mol. Genet. 12:3315-3323(2003).
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 (PubMed:29488390). Plays a role in basement membrane organization (By
CC similarity). May promote cleavage furrow maturation during cytokinesis
CC in preimplantation embryos (By similarity). May play a role in the
CC architecture of adhesive and flexible epithelial cell junctions (By
CC similarity). May play a role during myocardial remodeling by imparting
CC an effect on cardiac fibroblast migration (By similarity).
CC {ECO:0000250|UniProtKB:D3YXG0, ECO:0000269|PubMed:29488390}.
CC -!- INTERACTION:
CC Q96RW7; P0C7Q2: ARMS2; NbExp=4; IntAct=EBI-2806183, EBI-21986906;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000250|UniProtKB:D3YXG0}. Cytoplasm
CC {ECO:0000250|UniProtKB:D3YXG0}. Cell junction
CC {ECO:0000250|UniProtKB:D3YXG0}. Cleavage furrow
CC {ECO:0000250|UniProtKB:D3YXG0}. Note=Has been detected in the
CC glomerular basement membrane in one study. However, another study found
CC expression in the glomerular mesangial matrix but not in the glomerular
CC basement membrane. The antibody used to determine subcellular location
CC does not distinguish between HMCN1 and HMCN2.
CC {ECO:0000250|UniProtKB:D3YXG0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96RW7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96RW7-2; Sequence=VSP_016874;
CC Name=3;
CC IsoId=Q96RW7-3; Sequence=VSP_016871, VSP_016872, VSP_016873;
CC -!- TISSUE SPECIFICITY: Expressed in hair follicles and in the dermis (at
CC protein level). {ECO:0000269|PubMed:32035013}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Expressed in skin fibroblasts and
CC retinal pigment epithelium (RPE) cells. {ECO:0000269|PubMed:14570714}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in skin fibroblasts and
CC retinal pigment epithelium (RPE) cells. {ECO:0000269|PubMed:14570714}.
CC -!- INDUCTION: Induced by high glucose levels and transforming growth
CC factor beta (at protein level). {ECO:0000269|PubMed:29488390}.
CC -!- DISEASE: Macular degeneration, age-related, 1 (ARMD1) [MIM:603075]: A
CC form of age-related macular degeneration, a multifactorial eye disease
CC and the most common cause of irreversible vision loss in the developed
CC world. In most patients, the disease is manifest as ophthalmoscopically
CC visible yellowish accumulations of protein and lipid that lie beneath
CC the retinal pigment epithelium and within an elastin-containing
CC structure known as Bruch membrane. {ECO:0000269|PubMed:14570714}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- CAUTION: Has been shown in one study to play a role in cleavage furrow
CC maturation during cytokinesis. However, other studies have shown no
CC role in this process. {ECO:0000250|UniProtKB:D3YXG0}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71154.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB71216.1; Type=Erroneous initiation; 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; AF156100; AAK68690.1; -; mRNA.
DR EMBL; AK056336; BAB71154.1; ALT_SEQ; mRNA.
DR EMBL; AK056557; BAB71216.1; ALT_INIT; mRNA.
DR EMBL; AL118512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL135796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL135797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX928748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ306906; CAC37630.1; -; mRNA.
DR CCDS; CCDS30956.1; -. [Q96RW7-1]
DR RefSeq; NP_114141.2; NM_031935.2. [Q96RW7-1]
DR RefSeq; XP_011508340.1; XM_011510038.2. [Q96RW7-2]
DR BioGRID; 123785; 9.
DR IntAct; Q96RW7; 9.
DR STRING; 9606.ENSP00000271588; -.
DR CarbonylDB; Q96RW7; -.
DR GlyConnect; 1306; 1 N-Linked glycan (1 site).
DR GlyGen; Q96RW7; 35 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q96RW7; -.
DR PhosphoSitePlus; Q96RW7; -.
DR BioMuta; HMCN1; -.
DR DMDM; 85542049; -.
DR EPD; Q96RW7; -.
DR jPOST; Q96RW7; -.
DR MassIVE; Q96RW7; -.
DR MaxQB; Q96RW7; -.
DR PaxDb; Q96RW7; -.
DR PeptideAtlas; Q96RW7; -.
DR PRIDE; Q96RW7; -.
