GenomeNet

Database: UniProt
Entry: Q96RW7
LinkDB: Q96RW7
Original site: Q96RW7 
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   13-FEB-2019, entry version 153.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RP   SEQUENCE [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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   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.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   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.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   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
RT   domain II and III of the fibulin family.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   VARIANT ARMD1 ARG-5345, VARIANTS VAL-1624; ILE-2327; THR-2418;
RP   GLY-2893; TYR-4084; THR-4720 AND VAL-5087, TISSUE SPECIFICITY, AND
RP   ALTERNATIVE 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.,
RA   Schain M., Mahan A., Runckel C., Cassera M., Vittal V., Doyle T.M.,
RA   Martin T.M., Weleber R.G., Francis P.J., Acott T.S.;
RT   "Analysis of the ARMD1 locus: evidence that a mutation in hemicentin-1
RT   is associated with age-related macular degeneration in a large
RT   family.";
RL   Hum. Mol. Genet. 12:3315-3323(2003).
CC   -!- FUNCTION: Promotes cleavage furrow maturation during cytokinesis
CC       in preimplantation embryos. May play a role in the architecture of
CC       adhesive and flexible epithelial cell junctions. May play a role
CC       during myocardial remodeling by imparting an effect on cardiac
CC       fibroblast migration. {ECO:0000250|UniProtKB:D3YXG0}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000250|UniProtKB:D3YXG0}.
CC       Cytoplasm {ECO:0000250|UniProtKB:D3YXG0}. Cell junction
CC       {ECO:0000250|UniProtKB:D3YXG0}. Cleavage furrow
CC       {ECO:0000250|UniProtKB:D3YXG0}. Note=The antibody used to
CC       determine subcellular location does not distinguish between HMCN1
CC       and HMCN2. {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         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in skin
CC       fibroblasts and retinal pigment epithelium (RPE) cells
CC       (PubMed:14570714). {ECO:0000269|PubMed:14570714}.
CC   -!- DISEASE: Macular degeneration, age-related, 1 (ARMD1)
CC       [MIM:603075]: A form of age-related macular degeneration, a
CC       multifactorial eye disease and the most common cause of
CC       irreversible vision loss in the developed world. In most patients,
CC       the disease is manifest as ophthalmoscopically visible yellowish
CC       accumulations of protein and lipid that lie beneath the retinal
CC       pigment epithelium and within an elastin-containing structure
CC       known as Bruch membrane. {ECO:0000269|PubMed:14570714}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB71154.1; Type=Frameshift; Positions=657; Evidence={ECO:0000305};
CC       Sequence=BAB71216.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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   UniGene; Hs.58877; -.
DR   ProteinModelPortal; Q96RW7; -.
DR   SMR; Q96RW7; -.
DR   BioGrid; 123785; 5.
DR   IntAct; Q96RW7; 8.
DR   STRING; 9606.ENSP00000271588; -.
DR   CarbonylDB; Q96RW7; -.
DR   GlyConnect; 1306; -.
DR   iPTMnet; Q96RW7; -.
DR   PhosphoSitePlus; Q96RW7; -.
DR   BioMuta; HMCN1; -.
DR   DMDM; 85542049; -.
DR   EPD; Q96RW7; -.
DR   jPOST; Q96RW7; -.
DR   MaxQB; Q96RW7; -.
DR   PaxDb; Q96RW7; -.
DR   PeptideAtlas; Q96RW7; -.
DR   PRIDE; Q96RW7; -.
DR   ProteomicsDB; 78045; -.
DR   ProteomicsDB; 78046; -. [Q96RW7-2]
DR   ProteomicsDB; 78047; -. [Q96RW7-3]
DR   Ensembl; ENST00000271588; ENSP00000271588; ENSG00000143341. [Q96RW7-1]
DR   GeneID; 83872; -.
DR   KEGG; hsa:83872; -.
DR   UCSC; uc001grq.2; human. [Q96RW7-1]
DR   CTD; 83872; -.
DR   DisGeNET; 83872; -.
DR   EuPathDB; HostDB:ENSG00000143341.11; -.
DR   GeneCards; HMCN1; -.
DR   H-InvDB; HIX0001425; -.
DR   HGNC; HGNC:19194; HMCN1.
DR   HPA; HPA051677; -.
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   eggNOG; KOG4475; Eukaryota.
DR   eggNOG; ENOG410ZN3C; LUCA.
DR   GeneTree; ENSGT00940000154614; -.
DR   HOGENOM; HOG000231553; -.
DR   HOVERGEN; HBG080319; -.
DR   InParanoid; Q96RW7; -.
DR   KO; K17341; -.
DR   OMA; CNNPSAQ; -.
