GenomeNet

Database: UniProt
Entry: P35443
LinkDB: P35443
Original site: P35443 
ID   TSP4_HUMAN              Reviewed;         961 AA.
AC   P35443; B2R909; Q86TG2;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   13-FEB-2019, entry version 185.
DE   RecName: Full=Thrombospondin-4;
DE   Flags: Precursor;
GN   Name=THBS4; Synonyms=TSP4;
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], AND VARIANT VAL-420.
RC   TISSUE=Heart;
RX   PubMed=8350346; DOI=10.1007/BF00556355;
RA   Lawler J., Duquette M., Urry L., McHenry K., Smith T.F.;
RT   "The evolution of the thrombospondin gene family.";
RL   J. Mol. Evol. 36:509-516(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-420, AND SUBUNIT.
RX   PubMed=7852353; DOI=10.1074/jbc.270.6.2809;
RA   Lawler J., McHenry K., Duquette M., Derick L.;
RT   "Characterization of human thrombospondin-4.";
RL   J. Biol. Chem. 270:2809-2814(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-387.
RC   TISSUE=Synovium;
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-55; PRO-387;
RP   VAL-420 AND ILE-646.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PNS;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION IN CELL PROLIFERATION, AND INTERACTION WITH PTBP3.
RX   PubMed=19441079; DOI=10.1002/jcp.21817;
RA   Sadvakassova G., Dobocan M.C., Difalco M.R., Congote L.F.;
RT   "Regulator of differentiation 1 (ROD1) binds to the amphipathic C-
RT   terminal peptide of thrombospondin-4 and is involved in its mitogenic
RT   activity.";
RL   J. Cell. Physiol. 220:672-679(2009).
RN   [7]
RP   INTERACTION WITH ATF6.
RX   PubMed=22682248; DOI=10.1016/j.cell.2012.03.050;
RA   Lynch J.M., Maillet M., Vanhoutte D., Schloemer A., Sargent M.A.,
RA   Blair N.S., Lynch K.A., Okada T., Aronow B.J., Osinska H., Prywes R.,
RA   Lorenz J.N., Mori K., Lawler J., Robbins J., Molkentin J.D.;
RT   "A thrombospondin-dependent pathway for a protective ER stress
RT   response.";
RL   Cell 149:1257-1268(2012).
RN   [8]
RP   REVIEW.
RX   PubMed=23287452; DOI=10.1161/CIRCRESAHA.112.280560;
RA   Doroudgar S., Glembotski C.C.;
RT   "ATF6 [corrected] and thrombospondin 4: the dynamic duo of the
RT   adaptive endoplasmic reticulum stress response.";
RL   Circ. Res. 112:9-12(2013).
RN   [9]
RP   ERRATUM.
RX   DOI=10.1161/RES.0b013e318286c21f;
RA   Doroudgar S., Glembotski C.C.;
RL   Circ. Res. 112:E31-E31(2013).
RN   [10]
RP   REVIEW.
RX   PubMed=23892609; DOI=10.1097/MOL.0b013e3283642912;
RA   Stenina-Adognravi O.;
RT   "Thrombospondins: old players, new games.";
RL   Curr. Opin. Lipidol. 24:401-409(2013).
RN   [11]
RP   VARIANT PRO-387.
RX   PubMed=22011848; DOI=10.1160/TH11-03-0206;
RA   Corsetti J.P., Ryan D., Moss A.J., McCarthy J., Goldenberg I.,
RA   Zareba W., Sparks C.E.;
RT   "Thrombospondin-4 polymorphism (A387P) predicts cardiovascular risk in
RT   postinfarction patients with high HDL cholesterol and C-reactive
RT   protein levels.";
RL   Thromb. Haemost. 106:1170-1178(2011).
CC   -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and
CC       cell-to-matrix interactions and is involved in various processes
CC       including cellular proliferation, migration, adhesion and
CC       attachment, inflammatory response to CNS injury, regulation of
CC       vascular inflammation and adaptive responses of the heart to
CC       pressure overload and in myocardial function and remodeling. Binds
CC       to structural extracellular matrix (ECM) proteins and modulates
CC       the ECM in response to tissue damage, contributing to
CC       cardioprotective and adaptive ECM remodeling. Plays a role in ER
CC       stress response, via its interaction with the activating
CC       transcription factor 6 alpha (ATF6) which produces adaptive ER
CC       stress response factors and protects myocardium from pressure
CC       overload. May contribute to spinal presynaptic hypersensitivity
CC       and neuropathic pain states after peripheral nerve injury. May
CC       play a role in regulating protective astrogenesis from the
CC       subventricular zone (SVZ) niche after injury in a NOTCH1-dependent
CC       manner (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:19441079}.
CC   -!- SUBUNIT: Homopentamer; disulfide-linked. Interacts with PTBP3.