DR ProteomicsDB; 78045; -. [Q96RW7-1]
DR ProteomicsDB; 78046; -. [Q96RW7-2]
DR ProteomicsDB; 78047; -. [Q96RW7-3]
DR Antibodypedia; 63332; 22 antibodies from 11 providers.
DR DNASU; 83872; -.
DR Ensembl; ENST00000271588.9; ENSP00000271588.4; ENSG00000143341.12. [Q96RW7-1]
DR GeneID; 83872; -.
DR KEGG; hsa:83872; -.
DR MANE-Select; ENST00000271588.9; ENSP00000271588.4; NM_031935.3; NP_114141.2.
DR UCSC; uc001grq.2; human. [Q96RW7-1]
DR CTD; 83872; -.
DR DisGeNET; 83872; -.
DR GeneCards; HMCN1; -.
DR HGNC; HGNC:19194; HMCN1.
DR HPA; ENSG00000143341; Tissue enhanced (lung).
DR MalaCards; HMCN1; -.
DR MIM; 603075; phenotype.
DR MIM; 608548; gene.
DR neXtProt; NX_Q96RW7; -.
DR OpenTargets; ENSG00000143341; -.
DR Orphanet; 279; NON RARE IN EUROPE: Age-related macular degeneration.
DR PharmGKB; PA142671679; -.
DR VEuPathDB; HostDB:ENSG00000143341; -.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT00940000154614; -.
DR HOGENOM; CLU_000087_0_0_1; -.
DR InParanoid; Q96RW7; -.
DR OMA; MIEIRNP; -.
DR OrthoDB; 38313at2759; -.
DR PhylomeDB; Q96RW7; -.
DR PathwayCommons; Q96RW7; -.
DR SignaLink; Q96RW7; -.
DR BioGRID-ORCS; 83872; 22 hits in 1074 CRISPR screens.
DR ChiTaRS; HMCN1; human.
DR GeneWiki; HMCN1; -.
DR GenomeRNAi; 83872; -.
DR Pharos; Q96RW7; Tbio.
DR PRO; PR:Q96RW7; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96RW7; protein.
DR Bgee; ENSG00000143341; Expressed in descending thoracic aorta and 139 other tissues.
DR ExpressionAtlas; Q96RW7; baseline and differential.
DR Genevisible; Q96RW7; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005604; C:basement membrane; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005927; C:muscle tendon junction; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR GO; GO:0090527; P:actin filament reorganization; IMP:UniProtKB.
DR GO; GO:0071711; P:basement membrane organization; ISS: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; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00255; nidG2; 1.
DR Gene3D; 2.20.100.10; -; 6.
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; 15.
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; 44.
DR PROSITE; PS50993; NIDOGEN_G2; 1.
DR PROSITE; PS50092; TSP1; 6.
PE 1: Evidence at protein level;
KW Age-related macular degeneration; Alternative splicing; Basement membrane;
KW Calcium; Cell cycle; Cell division; Cell junction; Cytoplasm;
KW Disease variant; Disulfide bond; EGF-like domain; Extracellular matrix;
KW Glycoprotein; Immunoglobulin domain; Reference proteome; Repeat; Secreted;
KW Sensory transduction; Signal; Vision.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..5635
FT /note="Hemicentin-1"
FT /id="PRO_0000045391"
FT DOMAIN 41..216
FT /note="VWFA"
FT DOMAIN 431..517
FT /note="Ig-like C2-type 1"
FT DOMAIN 520..607
FT /note="Ig-like C2-type 2"
FT DOMAIN 612..697
