GenomeNet

Database: UniProt
Entry: Q9R1K2
LinkDB: Q9R1K2
Original site: Q9R1K2 
ID   TEN2_RAT                Reviewed;        2774 AA.
AC   Q9R1K2; Q9R1J9; Q9R1K0; Q9R1K1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   16-JAN-2019, entry version 128.
DE   RecName: Full=Teneurin-2;
DE            Short=Ten-2;
DE   AltName: Full=Neurestin;
DE   AltName: Full=Protein Odd Oz/ten-m homolog 2;
DE   AltName: Full=Tenascin-M2;
DE            Short=Ten-m2;
DE   AltName: Full=Teneurin transmembrane protein 2;
DE   Contains:
DE     RecName: Full=Ten-2, soluble form;
DE   Contains:
DE     RecName: Full=Ten-2 intracellular domain;
DE              Short=Ten-2 ICD;
GN   Name=Tenm2; Synonyms=Odz2, Tnm2;
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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   575-911 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 575-911 (ISOFORM
RP   4), NUCLEOTIDE SEQUENCE [MRNA] OF 575-911 (ISOFORM 1), AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Sprague-Dawley; TISSUE=Olfactory bulb;
RX   PubMed=10419693; DOI=10.1006/dbio.1999.9310;
RA   Otaki J.M., Firestein S.;
RT   "Neurestin: putative transmembrane molecule implicated in neuronal
RT   development.";
RL   Dev. Biol. 212:165-181(1999).
RN   [2]
RP   FUNCTION AS ADGRL1 LIGAND, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=21724987; DOI=10.1073/pnas.1019434108;
RA   Silva J.P., Lelianova V.G., Ermolyuk Y.S., Vysokov N., Hitchen P.G.,
RA   Berninghausen O., Rahman M.A., Zangrandi A., Fidalgo S.,
RA   Tonevitsky A.G., Dell A., Volynski K.E., Ushkaryov Y.A.;
RT   "Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-
RT   affinity transsynaptic receptor pair with signaling capabilities.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12113-12118(2011).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-155 AND SER-157, AND
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: Involved in neural development, regulating the
CC       establishment of proper connectivity within the nervous system.
CC       Promotes the formation of filopodia and enlarged growth cone in
CC       neuronal cells. Mediates axon guidance and homophilic and
CC       heterophilic cell-cell adhesion. May function as a cellular signal
CC       transducer (By similarity). Acts as a ligand of the ADGRL1
CC       receptor. {ECO:0000250, ECO:0000269|PubMed:21724987}.
CC   -!- FUNCTION: Ten-2 intracellular domain: Induces gene transcription
CC       inhibition. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (Probable). Heterodimer with
CC       either TENM1 or TENM3. May also form heterodimer with TENM4 (By
CC       similarity). Interacts with ADGRL1 isoform 2. {ECO:0000250,
CC       ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21724987};
CC       Single-pass membrane protein {ECO:0000269|PubMed:21724987}.
CC       Endoplasmic reticulum {ECO:0000250}. Golgi apparatus
CC       {ECO:0000250}. Cell junction, synapse
CC       {ECO:0000269|PubMed:21724987}. Cell projection, dendritic spine
CC       {ECO:0000269|PubMed:21724987}. Cell projection, filopodium
CC       {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cell
CC       junction, synapse, postsynaptic cell membrane
CC       {ECO:0000269|PubMed:21724987}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:21724987}. Cell junction, synapse, synaptosome
CC       {ECO:0000269|PubMed:21724987}. Note=Colocalizes with ADGRL1 in
CC       synaptic junctions.
CC   -!- SUBCELLULAR LOCATION: Ten-2 intracellular domain: Nucleus, PML
CC       body {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Gamma;
CC         IsoId=Q9R1K2-1; Sequence=Displayed;
CC       Name=2; Synonyms=Alpha;
CC         IsoId=Q9R1K2-2; Sequence=VSP_021396;
CC         Note=No experimental confirmation available.;
CC       Name=3; Synonyms=Delta;
CC         IsoId=Q9R1K2-3; Sequence=VSP_021395;
CC         Note=No experimental confirmation available.;
CC       Name=4; Synonyms=Beta;
CC         IsoId=Q9R1K2-4; Sequence=VSP_021397;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level).
CC       {ECO:0000269|PubMed:21724987}.
CC   -!- DEVELOPMENTAL STAGE: From E17-E18 embryos, a very strong signal
CC       appeared and continued throughout the remaining prenatal days. The
CC       signal was strongest in the cerebral cortex (including the
CC       cingulate cortex, neocortex, and orbital and insular area),
CC       thalamus (anterior and intermediate thalamus), and weak in
CC       posterior thalamus and midbrain. {ECO:0000269|PubMed:10419693}.
