GenomeNet

Database: UniProt
Entry: Q00918
LinkDB: Q00918
Original site: Q00918 
ID   LTBP1_RAT               Reviewed;        1712 AA.
AC   Q00918;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   16-JAN-2019, entry version 146.
DE   RecName: Full=Latent-transforming growth factor beta-binding protein 1;
DE            Short=LTBP-1;
DE   AltName: Full=Transforming growth factor beta-1-binding protein 1;
DE            Short=TGF-beta-1-BP-1;
DE   AltName: Full=Transforming growth factor beta-1-masking protein large subunit;
DE   Flags: Precursor;
GN   Name=Ltbp1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2247454; DOI=10.1073/pnas.87.22.8835;
RA   Tsuji T., Okada F., Yamaguchi K., Nakamura T.;
RT   "Molecular cloning of the large subunit of transforming growth factor
RT   type beta masking protein and expression of the mRNA in various rat
RT   tissues.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:8835-8839(1990).
RN   [2]
RP   FUNCTION.
RX   PubMed=7593177; DOI=10.1083/jcb.131.2.539;
RA   Dallas S.L., Miyazono K., Skerry T.M., Mundy G.R., Bonewald L.F.;
RT   "Dual role for the latent transforming growth factor-beta binding
RT   protein in storage of latent TGF-beta in the extracellular matrix and
RT   as a structural matrix protein.";
RL   J. Cell Biol. 131:539-549(1995).
RN   [3]
RP   REVIEW.
RX   PubMed=10743502; DOI=10.1016/S1359-6101(99)00010-6;
RA   Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J.;
RT   "Latent transforming growth factor-beta binding proteins (LTBPs)
RT   -- structural extracellular matrix proteins for targeting TGF-beta
RT   action.";
RL   Cytokine Growth Factor Rev. 10:99-117(1999).
RN   [4]
RP   REVIEW.
RX   PubMed=11104663; DOI=10.1042/bj3520601;
RA   Oklu R., Hesketh R.;
RT   "The latent transforming growth factor beta binding protein (LTBP)
RT   family.";
RL   Biochem. J. 352:601-610(2000).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Key regulator of transforming growth factor beta (TGFB1,
CC       TGFB2 and TGFB3) that controls TGF-beta activation by maintaining
CC       it in a latent state during storage in extracellular space
CC       (PubMed:7593177). Associates specifically via disulfide bonds with
CC       the Latency-associated peptide (LAP), which is the regulatory
CC       chain of TGF-beta, and regulates integrin-dependent activation of
CC       TGF-beta (By similarity). Outcompeted by LRRC32/GARP for binding
CC       to LAP regulatory chain of TGF-beta (By similarity).
CC       {ECO:0000250|UniProtKB:Q14766, ECO:0000269|PubMed:7593177}.
CC   -!- SUBUNIT: Interacts with TGFB1; associates via disulfide bonds with
CC       the Latency-associated peptide chain (LAP) regulatory chain of
CC       TGFB1, leading to regulate activation of TGF-beta-1. LTBP1 does
CC       not bind directly to TGF-beta-1, the active chain of TGFB1.
CC       Interacts (via C-terminal domain) with FBN1 (via N-terminal
CC       domain). Interacts with FBN2. Interacts with ADAMTSL2.
CC       {ECO:0000250|UniProtKB:Q14766}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q14766}.
CC       Secreted, extracellular space, extracellular matrix
CC       {ECO:0000250|UniProtKB:Q14766}.
CC   -!- DOMAIN: The 8-Cys3 region in the third TB domain mediates the
CC       interchain disulfide bond interaction with the Latency-associated
CC       peptide chain (LAP) regulatory chain of TGFB1.
CC       {ECO:0000250|UniProtKB:Q14766}.
CC   -!- PTM: Contains hydroxylated asparagine residues.
CC       {ECO:0000250|UniProtKB:Q14766}.
CC   -!- PTM: Two intrachain disulfide bonds from the TB3 domain are
CC       rearranged upon TGFB1 binding, and form interchain bonds with
CC       TGFB1 propeptide, anchoring it to the extracellular matrix.
CC       {ECO:0000250|UniProtKB:Q14766}.
CC   -!- SIMILARITY: Belongs to the LTBP family. {ECO:0000305}.
DR   EMBL; M55431; AAA42235.1; -; mRNA.
DR   PIR; A38261; A38261.
DR   RefSeq; NP_067598.1; NM_021587.1.
DR   UniGene; Rn.40942; -.
DR   ProteinModelPortal; Q00918; -.
DR   SMR; Q00918; -.
DR   STRING; 10116.ENSRNOP00000040099; -.
DR   CarbonylDB; Q00918; -.
DR   iPTMnet; Q00918; -.
DR   PhosphoSitePlus; Q00918; -.
DR   PaxDb; Q00918; -.
DR   PRIDE; Q00918; -.
DR   GeneID; 59107; -.