FT /note="Ig-like C2-type 3"
FT DOMAIN 702..788
FT /note="Ig-like C2-type 4"
FT DOMAIN 793..883
FT /note="Ig-like C2-type 5"
FT DOMAIN 890..976
FT /note="Ig-like C2-type 6"
FT DOMAIN 981..1067
FT /note="Ig-like C2-type 7"
FT DOMAIN 1072..1166
FT /note="Ig-like C2-type 8"
FT DOMAIN 1171..1255
FT /note="Ig-like C2-type 9"
FT DOMAIN 1262..1354
FT /note="Ig-like C2-type 10"
FT DOMAIN 1358..1447
FT /note="Ig-like C2-type 11"
FT DOMAIN 1452..1541
FT /note="Ig-like C2-type 12"
FT DOMAIN 1546..1634
FT /note="Ig-like C2-type 13"
FT DOMAIN 1638..1724
FT /note="Ig-like C2-type 14"
FT DOMAIN 1733..1821
FT /note="Ig-like C2-type 15"
FT DOMAIN 1826..1914
FT /note="Ig-like C2-type 16"
FT DOMAIN 1919..2007
FT /note="Ig-like C2-type 17"
FT DOMAIN 2012..2097
FT /note="Ig-like C2-type 18"
FT DOMAIN 2104..2190
FT /note="Ig-like C2-type 19"
FT DOMAIN 2195..2285
FT /note="Ig-like C2-type 20"
FT DOMAIN 2290..2379
FT /note="Ig-like C2-type 21"
FT DOMAIN 2384..2470
FT /note="Ig-like C2-type 22"
FT DOMAIN 2478..2564
FT /note="Ig-like C2-type 23"
FT DOMAIN 2571..2662
FT /note="Ig-like C2-type 24"
FT DOMAIN 2666..2763
FT /note="Ig-like C2-type 25"
FT DOMAIN 2766..2864
FT /note="Ig-like C2-type 26"
FT DOMAIN 2868..2959
FT /note="Ig-like C2-type 27"
FT DOMAIN 2964..3051
FT /note="Ig-like C2-type 28"
FT DOMAIN 3056..3146
FT /note="Ig-like C2-type 29"
FT DOMAIN 3151..3240
FT /note="Ig-like C2-type 30"
FT DOMAIN 3245..3335
FT /note="Ig-like C2-type 31"
FT DOMAIN 3340..3429
FT /note="Ig-like C2-type 32"
FT DOMAIN 3434..3516
FT /note="Ig-like C2-type 33"
FT DOMAIN 3527..3615
FT /note="Ig-like C2-type 34"
FT DOMAIN 3620..3708
FT /note="Ig-like C2-type 35"
FT DOMAIN 3713..3797
FT /note="Ig-like C2-type 36"
FT DOMAIN 3804..3892
FT /note="Ig-like C2-type 37"
FT DOMAIN 3897..3983
FT /note="Ig-like C2-type 38"
FT DOMAIN 3988..4076
FT /note="Ig-like C2-type 39"
FT DOMAIN 4079..4164
FT /note="Ig-like C2-type 40"
FT DOMAIN 4169..4255
FT /note="Ig-like C2-type 41"
FT DOMAIN 4260..4344
FT /note="Ig-like C2-type 42"
FT DOMAIN 4348..4435
FT /note="Ig-like C2-type 43"
FT DOMAIN 4440..4527
FT /note="Ig-like C2-type 44"
FT DOMAIN 4529..4584
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 4586..4641
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 4643..4698
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 4700..4755
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 4757..4812
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 4814..4869
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 4871..5093
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00348"
FT DOMAIN 5107..5146
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 5147..5191
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 5192..5229
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 5230..5271
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 5272..5307