CC       Interacts with NOTCH1 (By similarity). Interacts (via EGF-like 3;
CC       calcium-binding domain) with ATF6 and facilitates its processing,
CC       activation and nuclear translocation. {ECO:0000250,
CC       ECO:0000269|PubMed:19441079, ECO:0000269|PubMed:22682248,
CC       ECO:0000269|PubMed:7852353}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q9Z1T2}. Sarcoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q9Z1T2}. Secreted
CC       {ECO:0000250|UniProtKB:Q9Z1T2}. Secreted, extracellular space
CC       {ECO:0000250|UniProtKB:Q9Z1T2}. Secreted, extracellular space,
CC       extracellular matrix {ECO:0000250|UniProtKB:Q9Z1T2}.
CC   -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/thbs4/";
DR   EMBL; Z19585; CAA79635.1; -; mRNA.
DR   EMBL; AK313587; BAG36356.1; -; mRNA.
DR   EMBL; AY566253; AAS66982.1; -; Genomic_DNA.
DR   EMBL; BC050456; AAH50456.1; -; mRNA.
DR   CCDS; CCDS4049.1; -.
DR   PIR; A55710; TSHUP4.
DR   RefSeq; NP_001293141.1; NM_001306212.1.
DR   RefSeq; NP_001293142.1; NM_001306213.1.
DR   RefSeq; NP_001293143.1; NM_001306214.1.
DR   RefSeq; NP_003239.2; NM_003248.5.
DR   UniGene; Hs.211426; -.
DR   ProteinModelPortal; P35443; -.
DR   SMR; P35443; -.
DR   BioGrid; 112918; 3.
DR   ComplexPortal; CPX-1790; Thrombospondin 4 complex.
DR   IntAct; P35443; 1.
DR   STRING; 9606.ENSP00000339730; -.
DR   iPTMnet; P35443; -.
DR   PhosphoSitePlus; P35443; -.
DR   BioMuta; THBS4; -.
DR   DMDM; 55977790; -.
DR   EPD; P35443; -.
DR   jPOST; P35443; -.
DR   MaxQB; P35443; -.
DR   PaxDb; P35443; -.
DR   PeptideAtlas; P35443; -.
DR   PRIDE; P35443; -.
DR   ProteomicsDB; 55063; -.
DR   Ensembl; ENST00000350881; ENSP00000339730; ENSG00000113296.
DR   GeneID; 7060; -.
DR   KEGG; hsa:7060; -.
DR   UCSC; uc021yaw.2; human.
DR   CTD; 7060; -.
DR   DisGeNET; 7060; -.
DR   EuPathDB; HostDB:ENSG00000113296.14; -.
DR   GeneCards; THBS4; -.
DR   HGNC; HGNC:11788; THBS4.
DR   HPA; CAB004597; -.
DR   HPA; HPA042426; -.
DR   MIM; 600715; gene.
DR   neXtProt; NX_P35443; -.
DR   OpenTargets; ENSG00000113296; -.
DR   PharmGKB; PA36500; -.
DR   eggNOG; ENOG410IFQQ; Eukaryota.
DR   eggNOG; ENOG410XQKE; LUCA.
DR   GeneTree; ENSGT00940000155227; -.
DR   HOGENOM; HOG000007542; -.
DR   HOVERGEN; HBG000636; -.
DR   InParanoid; P35443; -.
DR   KO; K04659; -.
DR   OMA; CFRGVRC; -.
DR   OrthoDB; 120983at2759; -.
DR   PhylomeDB; P35443; -.
DR   TreeFam; TF324917; -.
DR   Reactome; R-HSA-186797; Signaling by PDGF.
DR   GeneWiki; THBS4; -.
DR   GenomeRNAi; 7060; -.
DR   PRO; PR:P35443; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   Bgee; ENSG00000113296; Expressed in 209 organ(s), highest expression level in tendon.
DR   ExpressionAtlas; P35443; baseline and differential.
DR   Genevisible; P35443; HS.
DR   GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR   GO; GO:0048266; P:behavioral response to pain; ISS:UniProtKB.
DR   GO; GO:0071603; P:endothelial cell-cell adhesion; IDA:UniProtKB.
DR   GO; GO:0051451; P:myoblast migration; IDA:UniProtKB.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEP:UniProtKB.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
DR   GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IDA:UniProtKB.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0034103; P:regulation of tissue remodeling; ISS:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.1080.10; -; 3.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR024665; Thbs/COMP_coiled-coil.
DR   InterPro; IPR037349; Thrombospondin.
DR   InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR   InterPro; IPR017897; Thrombospondin_3_rpt.
DR   InterPro; IPR008859; Thrombospondin_C.
DR   InterPro; IPR028974; TSP_type-3_rpt.
DR   PANTHER; PTHR10199; PTHR10199; 1.
DR   Pfam; PF11598; COMP; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF02412; TSP_3; 6.
DR   Pfam; PF05735; TSP_C; 1.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF103647; SSF103647; 3.
DR   SUPFAM; SSF49899; SSF49899; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS51234; TSP3; 8.
DR   PROSITE; PS51236; TSP_CTER; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Complete proteome; Disulfide bond;
KW   EGF-like domain; Endoplasmic reticulum; Extracellular matrix;
KW   Glycoprotein; Growth factor; Mitogen; Polymorphism;
KW   Reference proteome; Repeat; Sarcoplasmic reticulum; Secreted; Signal;
KW   Tissue remodeling; Unfolded protein response.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27    961       Thrombospondin-4.