DR   OrthoDB; 38313at2759; -.
DR   PhylomeDB; Q96RW7; -.
DR   ChiTaRS; HMCN1; human.
DR   GeneWiki; HMCN1; -.
DR   GenomeRNAi; 83872; -.
DR   PRO; PR:Q96RW7; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000143341; Expressed in 157 organ(s), highest expression level in thoracic aorta.
DR   ExpressionAtlas; Q96RW7; baseline and differential.
DR   Genevisible; Q96RW7; HS.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0005913; C:cell-cell adherens junction; IBA:GO_Central.
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:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
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; -; 5.
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; 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; 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; 33.
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;
KW   Basement membrane; Calcium; Cell cycle; Cell division; Cell junction;
KW   Complete proteome; Cytoplasm; Disease mutation; Disulfide bond;
KW   EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Immunoglobulin domain; Polymorphism; Reference proteome; Repeat;
KW   Secreted; Sensory transduction; Signal; Vision.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22   5635       Hemicentin-1.
FT                                /FTId=PRO_0000045391.
FT   DOMAIN       41    216       VWFA.
FT   DOMAIN      431    517       Ig-like C2-type 1.
FT   DOMAIN      520    607       Ig-like C2-type 2.
FT   DOMAIN      612    697       Ig-like C2-type 3.
FT   DOMAIN      702    788       Ig-like C2-type 4.
FT   DOMAIN      793    883       Ig-like C2-type 5.
FT   DOMAIN      890    976       Ig-like C2-type 6.
FT   DOMAIN      981   1067       Ig-like C2-type 7.
FT   DOMAIN     1072   1166       Ig-like C2-type 8.
FT   DOMAIN     1171   1255       Ig-like C2-type 9.
FT   DOMAIN     1262   1354       Ig-like C2-type 10.
FT   DOMAIN     1358   1447       Ig-like C2-type 11.
FT   DOMAIN     1452   1541       Ig-like C2-type 12.
FT   DOMAIN     1546   1634       Ig-like C2-type 13.
FT   DOMAIN     1638   1724       Ig-like C2-type 14.
FT   DOMAIN     1733   1821       Ig-like C2-type 15.
FT   DOMAIN     1826   1914       Ig-like C2-type 16.
FT   DOMAIN     1919   2007       Ig-like C2-type 17.
FT   DOMAIN     2012   2097       Ig-like C2-type 18.
FT   DOMAIN     2104   2190       Ig-like C2-type 19.
FT   DOMAIN     2195   2285       Ig-like C2-type 20.
FT   DOMAIN     2290   2379       Ig-like C2-type 21.
FT   DOMAIN     2384   2470       Ig-like C2-type 22.
FT   DOMAIN     2478   2564       Ig-like C2-type 23.
FT   DOMAIN     2571   2662       Ig-like C2-type 24.
FT   DOMAIN     2666   2763       Ig-like C2-type 25.
FT   DOMAIN     2766   2864       Ig-like C2-type 26.
FT   DOMAIN     2868   2959       Ig-like C2-type 27.
FT   DOMAIN     2964   3051       Ig-like C2-type 28.
FT   DOMAIN     3056   3146       Ig-like C2-type 29.
FT   DOMAIN     3151   3240       Ig-like C2-type 30.
FT   DOMAIN     3245   3335       Ig-like C2-type 31.
FT   DOMAIN     3340   3429       Ig-like C2-type 32.
FT   DOMAIN     3434   3516       Ig-like C2-type 33.
FT   DOMAIN     3527   3615       Ig-like C2-type 34.
FT   DOMAIN     3620   3708       Ig-like C2-type 35.
FT   DOMAIN     3713   3797       Ig-like C2-type 36.
FT   DOMAIN     3804   3892       Ig-like C2-type 37.
FT   DOMAIN     3897   3983       Ig-like C2-type 38.
FT   DOMAIN     3988   4076       Ig-like C2-type 39.
FT   DOMAIN     4079   4164       Ig-like C2-type 40.
FT   DOMAIN     4169   4255       Ig-like C2-type 41.
FT   DOMAIN     4260   4344       Ig-like C2-type 42.
FT   DOMAIN     4348   4435       Ig-like C2-type 43.
FT   DOMAIN     4440   4527       Ig-like C2-type 44.
FT   DOMAIN     4529   4584       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN     4586   4641       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN     4643   4698       TSP type-1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN     4700   4755       TSP type-1 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN     4757   4812       TSP type-1 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN     4814   4869       TSP type-1 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN     4871   5093       Nidogen G2 beta-barrel.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00348}.