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 5315..5355
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 5432..5471
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 970
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2887
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2973
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3812
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4029
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4894
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5040
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 451..499
FT /evidence="ECO:0000250"
FT DISULFID 541..591
FT /evidence="ECO:0000250"
FT DISULFID 633..681
FT /evidence="ECO:0000250"
FT DISULFID 723..772
FT /evidence="ECO:0000250"
FT DISULFID 814..867
FT /evidence="ECO:0000250"
FT DISULFID 911..960
FT /evidence="ECO:0000250"
FT DISULFID 1002..1051
FT /evidence="ECO:0000250"
FT DISULFID 1101..1150
FT /evidence="ECO:0000250"
FT DISULFID 1192..1241
FT /evidence="ECO:0000250"
FT DISULFID 1288..1338
FT /evidence="ECO:0000250"
FT DISULFID 1382..1431
FT /evidence="ECO:0000250"
FT DISULFID 1475..1525
FT /evidence="ECO:0000250"
FT DISULFID 1569..1618
FT /evidence="ECO:0000250"
FT DISULFID 1663..1712
FT /evidence="ECO:0000250"
FT DISULFID 1756..1805
FT /evidence="ECO:0000250"
FT DISULFID 1848..1898
FT /evidence="ECO:0000250"
FT DISULFID 1942..1991
FT /evidence="ECO:0000250"
FT DISULFID 2033..2083
FT /evidence="ECO:0000250"
FT DISULFID 2125..2174
FT /evidence="ECO:0000250"
FT DISULFID 2218..2269
FT /evidence="ECO:0000250"
FT DISULFID 2314..2363
FT /evidence="ECO:0000250"
FT DISULFID 2408..2457
FT /evidence="ECO:0000250"
FT DISULFID 2501..2550
FT /evidence="ECO:0000250"
FT DISULFID 2597..2646
FT /evidence="ECO:0000250"
FT DISULFID 2696..2745
FT /evidence="ECO:0000250"
FT DISULFID 2799..2848
FT /evidence="ECO:0000250"
FT DISULFID 2894..2943
FT /evidence="ECO:0000250"
FT DISULFID 2986..3035
FT /evidence="ECO:0000250"
FT DISULFID 3081..3130
FT /evidence="ECO:0000250"
FT DISULFID 3173..3224
FT /evidence="ECO:0000250"
FT DISULFID 3268..3319
FT /evidence="ECO:0000250"
FT DISULFID 3364..3413
FT /evidence="ECO:0000250"
FT DISULFID 3457..3506
FT /evidence="ECO:0000250"
FT DISULFID 3550..3599
FT /evidence="ECO:0000250"
FT DISULFID 3643..3692
FT /evidence="ECO:0000250"
FT DISULFID 3734..3783
FT /evidence="ECO:0000250"
FT DISULFID 3825..3876
FT /evidence="ECO:0000250"
FT DISULFID 3918..3967
FT /evidence="ECO:0000250"
FT DISULFID 4009..4058
FT /evidence="ECO:0000250"
FT DISULFID 4100..4148
FT /evidence="ECO:0000250"
FT DISULFID 4190..4239
FT /evidence="ECO:0000250"
FT DISULFID 4281..4328
FT /evidence="ECO:0000250"
FT DISULFID 4371..4419
FT /evidence="ECO:0000250"
FT DISULFID 4461..4509
FT /evidence="ECO:0000250"
FT DISULFID 4541..4578
FT /evidence="ECO:0000250"