CC   -!- DOMAIN: EGF-like domains 2 and 5 which have an odd number of
CC       cysteines might enable the formation of intermolecular disulfide
CC       bonds.
CC   -!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking
CC       domains for intracellular SH3-containing proteins.
CC   -!- PTM: Ten-2, soluble form: Derives from the membrane form by
CC       proteolytic processing. {ECO:0000250}.
CC   -!- PTM: Ten-2 intracellular domain: Derives from the plasma membrane
CC       form by proteolytic cleavage and translocates to the nucleus.
CC       Homophilic binding of the C-terminal extracellular domain
CC       stimulates its proteolytic cleavage and release in the
CC       cytoplasmic. Is subjected to rapid degradation by the proteasome
CC       pathway (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC       {ECO:0000305}.
DR   EMBL; AF086607; AAD47383.1; -; mRNA.
DR   EMBL; AF086608; AAD47384.1; -; mRNA.
DR   EMBL; AF086609; AAD47385.1; -; mRNA.
DR   EMBL; AF086610; AAD47386.1; -; mRNA.
DR   RefSeq; NP_064473.1; NM_020088.1. [Q9R1K2-2]
DR   UniGene; Rn.229571; -.
DR   ProteinModelPortal; Q9R1K2; -.
DR   SMR; Q9R1K2; -.
DR   STRING; 10116.ENSRNOP00000011922; -.
DR   iPTMnet; Q9R1K2; -.
DR   PhosphoSitePlus; Q9R1K2; -.
DR   SwissPalm; Q9R1K2; -.
DR   UniCarbKB; Q9R1K2; -.
DR   PaxDb; Q9R1K2; -.
DR   PRIDE; Q9R1K2; -.
DR   GeneID; 117242; -.
DR   KEGG; rno:117242; -.
DR   UCSC; RGD:727907; rat. [Q9R1K2-1]
DR   CTD; 57451; -.
DR   RGD; 727907; Tenm2.
DR   eggNOG; KOG1225; Eukaryota.
DR   eggNOG; KOG4659; Eukaryota.
DR   eggNOG; ENOG410XQQD; LUCA.
DR   HOGENOM; HOG000231701; -.
DR   HOVERGEN; HBG080306; -.
DR   InParanoid; Q9R1K2; -.
DR   OrthoDB; 7516at2759; -.
DR   PhylomeDB; Q9R1K2; -.
DR   PRO; PR:Q9R1K2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR   GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IDA:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IDA:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR   GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; ISS:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; TAS:RGD.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR   Gene3D; 2.120.10.30; -; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR022385; Rhs_assc_core.
DR   InterPro; IPR027689; Ten-2/3.
DR   InterPro; IPR009471; Ten_N.
DR   InterPro; IPR028916; Tox-GHH_dom.
DR   InterPro; IPR006530; YD.
DR   PANTHER; PTHR11219:SF64; PTHR11219:SF64; 2.
DR   Pfam; PF06484; Ten_N; 1.
DR   Pfam; PF15636; Tox-GHH; 1.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00179; EGF_CA; 2.
DR   SUPFAM; SSF49464; SSF49464; 1.
DR   TIGRFAMs; TIGR03696; Rhs_assc_core; 1.
DR   TIGRFAMs; TIGR01643; YD_repeat_2x; 1.
DR   PROSITE; PS00022; EGF_1; 8.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS51361; TENEURIN_N; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW   Cell projection; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain;
KW   Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW   Nucleus; Phosphoprotein; Postsynaptic cell membrane;
KW   Reference proteome; Repeat; Repressor; Synapse; Synaptosome;
KW   Transcription; Transcription regulation; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   2774       Teneurin-2.
FT                                /FTId=PRO_0000259503.
FT   CHAIN         1      ?       Ten-2 intracellular domain.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000421015.
FT   CHAIN       529   2774       Ten-2, soluble form. {ECO:0000250}.
FT                                /FTId=PRO_0000421016.
FT   TOPO_DOM      1    379       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    380    400       Helical. {ECO:0000255}.
FT   TOPO_DOM    401   2774       Extracellular. {ECO:0000255}.
FT   DOMAIN        1    375       Teneurin N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00694}.
FT   DOMAIN      575    603       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      605    634       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      636    668       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      669    701       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      702    735       EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      738    766       EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      769    797       EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      808    841       EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   REPEAT     1272   1316       NHL 1.
FT   REPEAT     1342   1386       NHL 2.
FT   REPEAT     1401   1452       NHL 3.
FT   REPEAT     1474   1501       NHL 4.
FT   REPEAT     1530   1573       NHL 5.
FT   REPEAT     1583   1602       YD 1.
FT   REPEAT     1619   1639       YD 2.