FT   DOMAIN     5107   5146       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     5147   5191       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     5192   5229       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     5230   5271       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     5272   5307       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     5315   5355       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     5432   5471       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   CARBOHYD    349    349       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    390    390       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    528    528       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    550    550       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    573    573       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    620    620       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    693    693       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    809    809       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    970    970       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1158   1158       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1272   1272       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1369   1369       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1552   1552       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1929   1929       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2112   2112       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2155   2155       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2395   2395       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2689   2689       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2887   2887       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2973   2973       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3221   3221       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3300   3300       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3530   3530       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3689   3689       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3727   3727       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3812   3812       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4029   4029       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4401   4401       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4491   4491       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4606   4606       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   4894   4894       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   5040   5040       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   5267   5267       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   5615   5615       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    451    499       {ECO:0000250}.
FT   DISULFID    541    591       {ECO:0000250}.
FT   DISULFID    633    681       {ECO:0000250}.
FT   DISULFID    723    772       {ECO:0000250}.
FT   DISULFID    814    867       {ECO:0000250}.
FT   DISULFID    911    960       {ECO:0000250}.
FT   DISULFID   1002   1051       {ECO:0000250}.
FT   DISULFID   1101   1150       {ECO:0000250}.
FT   DISULFID   1192   1241       {ECO:0000250}.
FT   DISULFID   1288   1338       {ECO:0000250}.
FT   DISULFID   1382   1431       {ECO:0000250}.
FT   DISULFID   1475   1525       {ECO:0000250}.
FT   DISULFID   1569   1618       {ECO:0000250}.
FT   DISULFID   1663   1712       {ECO:0000250}.
FT   DISULFID   1756   1805       {ECO:0000250}.
FT   DISULFID   1848   1898       {ECO:0000250}.
FT   DISULFID   1942   1991       {ECO:0000250}.
FT   DISULFID   2033   2083       {ECO:0000250}.
FT   DISULFID   2125   2174       {ECO:0000250}.
FT   DISULFID   2218   2269       {ECO:0000250}.
FT   DISULFID   2314   2363       {ECO:0000250}.
FT   DISULFID   2408   2457       {ECO:0000250}.
FT   DISULFID   2501   2550       {ECO:0000250}.
FT   DISULFID   2597   2646       {ECO:0000250}.
FT   DISULFID   2696   2745       {ECO:0000250}.
FT   DISULFID   2799   2848       {ECO:0000250}.
FT   DISULFID   2894   2943       {ECO:0000250}.
FT   DISULFID   2986   3035       {ECO:0000250}.
FT   DISULFID   3081   3130       {ECO:0000250}.
FT   DISULFID   3173   3224       {ECO:0000250}.
FT   DISULFID   3268   3319       {ECO:0000250}.
FT   DISULFID   3364   3413       {ECO:0000250}.
FT   DISULFID   3457   3506       {ECO:0000250}.
FT   DISULFID   3550   3599       {ECO:0000250}.
FT   DISULFID   3643   3692       {ECO:0000250}.
FT   DISULFID   3734   3783       {ECO:0000250}.
FT   DISULFID   3825   3876       {ECO:0000250}.
FT   DISULFID   3918   3967       {ECO:0000250}.
FT   DISULFID   4009   4058       {ECO:0000250}.
FT   DISULFID   4100   4148       {ECO:0000250}.
FT   DISULFID   4190   4239       {ECO:0000250}.
FT   DISULFID   4281   4328       {ECO:0000250}.
FT   DISULFID   4371   4419       {ECO:0000250}.
FT   DISULFID   4461   4509       {ECO:0000250}.
FT   DISULFID   4541   4578       {ECO:0000250}.
FT   DISULFID   4545   4583       {ECO:0000250}.
FT   DISULFID   4556   4568       {ECO:0000250}.
FT   DISULFID   4598   4635       {ECO:0000250}.
FT   DISULFID   4602   4640       {ECO:0000250}.
FT   DISULFID   4613   4625       {ECO:0000250}.
FT   DISULFID   4655   4692       {ECO:0000250}.
FT   DISULFID   4659   4697       {ECO:0000250}.
FT   DISULFID   4670   4682       {ECO:0000250}.
FT   DISULFID   4712   4749       {ECO:0000250}.
FT   DISULFID   4716   4754       {ECO:0000250}.
FT   DISULFID   4727   4739       {ECO:0000250}.
FT   DISULFID   4769   4806       {ECO:0000250}.
FT   DISULFID   4773   4811       {ECO:0000250}.
FT   DISULFID   4784   4796       {ECO:0000250}.
FT   DISULFID   4826   4863       {ECO:0000250}.
FT   DISULFID   4830   4868       {ECO:0000250}.
FT   DISULFID   4841   4853       {ECO:0000250}.