FT                                /FTId=PRO_0000035852.
FT   DOMAIN       27    192       Laminin G-like.
FT   DOMAIN      286    325       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      326    363       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      379    419       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      420    462       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT      463    495       TSP type-3 1.
FT   REPEAT      496    531       TSP type-3 2.
FT   REPEAT      532    554       TSP type-3 3.
FT   REPEAT      555    590       TSP type-3 4.
FT   REPEAT      591    613       TSP type-3 5.
FT   REPEAT      614    651       TSP type-3 6.
FT   REPEAT      652    691       TSP type-3 7.
FT   REPEAT      692    727       TSP type-3 8.
FT   DOMAIN      731    945       TSP C-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00635}.
FT   MOTIF       562    564       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    612    612       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    941    941       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    258    258       Interchain. {ECO:0000305}.
FT   DISULFID    261    261       Interchain. {ECO:0000305}.
FT   DISULFID    290    301       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    295    310       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    313    324       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    330    341       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    335    350       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    353    377       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    383    394       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    388    403       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    406    418       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    424    438       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    432    448       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    450    461       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    477    482       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    487    507       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    523    543       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    546    566       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    582    602       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    605    625       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    643    663       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    683    703       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    719    940       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VARIANT      55     55       L -> Q (in dbSNP:rs17881847).
FT                                {ECO:0000269|Ref.4}.
FT                                /FTId=VAR_019951.
FT   VARIANT     387    387       A -> P (functional polymorphism;
FT                                associated with a pro-atherogenic
FT                                phenotype; dbSNP:rs1866389).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:22011848,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_019952.
FT   VARIANT     420    420       A -> V (in dbSNP:rs17882372).
FT                                {ECO:0000269|PubMed:7852353,
FT                                ECO:0000269|PubMed:8350346,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_019953.
FT   VARIANT     646    646       V -> I (in dbSNP:rs2229396).
FT                                {ECO:0000269|Ref.4}.
FT                                /FTId=VAR_019954.
FT   VARIANT     737    737       V -> I (in dbSNP:rs2229398).
FT                                /FTId=VAR_052659.
FT   CONFLICT     96     96       N -> S (in Ref. 1; no nucleotide entry
FT                                and 2; CAA79635). {ECO:0000305}.
FT   CONFLICT    276    276       P -> A (in Ref. 1; no nucleotide entry
FT                                and 2; CAA79635). {ECO:0000305}.
FT   CONFLICT    737    737       V -> G (in Ref. 1; no nucleotide entry
FT                                and 2; CAA79635). {ECO:0000305}.
SQ   SEQUENCE   961 AA;  105869 MW;  18F867AA5FFDA54B CRC64;
     MLAPRGAAVL LLHLVLQRWL AAGAQATPQV FDLLPSSSQR LNPGALLPVL TDPALNDLYV
     ISTFKLQTKS SATIFGLYSS TDNSKYFEFT VMGRLNKAIL RYLKNDGKVH LVVFNNLQLA
     DGRRHRILLR LSNLQRGAGS LELYLDCIQV DSVHNLPRAF AGPSQKPETI ELRTFQRKPQ
     DFLEELKLVV RGSLFQVASL QDCFLQQSEP LAATGTGDFN RQFLGQMTQL NQLLGEVKDL
     LRQQVKETSF LRNTIAECQA CGPLKFQSPT PSTVVPPAPP APPTRPPRRC DSNPCFRGVQ
     CTDSRDGFQC GPCPEGYTGN GITCIDVDEC KYHPCYPGVH CINLSPGFRC DACPVGFTGP
     MVQGVGISFA KSNKQVCTDI DECRNGACVP NSICVNTLGS YRCGPCKPGY TGDQIRGCKA
     ERNCRNPELN PCSVNAQCIE ERQGDVTCVC GVGWAGDGYI CGKDVDIDSY PDEELPCSAR
     NCKKDNCKYV PNSGQEDADR DGIGDACDED ADGDGILNEQ DNCVLIHNVD QRNSDKDIFG
     DACDNCLSVL NNDQKDTDGD GRGDACDDDM DGDGIKNILD NCPKFPNRDQ RDKDGDGVGD
     ACDSCPDVSN PNQSDVDNDL VGDSCDTNQD SDGDGHQDST DNCPTVINSA QLDTDKDGIG
     DECDDDDDND GIPDLVPPGP DNCRLVPNPA QEDSNSDGVG DICESDFDQD QVIDRIDVCP
     ENAEVTLTDF RAYQTVVLDP EGDAQIDPNW VVLNQGMEIV QTMNSDPGLA VGYTAFNGVD
     FEGTFHVNTQ TDDDYAGFIF GYQDSSSFYV VMWKQTEQTY WQATPFRAVA EPGIQLKAVK
     SKTGPGEHLR NSLWHTGDTS DQVRLLWKDS RNVGWKDKVS YRWFLQHRPQ VGYIRVRFYE
     GSELVADSGV TIDTTMRGGR LGVFCFSQEN IIWSNLKYRC NDTIPEDFQE FQTQNFDRFD
     N
//
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