FT DISULFID 4545..4583
FT /evidence="ECO:0000250"
FT DISULFID 4556..4568
FT /evidence="ECO:0000250"
FT DISULFID 4598..4635
FT /evidence="ECO:0000250"
FT DISULFID 4602..4640
FT /evidence="ECO:0000250"
FT DISULFID 4613..4625
FT /evidence="ECO:0000250"
FT DISULFID 4655..4692
FT /evidence="ECO:0000250"
FT DISULFID 4659..4697
FT /evidence="ECO:0000250"
FT DISULFID 4670..4682
FT /evidence="ECO:0000250"
FT DISULFID 4712..4749
FT /evidence="ECO:0000250"
FT DISULFID 4716..4754
FT /evidence="ECO:0000250"
FT DISULFID 4727..4739
FT /evidence="ECO:0000250"
FT DISULFID 4769..4806
FT /evidence="ECO:0000250"
FT DISULFID 4773..4811
FT /evidence="ECO:0000250"
FT DISULFID 4784..4796
FT /evidence="ECO:0000250"
FT DISULFID 4826..4863
FT /evidence="ECO:0000250"
FT DISULFID 4830..4868
FT /evidence="ECO:0000250"
FT DISULFID 4841..4853
FT /evidence="ECO:0000250"
FT DISULFID 5111..5121
FT /evidence="ECO:0000250"
FT DISULFID 5117..5130
FT /evidence="ECO:0000250"
FT DISULFID 5132..5145
FT /evidence="ECO:0000250"
FT DISULFID 5196..5206
FT /evidence="ECO:0000250"
FT DISULFID 5202..5215
FT /evidence="ECO:0000250"
FT DISULFID 5217..5228
FT /evidence="ECO:0000250"
FT DISULFID 5276..5289
FT /evidence="ECO:0000250"
FT DISULFID 5283..5298
FT /evidence="ECO:0000250"
FT DISULFID 5319..5330
FT /evidence="ECO:0000250"
FT DISULFID 5326..5339
FT /evidence="ECO:0000250"
FT DISULFID 5341..5354
FT /evidence="ECO:0000250"
FT DISULFID 5436..5446
FT /evidence="ECO:0000250"
FT DISULFID 5442..5455
FT /evidence="ECO:0000250"
FT DISULFID 5457..5470
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..616
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016871"
FT VAR_SEQ 1169..1171
FT /note="VPP -> GES (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016872"
FT VAR_SEQ 1172..5635
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016873"
FT VAR_SEQ 5315..5431
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_016874"
FT VARIANT 1056
FT /note="T -> A (in dbSNP:rs7539719)"
FT /id="VAR_049875"
FT VARIANT 1184
FT /note="V -> F (in dbSNP:rs12239296)"
FT /id="VAR_049876"
FT VARIANT 1624
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:14570714"
FT /id="VAR_024811"
FT VARIANT 2327
FT /note="M -> I (in dbSNP:rs12067376)"
FT /evidence="ECO:0000269|PubMed:14570714"
FT /id="VAR_024812"
FT VARIANT 2418
FT /note="I -> T (in dbSNP:rs12129650)"
FT /evidence="ECO:0000269|PubMed:14570714, ECO:0000269|Ref.1"
FT /id="VAR_024813"
FT VARIANT 2893
FT /note="E -> G (in dbSNP:rs10798035)"
FT /evidence="ECO:0000269|PubMed:14570714"
FT /id="VAR_024814"
FT VARIANT 4084
FT /note="H -> Y (in dbSNP:rs41317489)"
FT /evidence="ECO:0000269|PubMed:14570714"
FT /id="VAR_024815"
FT VARIANT 4437
FT /note="Q -> R (in dbSNP:rs10911825)"
FT /id="VAR_049877"
FT VARIANT 4720
FT /note="A -> T (in dbSNP:rs6693069)"
FT /evidence="ECO:0000269|PubMed:14570714"