FT   REPEAT     1682   1701       YD 3.
FT   REPEAT     1702   1724       YD 4.
FT   REPEAT     1895   1914       YD 5.
FT   REPEAT     1936   1954       YD 6.
FT   REPEAT     1955   1975       YD 7.
FT   REPEAT     1982   1999       YD 8.
FT   REPEAT     2000   2021       YD 9.
FT   REPEAT     2022   2039       YD 10.
FT   REPEAT     2042   2062       YD 11.
FT   REPEAT     2065   2085       YD 12.
FT   REPEAT     2093   2113       YD 13.
FT   REPEAT     2119   2136       YD 14.
FT   REPEAT     2137   2163       YD 15.
FT   REPEAT     2165   2178       YD 16.
FT   REPEAT     2179   2202       YD 17.
FT   REPEAT     2205   2225       YD 18.
FT   REPEAT     2226   2246       YD 19.
FT   REPEAT     2248   2268       YD 20.
FT   REPEAT     2280   2300       YD 21.
FT   REPEAT     2302   2322       YD 22.
FT   REPEAT     2348   2389       YD 23.
FT   COMPBIAS    175    178       Poly-Ser.
FT   COMPBIAS    331    334       Poly-Ser.
FT   SITE        528    529       Cleavage. {ECO:0000250}.
FT   MOD_RES      90     90       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9WTS5}.
FT   MOD_RES     124    124       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q3UHK6}.
FT   MOD_RES     155    155       Phosphothreonine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   MOD_RES     157    157       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   CARBOHYD    443    443       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    482    482       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    925    925       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    948    948       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1267   1267       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1616   1616       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1712   1712       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1749   1749       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1773   1773       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1807   1807       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1892   1892       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1993   1993       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2197   2197       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2337   2337       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2648   2648       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    576    586       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    580    591       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    593    602       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    611    622       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    624    633       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    640    651       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    645    656       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    658    667       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    672    683       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    677    688       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    690    699       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    710    723       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    725    734       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    739    749       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    743    754       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    756    765       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    770    780       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    774    785       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    787    796       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    810    820       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    814    829       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    831    840       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ     605    669       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:10419693}.