DR   KEGG; rno:59107; -.
DR   UCSC; RGD:68379; rat.
DR   CTD; 4052; -.
DR   RGD; 68379; Ltbp1.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; ENOG410Z7XK; LUCA.
DR   HOGENOM; HOG000293153; -.
DR   HOVERGEN; HBG052370; -.
DR   InParanoid; Q00918; -.
DR   KO; K19559; -.
DR   OrthoDB; 1174178at2759; -.
DR   PhylomeDB; Q00918; -.
DR   PRO; PR:Q00918; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0038045; C:large latent transforming growth factor-beta complex; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR   GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEP:RGD.
DR   GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
DR   GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
DR   GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IMP:RGD.
DR   GO; GO:1901388; P:regulation of transforming growth factor beta activation; ISS:UniProtKB.
DR   GO; GO:0035583; P:sequestering of TGFbeta in extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0042060; P:wound healing; IEP:RGD.
DR   Gene3D; 3.90.290.10; -; 4.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR017878; TB_dom.
DR   InterPro; IPR036773; TB_dom_sf.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF07645; EGF_CA; 13.
DR   Pfam; PF00683; TB; 4.
DR   SMART; SM00181; EGF; 18.
DR   SMART; SM00179; EGF_CA; 16.
DR   SUPFAM; SSF57184; SSF57184; 4.
DR   SUPFAM; SSF57581; SSF57581; 4.
DR   PROSITE; PS00010; ASX_HYDROXYL; 13.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 10.
DR   PROSITE; PS50026; EGF_3; 14.
DR   PROSITE; PS01187; EGF_CA; 15.
DR   PROSITE; PS51364; TB; 4.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Growth factor binding;
KW   Hydroxylation; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21   1712       Latent-transforming growth factor beta-
FT                                binding protein 1.
FT                                /FTId=PRO_0000445555.
FT   DOMAIN      181    213       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      391    423       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      549    601       TB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00697}.
FT   DOMAIN      618    658       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      669    721       TB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00697}.
FT   DOMAIN      865    906       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      907    948       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      949    989       EGF-like 6; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      990   1029       EGF-like 7; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1030   1070       EGF-like 8; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1071   1111       EGF-like 9; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1112   1152       EGF-like 10; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1153   1193       EGF-like 11; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1194   1235       EGF-like 12; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1236   1277       EGF-like 13; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1278   1320       EGF-like 14; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1338   1392       TB 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00697}.
FT   DOMAIN     1415   1457       EGF-like 15; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1458   1498       EGF-like 16; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1515   1568       TB 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00697}.
FT   DOMAIN     1612   1652       EGF-like 17. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1653   1697       EGF-like 18; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   REGION     1335   1402       8-Cys3 region.
FT                                {ECO:0000250|UniProtKB:Q14766}.
FT   REGION     1498   1712       C-terminal domain.
FT                                {ECO:0000250|UniProtKB:Q14766}.
FT   COMPBIAS     96    124       Pro-rich.
FT   SITE        736    737       Cleavage. {ECO:0000255}.
FT   SITE       1577   1578       Cleavage. {ECO:0000255}.
FT   MOD_RES     966    966       (3R)-3-hydroxyasparagine.
FT                                {ECO:0000250|UniProtKB:Q14766}.
FT   MOD_RES    1129   1129       (3R)-3-hydroxyasparagine.
FT                                {ECO:0000250|UniProtKB:Q14766}.
FT   MOD_RES    1405   1405       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14766}.
FT   MOD_RES    1588   1588       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14766}.
FT   MOD_RES    1607   1607       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CG19}.
FT   CARBOHYD    339    339       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    370    370       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    416    416       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    612    612       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1042   1042       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1242   1242       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1357   1357       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000250}.
FT   DISULFID    185    195       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    189    201       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    203    212       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    395    405       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    399    411       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    413    422       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    551    573       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    560    586       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    574    589       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    622    633       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    628    642       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    644    657       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    671    694       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    681    706       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    695    709       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    696    721       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID    869    881       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    876    890       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    892    905       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    911    923       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    918    932       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    934    947       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    953    964       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    959    973       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    976    988       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    994   1005       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1000   1014       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1017   1028       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1034   1045       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1040   1054       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1056   1069       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1075   1086       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1081   1095       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1097   1110       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1116   1127       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1122   1136       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1138   1151       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1157   1169       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1164   1178       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1180   1192       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1198   1210       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1204   1219       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1221   1234       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1240   1252       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1246   1261       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1263   1276       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1282   1294       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1289   1303       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1305   1319       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1340   1363       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1350   1375       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1350   1350       Interchain (with C-33 in TGFB1); in
FT                                linked form.
FT                                {ECO:0000250|UniProtKB:Q14766}.
FT   DISULFID   1364   1380       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1365   1392       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1375   1375       Interchain (with C-33 in TGFB1); in
FT                                linked form.