FT /id="VAR_024816"
FT VARIANT 5087
FT /note="D -> V (in dbSNP:rs41317507)"
FT /evidence="ECO:0000269|PubMed:14570714"
FT /id="VAR_024817"
FT VARIANT 5345
FT /note="Q -> R (in ARMD1; dbSNP:rs121434382)"
FT /evidence="ECO:0000269|PubMed:14570714"
FT /id="VAR_024818"
FT CONFLICT 35
FT /note="I -> F (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="N -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1042
FT /note="G -> E (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1078
FT /note="Q -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1153
FT /note="T -> I (in Ref. 2; BAB71216)"
FT /evidence="ECO:0000305"
FT CONFLICT 1319
FT /note="D -> E (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1368
FT /note="T -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1414
FT /note="K -> R (in Ref. 2; BAB71216)"
FT /evidence="ECO:0000305"
FT CONFLICT 1461
FT /note="N -> K (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1570
FT /note="E -> K (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1664
FT /note="K -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1688
FT /note="I -> F (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1775
FT /note="I -> V (in Ref. 2; BAB71216)"
FT /evidence="ECO:0000305"
FT CONFLICT 1816
FT /note="K -> E (in Ref. 2; BAB71216)"
FT /evidence="ECO:0000305"
FT CONFLICT 1959
FT /note="R -> C (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 2073
FT /note="A -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 2184
FT /note="E -> EK (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 2872
FT /note="K -> E (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 3189
FT /note="H -> Y (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 3355
FT /note="L -> Y (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 4136
FT /note="A -> T (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 4340
FT /note="I -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 4358
FT /note="N -> H (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 4699
FT /note="I -> V (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 5294
FT /note="G -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 5317
FT /note="N -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5635 AA; 613390 MW; 19AE01E5E2A27E2A CRC64;
MISWEVVHTV FLFALLYSSL AQDASPQSEI RAEEIPEGAS TLAFVFDVTG SMYDDLVQVI
EGASKILETS LKRPKRPLFN FALVPFHDPE IGPVTITTDP KKFQYELREL YVQGGGDCPE
MSIGAIKIAL EISLPGSFIY VFTDARSKDY RLTHEVLQLI QQKQSQVVFV LTGDCDDRTH
IGYKVYEEIA STSSGQVFHL DKKQVNEVLK WVEEAVQASK VHLLSTDHLE QAVNTWRIPF
DPSLKEVTVS LSGPSPMIEI RNPLGKLIKK GFGLHELLNI HNSAKVVNVK EPEAGMWTVK
TSSSGRHSVR ITGLSTIDFR AGFSRKPTLD FKKTVSRPVQ GIPTYVLLNT SGISTPARID
LLELLSISGS SLKTIPVKYY PHRKPYGIWN ISDFVPPNEA FFLKVTGYDK DDYLFQRVSS
VSFSSIVPDA PKVTMPEKTP GYYLQPGQIP CSVDSLLPFT LSFVRNGVTL GVDQYLKESA