FT                                /FTId=VSP_021395.
FT   VAR_SEQ     737    807       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:10419693}.
FT                                /FTId=VSP_021397.
FT   VAR_SEQ     799    807       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10419693}.
FT                                /FTId=VSP_021396.
SQ   SEQUENCE   2774 AA;  307474 MW;  7916D882A6C9E9A1 CRC64;
     MDVKDRRHRS LTRGRCGKEC RYTSSSLDSE DCRVPTQKSY SSSETLKAYD HDSRMHYGNR
     VTDLVHRESD EFSRQGANFT LAELGICEPS PHRSGYCSDM GILHQGYSLS TGSDADSDTE
     GGMSPEHAIR LWGRGIKSRR SSGLSSRENS ALTLTDSDNE NKSDDDNGRP IPPTSSSSLL
     PSAQLPSSHN PPPVSCQMPL LDSNTSHQIM DTNPDEEFSP NSYLLRACSG PQQASSSGPP
     NHHSQSTLRP PLPPPHNHTL SHHHSSANSL NRNSLTNRRS QIHAPAPAPN DLATTPESVQ
     LQDSWVLNSN VPLETRHFLF KTSSGSTPLF SSSSPGYPLT SGTVYTPPPR LLPRNTFSRK
     AFKLKKPSKY CSWKCAALSA IAAALLLAIL LAYFIAMHLL GLNWQLQPAD GHTFNNGVRT
     GLPGNDDVAT VPSGGKVPWS LKNSSIDSGE AEVGRRVTQE VPPGVFWRSQ IHISQPQFLK
     FNISLGKDAL FGVYIRRGLP PSHAQYDFME RLDGKEKWSV VESPRERRSI QTLVQNEAVF
     VQYLDVGLWH LAFYNDGKDK EMVSFNTVVL DSVQDCPRNC HGNGECVSGL CHCFPGFLGA
     DCAKAACPVL CSGNGQYSKG TCQCYSGWKG AECDVPMNQC IDPSCGGHGS CIDGNCVCAA
     GYKGEHCEEV DCLDPTCSSH GVCVNGECLC SPGWGGLNCE LARVQCPDQC SGHGTYLPDS
     GLCNCDPNWM GPDCSVEVCS VDCGTHGVCI GGACRCEEGW TGAACDQRVC HPRCIEHGTC
     KDGKCECREG WNGEHCTIGR QTAGTETDGC PDLCNGNGRC TLGQNSWQCV CQTGWRGPGC
     NVAMETSCAD NKDNEGDGLV DCLDPDCCLQ SACQNSLLCR GSRDPLDIIQ QGQTDWPAVK
     SFYDRIKLLA GKDSTHIIPG DNPFNSSLVS LIRGQVVTTD GTPLVGVNVS FVKYPKYGYT
     ITRQDGTFDL IANGGSALTL HFERAPFMSR ERTVWPPWNS FYAMDTLVMK TEENSIPSCD
     LSGFVRPDPI IISSPLSTFF SASPAANPIV PETQVLHEEI ELPGTNVKLR YLSSRTAGYK
     SLLKITMTQS TVPLNLIRVH LMVAVEGHLF QKSFQASPNL AYTFIWDKTD AYGQRVYGLS
     DAVVSVGFEY ETCPSLILWE KRTALLQGFE LDPSNLGGWS LDKHHTLNVK SGILLKGTGE
     NQFLTQQPAI ITSIMGNGRR RSISCPSCNG LAEGNKLLAP VALAVGIDGS LFVGDFNYIR
     RIFPSRNVTS ILELRNKEFK HSNSPGHKYY LAVDPVTGSL YVSDTNSRRI YRVKSLSGAK
     DLAGNSEVVA GTGEQCLPFD EARCGDGGKA VDATLMSPRG IAVDKNGLMY FVDATMIRKV
     DQNGIISTLL GSNDLTAVRP LSCDSSMDVA QVRLEWPTDL AVNPMDNSLY VLENNVILRI
     TENHQVSIIA GRPMHCQVPG IDYSLSKLAI HSALESASAI AISHTGVLYI TETDEKKINR
     LRQVTTNGEI CLLAGAASDC DCKNDVNCIC YSGDDAYATD AILNSPSSLA VAPDGTIYIA
     DLGNIRIRAV SKNKPVLNAF NQYEAASPGE QELYVFNADG IHQYTVSLVT GEYLYNFTYS
     ADNDVTELID NNGNSLKIRR DSSGMPRHLL MPDNQIITLT VGTNGGLKAV STQNLELGLM
     TYDGNTGLLA TKSDETGWTT FYDYDHEGRL TNVTRPTGVV TSLHREMEKS ITVDIENSNR
     DNDVTVITNL SSVEASYTVV QDQVRNSYQL CSNGTLRVMY ANGMGVSFHS EPHVLAGTLT
     PTIGRCNISL PMENGLNSIE WRLRKEQIKG KVTIFGRKLR VHGRNLLSID YDRNIRTEKI
     YDDHRKFTLR IIYDQVGRPF LWLPSSGLAA VNVSYFFNGR LAGLQRGAMS ERTDIDKQGR
     IVSRMFADGK VWSYSYLDKS MVLLLQSQRQ YIFEYDSSDR LHAVTMPSVA RHSMSTHTSI
     GYIRNIYNPP ESNASVIFDY SDDGRILKTS FLGTGRQVFY KYGKLSKLSE IVYDSTAVTF
     GYDETTGVLK MVNLQSGGFS CTIRYRKVGP LVDKQIYRFS EEGMINARFD YTYHDNSFRI
     ASIKPVISET PLPVDLYRYD EISGKVEHFG KFGVIYYDIN QIITTAVMTL SKHFDTHGRI
     KEVQYEMFRS LMYWMTVQYD SMGRVIKREL KLGPYANTTK YTYDYDGDGQ LQSVAVNDRP
     TWRYSYDLNG NLHLLNPGNS ARLMPLRYDL RDRITRLGDV QYKIDDDGYL CQRGSDIFEY
     NSKGLLTRAY NKASGWSVQY RYDGVSRRAS YKTNLGHHLQ YFYSDLHHPT RITHVYNHSN
     SEITSLYYDL QGHLFAMESS SGEEYYVASD NTGTPLAVFS INGLMIKQLQ YTAYGEIYYD
     SNPDFQMVIG FHGGLYDPLT KLVHFTQRDY DVLAGRWTSP DYTMWRNVGK EPAPFNLYMF
     KNNNPLSNEL DLKNYVTDVK SWLVMFGFQL SNIIPGFPRA KMYFVPPPYE LSESQASENG
     QLITGVQQTT ERHNQAFLAL EGQVISKKLH AGIREKAGHW FATTTPIIGK GIMFAIKEGR
     VTTGVSSIAS EDSRKVASVL NNAYYLDKMH YSIEGKDTHY FVKIGAADGD LVTLGTTIGR
     KVLESGVNVT VSQPTLLVNG RTRRFTNIEF QYSTLLLSIR YGLTPDTLDE EKARVLDQAR
     QRALGTAWAK EQQKARDGRE GSRLWTEGEK QQLLSTGRVQ GYEGYYVLPV EQYPELADSS
     SNIQFLRQNE MGKR
//
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