FT                                {ECO:0000250|UniProtKB:Q14766}.
FT   DISULFID   1419   1432       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1427   1441       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1443   1456       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1462   1473       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1468   1482       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1484   1497       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1517   1541       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1527   1553       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1542   1556       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1543   1568       {ECO:0000255|PROSITE-ProRule:PRU00697}.
FT   DISULFID   1616   1627       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1622   1636       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1638   1651       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1657   1672       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1667   1681       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1683   1696       {ECO:0000255|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   1712 AA;  186599 MW;  650BCEAA691FD134 CRC64;
     MAGAWLRWGL LLWAGLLAWS AHGRVRRITY VVRPGPGLPA GTLPLAGPPR TFNVALDARY
     SRSSTATSSR SLAGPPAERT RRTSQPGGAA LPGLRSPLPP EPARPGAPSR QLHSKAGAQT
     AVTRFAKHGR QVVRSKVQQD TQSSGGSRLQ VQQKQQLQGI NVCGGQCCHG WSKAPGSQRC
     TKPSCVPPCQ NGGMCLRPQF CVCKPGTKGK ACEITAAQDT MSPVFGGQNP GSSWVPPEPA
     AKRTSTKKAD TLPRVSPVAQ MTLTLKPKPS MGLSQQIHSQ VAPLSSQNVM IRHGQTQEYV
     LKPKYFPAPK VVSGEQSTEG SFSLRYGQEQ GTAPFQVSNH TGRIKVVFTP SICKVTCTKG
     NCHNSCQKGN TTTLISENGH AADTLTATNF RVVICHLPCM NGGQCSSRDK CQCPPNFTGK
     LCQIPVLGAS MPKLYQHAQQ PGKALGSHVI HSTHTLPLTM TNQQGVKVKF PPNIVNIHVK
     HPPEASVQIH QVSRIDGPVG QRVKEVQPGQ SQVSYQGLPV QKTQTVHSTY SHQQVIPHVY
     PVAAKTQLGR CFQETIGSQC GKALPGLSKQ EDCCGTVGTS WGFNKCQKCP KKQSYHGYTQ
     MMECLQGYKR VNNTFCQDIN ECQLQGVCPN GECLNTMGSY RCSCKMGFGP DPTFSSCVPD
     PPMISEEKGP CYRLVSPGRQ CMHPLSVHLT KQICCCSVGK AWGPQCEKCP LPGTAAFKEI
     CPGGMGYTVS GIHRRRPIHQ HIGKEAVFVK PKNTQPVAKS THPPPLPAKE EPVEALTSSR
     EHGPGVAEPE VVTAPPEKEI PSLDQEKTRL EPGQPQLSPG VSTIHLHPQF PVVVEKTSPP
     VPVEVAPEGS TSSASQVIAP TQVTEINECT VNPDICGAGH CINLPVRYTC ICYEGYKFSE
     QQRKCIDIDE CAQAQHLCSQ GRCENTEGSF LCICPAGFIA SEEGSNCIDV DECLRPDVCR
     DGRCINTAGA FRCEYCDSGY RMSRRGHCED IDECLTPSTC PEEQCVNSPG SYQCVPCTEG
     FRGWNGQCLD VDECLQPKVC TNGSCTNLEG SYMCSCHKGY SPTPDHRHCQ DIDECQQGNL
     CMNGQCKNTD GSFRCTCGQG YQLSAAKDQC EDIDECEHRH LCSHGQCRNT EGSFQCLCNQ
     GYRASVLGDH CEDINECLED SSVCQGGDCI NTAGSYDCTC PDGLQLNDNK GCQDINECAQ
     PGLCAPHGEC LNTQGSFHCV CEQGFSISAD GRTCEDIDEC VNNTVCDSHG FCDNTAGSFR
     CLCYQGFQAP QDGQGCVDVN ECELLSGVCG EAFCENVEGS FLCVCADENQ EYSPMTGQCR
     SRATEDSGVD RQPKEEKKEC YYNLNDASLC DNVLAPNVTK QECCCTSGAG WGDNCEIFPC
     PVQGTAEFSE MCPRGKGFVP AGESSYETGG ENYKDADECL LFGEEICKNG YCLNTQPGYE
     CYCKEGTYYD PVKLQCFDMD ECQDPNSCID GQCVNTEGSY NCFCTHPMVL DASEKRCVQP
     TESNEQIEET DVYQDLCWEH LSEEYVCSRP LVGKQTTYTE CCCLYGEAWG MQCALCPMKD
     SDDYAQLCNI PVTGRRRPYG RDALVDFSEQ YGPETDPYFI QDRFLNSFEE LQAEECGILN
     GCENGRCVRV QEGYTCDCFD GYHLDMAKMT CVDVNECSEL NNRMSLCKNA KCINTEGSYK
     CVCLPGYVPS DKPNYCTPLN TALNLDKDSD LE
//
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