SVNLDIAKVT LSDEGFYECI AVSSAGTGRA QTFFDVSEPP PVIQVPNNVT VTPGERAVLT
CLIISAVDYN LTWQRNDRDV RLAEPARIRT LANLSLELKS VKFNDAGEYH CMVSSEGGSS
AASVFLTVQE PPKVTVMPKN QSFTGGSEVS IMCSATGYPK PKIAWTVNDM FIVGSHRYRM
TSDGTLFIKN AAPKDAGIYG CLASNSAGTD KQNSTLRYIE APKLMVVQSE LLVALGDITV
MECKTSGIPP PQVKWFKGDL ELRPSTFLII DPLLGLLKIQ ETQDLDAGDY TCVAINEAGR
ATGKITLDVG SPPVFIQEPA DVSMEIGSNV TLPCYVQGYP EPTIKWRRLD NMPIFSRPFS
VSSISQLRTG ALFILNLWAS DKGTYICEAE NQFGKIQSET TVTVTGLVAP LIGISPSVAN
VIEGQQLTLP CTLLAGNPIP ERRWIKNSAM LLQNPYITVR SDGSLHIERV QLQDGGEYTC
VASNVAGTNN KTTSVVVHVL PTIQHGQQIL STIEGIPVTL PCKASGNPKP SVIWSKKGEL
ISTSSAKFSA GADGSLYVVS PGGEESGEYV CTATNTAGYA KRKVQLTVYV RPRVFGDQRG
LSQDKPVEIS VLAGEEVTLP CEVKSLPPPI ITWAKETQLI SPFSPRHTFL PSGSMKITET
RTSDSGMYLC VATNIAGNVT QAVKLNVHVP PKIQRGPKHL KVQVGQRVDI PCNAQGTPLP
VITWSKGGST MLVDGEHHVS NPDGTLSIDQ ATPSDAGIYT CVATNIAGTD ETEITLHVQE
PPTVEDLEPP YNTTFQERVA NQRIEFPCPA KGTPKPTIKW LHNGRELTGR EPGISILEDG
TLLVIASVTP YDNGEYICVA VNEAGTTERK YNLKVHVPPV IKDKEQVTNV SVLLNQLTNL
FCEVEGTPSP IIMWYKDNVQ VTESSTIQTV NNGKILKLFR ATPEDAGRYS CKAINIAGTS
QKYFNIDVLV PPTIIGTNFP NEVSVVLNRD VALECQVKGT PFPDIHWFKD GKPLFLGDPN
VELLDRGQVL HLKNARRNDK GRYQCTVSNA AGKQAKDIKL TIYIPPSIKG GNVTTDISVL
INSLIKLECE TRGLPMPAIT WYKDGQPIMS SSQALYIDKG QYLHIPRAQV SDSATYTCHV
ANVAGTAEKS FHVDVYVPPM IEGNLATPLN KQVVIAHSLT LECKAAGNPS PILTWLKDGV
PVKANDNIRI EAGGKKLEIM SAQEIDRGQY ICVATSVAGE KEIKYEVDVL VPPAIEGGDE
TSYFIVMVNN LLELDCHVTG SPPPTIMWLK DGQLIDERDG FKILLNGRKL VIAQAQVSNT
GLYRCMAANT AGDHKKEFEV TVHVPPTIKS SGLSERVVVK YKPVALQCIA NGIPNPSITW
LKDDQPVNTA QGNLKIQSSG RVLQIAKTLL EDAGRYTCVA TNAAGETQQH IQLHVHEPPS
LEDAGKMLNE TVLVSNPVQL ECKAAGNPVP VITWYKDNRL LSGSTSMTFL NRGQIIDIES
AQISDAGIYK CVAINSAGAT ELFYSLQVHV APSISGSNNM VAVVVNNPVR LECEARGIPA
PSLTWLKDGS PVSSFSNGLQ VLSGGRILAL TSAQISDTGR YTCVAVNAAG EKQRDIDLRV
YVPPNIMGEE QNVSVLISQA VELLCQSDAI PPPTLTWLKD GHPLLKKPGL SISENRSVLK
IEDAQVQDTG RYTCEATNVA GKTEKNYNVN IWVPPNIGGS DELTQLTVIE GNLISLLCES
SGIPPPNLIW KKKGSPVLTD SMGRVRILSG GRQLQISIAE KSDAALYSCV ASNVAGTAKK
EYNLQVYIRP TITNSGSHPT EIIVTRGKSI SLECEVQGIP PPTVTWMKDG HPLIKAKGVE
ILDEGHILQL KNIHVSDTGR YVCVAVNVAG MTDKKYDLSV HAPPSIIGNH RSPENISVVE
KNSVSLTCEA SGIPLPSITW FKDGWPVSLS NSVRILSGGR MLRLMQTTME DAGQYTCVVR
NAAGEERKIF GLSVLVPPHI VGENTLEDVK VKEKQSVTLT CEVTGNPVPE ITWHKDGQPL
QEDEAHHIIS GGRFLQITNV QVPHTGRYTC LASSPAGHKS RSFSLNVFVS PTIAGVGSDG
NPEDVTVILN SPTSLVCEAY SYPPATITWF KDGTPLESNR NIRILPGGRT LQILNAQEDN
AGRYSCVATN EAGEMIKHYE VKVYIPPIIN KGDLWGPGLS PKEVKIKVNN TLTLECEAYA
IPSASLSWYK DGQPLKSDDH VNIAANGHTL QIKEAQISDT GRYTCVASNI AGEDELDFDV
NIQVPPSFQK LWEIGNMLDT GRNGEAKDVI INNPISLYCE TNAAPPPTLT WYKDGHPLTS
SDKVLILPGG RVLQIPRAKV EDAGRYTCVA VNEAGEDSLQ YDVRVLVPPI IKGANSDLPE
EVTVLVNKSA LIECLSSGSP APRNSWQKDG QPLLEDDHHK FLSNGRILQI LNTQITDIGR
YVCVAENTAG SAKKYFNLNV HVPPSVIGPK SENLTVVVNN FISLTCEVSG FPPPDLSWLK
NEQPIKLNTN TLIVPGGRTL QIIRAKVSDG GEYTCIAINQ AGESKKKFSL TVYVPPSIKD