FT   DISULFID   5111   5121       {ECO:0000250}.
FT   DISULFID   5117   5130       {ECO:0000250}.
FT   DISULFID   5132   5145       {ECO:0000250}.
FT   DISULFID   5196   5206       {ECO:0000250}.
FT   DISULFID   5202   5215       {ECO:0000250}.
FT   DISULFID   5217   5228       {ECO:0000250}.
FT   DISULFID   5276   5289       {ECO:0000250}.
FT   DISULFID   5283   5298       {ECO:0000250}.
FT   DISULFID   5319   5330       {ECO:0000250}.
FT   DISULFID   5326   5339       {ECO:0000250}.
FT   DISULFID   5341   5354       {ECO:0000250}.
FT   DISULFID   5436   5446       {ECO:0000250}.
FT   DISULFID   5442   5455       {ECO:0000250}.
FT   DISULFID   5457   5470       {ECO:0000250}.
FT   VAR_SEQ       1    616       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_016871.
FT   VAR_SEQ    1169   1171       VPP -> GES (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_016872.
FT   VAR_SEQ    1172   5635       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_016873.
FT   VAR_SEQ    5315   5431       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_016874.
FT   VARIANT    1056   1056       T -> A (in dbSNP:rs7539719).
FT                                /FTId=VAR_049875.
FT   VARIANT    1184   1184       V -> F (in dbSNP:rs12239296).
FT                                /FTId=VAR_049876.
FT   VARIANT    1624   1624       A -> V. {ECO:0000269|PubMed:14570714}.
FT                                /FTId=VAR_024811.
FT   VARIANT    2327   2327       M -> I (in dbSNP:rs12067376).
FT                                {ECO:0000269|PubMed:14570714}.
FT                                /FTId=VAR_024812.
FT   VARIANT    2418   2418       I -> T (in dbSNP:rs12129650).
FT                                {ECO:0000269|PubMed:14570714,
FT                                ECO:0000269|Ref.1}.
FT                                /FTId=VAR_024813.
FT   VARIANT    2893   2893       E -> G (in dbSNP:rs10798035).
FT                                {ECO:0000269|PubMed:14570714}.
FT                                /FTId=VAR_024814.
FT   VARIANT    4084   4084       H -> Y (in dbSNP:rs41317489).
FT                                {ECO:0000269|PubMed:14570714}.
FT                                /FTId=VAR_024815.
FT   VARIANT    4437   4437       Q -> R (in dbSNP:rs10911825).
FT                                /FTId=VAR_049877.
FT   VARIANT    4720   4720       A -> T (in dbSNP:rs6693069).
FT                                {ECO:0000269|PubMed:14570714}.
FT                                /FTId=VAR_024816.
FT   VARIANT    5087   5087       D -> V (in dbSNP:rs41317507).
FT                                {ECO:0000269|PubMed:14570714}.
FT                                /FTId=VAR_024817.
FT   VARIANT    5345   5345       Q -> R (in ARMD1; dbSNP:rs121434382).
FT                                {ECO:0000269|PubMed:14570714}.
FT                                /FTId=VAR_024818.
FT   CONFLICT     35     35       I -> F (in Ref. 1). {ECO:0000305}.
FT   CONFLICT    483    483       N -> S (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   1042   1042       G -> E (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   1078   1078       Q -> L (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   1153   1153       T -> I (in Ref. 2; BAB71216).
FT                                {ECO:0000305}.
FT   CONFLICT   1319   1319       D -> E (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   1368   1368       T -> S (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   1414   1414       K -> R (in Ref. 2; BAB71216).
FT                                {ECO:0000305}.
FT   CONFLICT   1461   1461       N -> K (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   1570   1570       E -> K (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   1664   1664       K -> N (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   1688   1688       I -> F (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   1775   1775       I -> V (in Ref. 2; BAB71216).
FT                                {ECO:0000305}.
FT   CONFLICT   1816   1816       K -> E (in Ref. 2; BAB71216).
FT                                {ECO:0000305}.
FT   CONFLICT   1959   1959       R -> C (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   2073   2073       A -> T (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   2184   2184       E -> EK (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   2872   2872       K -> E (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   3189   3189       H -> Y (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   3355   3355       L -> Y (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   4136   4136       A -> T (in Ref. 4). {ECO:0000305}.
FT   CONFLICT   4340   4340       I -> T (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   4358   4358       N -> H (in Ref. 4). {ECO:0000305}.
FT   CONFLICT   4699   4699       I -> V (in Ref. 4). {ECO:0000305}.
FT   CONFLICT   5294   5294       G -> S (in Ref. 1). {ECO:0000305}.
FT   CONFLICT   5317   5317       N -> D (in Ref. 1). {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
//
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