HDSESLSVVN VREGTSVSLE CESNAVPPPV ITWYKNGRMI TESTHVEILA DGQMLHIKKA
EVSDTGQYVC RAINVAGRDD KNFHLNVYVP PSIEGPEREV IVETISNPVT LTCDATGIPP
PTIAWLKNHK RIENSDSLEV RILSGGSKLQ IARSQHSDSG NYTCIASNME GKAQKYYFLS
IQVPPSVAGA EIPSDVSVLL GENVELVCNA NGIPTPLIQW LKDGKPIASG ETERIRVSAN
GSTLNIYGAL TSDTGKYTCV ATNPAGEEDR IFNLNVYVTP TIRGNKDEAE KLMTLVDTSI
NIECRATGTP PPQINWLKNG LPLPLSSHIR LLAAGQVIRI VRAQVSDVAV YTCVASNRAG
VDNKHYNLQV FAPPNMDNSM GTEEITVLKG SSTSMACITD GTPAPSMAWL RDGQPLGLDA
HLTVSTHGMV LQLLKAETED SGKYTCIASN EAGEVSKHFI LKVLEPPHIN GSEEHEEISV
IVNNPLELTC IASGIPAPKM TWMKDGRPLP QTDQVQTLGG GEVLRISTAQ VEDTGRYTCL
ASSPAGDDDK EYLVRVHVPP NIAGTDEPRD ITVLRNRQVT LECKSDAVPP PVITWLRNGE
RLQATPRVRI LSGGRYLQIN NADLGDTANY TCVASNIAGK TTREFILTVN VPPNIKGGPQ
SLVILLNKST VLECIAEGVP TPRITWRKDG AVLAGNHARY SILENGFLHI QSAHVTDTGR
YLCMATNAAG TDRRRIDLQV HVPPSIAPGP TNMTVIVNVQ TTLACEATGI PKPSINWRKN
GHLLNVDQNQ NSYRLLSSGS LVIISPSVDD TATYECTVTN GAGDDKRTVD LTVQVPPSIA
DEPTDFLVTK HAPAVITCTA SGVPFPSIHW TKNGIRLLPR GDGYRILSSG AIEILATQLN
HAGRYTCVAR NAAGSAHRHV TLHVHEPPVI QPQPSELHVI LNNPILLPCE ATGTPSPFIT
WQKEGINVNT SGRNHAVLPS GGLQISRAVR EDAGTYMCVA QNPAGTALGK IKLNVQVPPV
ISPHLKEYVI AVDKPITLSC EADGLPPPDI TWHKDGRAIV ESIRQRVLSS GSLQIAFVQP
GDAGHYTCMA ANVAGSSSTS TKLTVHVPPR IRSTEGHYTV NENSQAILPC VADGIPTPAI
NWKKDNVLLA NLLGKYTAEP YGELILENVV LEDSGFYTCV ANNAAGEDTH TVSLTVHVLP
TFTELPGDVS LNKGEQLRLS CKATGIPLPK LTWTFNNNII PAHFDSVNGH SELVIERVSK
EDSGTYVCTA ENSVGFVKAI GFVYVKEPPV FKGDYPSNWI EPLGGNAILN CEVKGDPTPT
IQWNRKGVDI EISHRIRQLG NGSLAIYGTV NEDAGDYTCV ATNEAGVVER SMSLTLQSPP
IITLEPVETV INAGGKIILN CQATGEPQPT ITWSRQGHSI SWDDRVNVLS NNSLYIADAQ
KEDTSEFECV ARNLMGSVLV RVPVIVQVHG GFSQWSAWRA CSVTCGKGIQ KRSRLCNQPL
PANGGKPCQG SDLEMRNCQN KPCPVDGSWS EWSLWEECTR SCGRGNQTRT RTCNNPSVQH
GGRPCEGNAV EIIMCNIRPC PVHGAWSAWQ PWGTCSESCG KGTQTRARLC NNPPPAFGGS
YCDGAETQMQ VCNERNCPIH GKWATWASWS ACSVSCGGGA RQRTRGCSDP VPQYGGRKCE
GSDVQSDFCN SDPCPTHGNW SPWSGWGTCS RTCNGGQMRR YRTCDNPPPS NGGRACGGPD
SQIQRCNTDM CPVDGSWGSW HSWSQCSASC GGGEKTRKRL CDHPVPVKGG RPCPGDTTQV
TRCNVQACPG GPQRARGSVI GNINDVEFGI AFLNATITDS PNSDTRIIRA KITNVPRSLG
SAMRKIVSIL NPIYWTTAKE IGEAVNGFTL TNAVFKRETQ VEFATGEILQ MSHIARGLDS
DGSLLLDIVV SGYVLQLQSP AEVTVKDYTE DYIQTGPGQL YAYSTRLFTI DGISIPYTWN
HTVFYDQAQG RMPFLVETLH ASSVESDYNQ IEETLGFKIH ASISKGDRSN QCPSGFTLDS
VGPFCADEDE CAAGNPCSHS CHNAMGTYYC SCPKGLTIAA DGRTCQDIDE CALGRHTCHA
GQDCDNTIGS YRCVVRCGSG FRRTSDGLSC QDINECQESS PCHQRCFNAI GSFHCGCEPG
YQLKGRKCMD VNECRQNVCR PDQHCKNTRG GYKCIDLCPN GMTKAENGTC IDIDECKDGT
HQCRYNQICE NTRGSYRCVC PRGYRSQGVG RPCMDINECE QVPKPCAHQC SNTPGSFKCI
CPPGQHLLGD GKSCAGLERL PNYGTQYSSY NLARFSPVRN NYQPQQHYRQ YSHLYSSYSE
YRNSRTSLSR TRRTIRKTCP EGSEASHDTC VDIDECENTD ACQHECKNTF GSYQCICPPG
YQLTHNGKTC QDIDECLEQN VHCGPNRMCF NMRGSYQCID TPCPPNYQRD PVSGFCLKNC
PPNDLECALS PYALEYKLVS LPFGIATNQD LIRLVAYTQD GVMHPRTTFL MVDEEQTVPF
ALRDENLKGV VYTTRPLREA ETYRMRVRAS SYSANGTIEY QTTFIVYIAV SAYPY
