GenomeNet

Database: UniProt
Entry: RPGF2_CANLF
LinkDB: RPGF2_CANLF
Original site: RPGF2_CANLF 
ID   RPGF2_CANLF             Reviewed;        1498 AA.
AC   F1PBJ0;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 2.
DT   10-APR-2019, entry version 67.
DE   RecName: Full=Rap guanine nucleotide exchange factor 2;
DE   AltName: Full=Cyclic nucleotide ras GEF;
DE            Short=CNrasGEF;
DE   AltName: Full=Neural RAP guanine nucleotide exchange protein;
DE            Short=nRap GEP;
DE   AltName: Full=PDZ domain-containing guanine nucleotide exchange factor 1;
DE            Short=PDZ-GEF1;
DE   AltName: Full=RA-GEF-1;
DE   AltName: Full=Ras/Rap1-associating GEF-1;
GN   Name=RAPGEF2; Synonyms=NRAPGEP, PDZGEF1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer;
RX   PubMed=16341006; DOI=10.1038/nature04338;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
RA   Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
RA   Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
RA   Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
RA   Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
RA   Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
RA   Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
RA   Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
RA   Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
RA   Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
RA   Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
RA   Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
RA   Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
RA   Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
RA   Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
RA   Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
RA   Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
RA   Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
RA   Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
RA   Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
RA   Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
RA   Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
RA   Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
RA   Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
RA   Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
RA   Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
RA   Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
RA   Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
RA   Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
RA   Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
RA   Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
RA   Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
RA   Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
RA   Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
RA   Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2]
RP   INTERACTION WITH CDH1; CTNNB1 AND TJP1, AND SUBCELLULAR LOCATION.
RX   PubMed=10873669; DOI=10.1006/bbrc.2000.3002;
RA   Kawajiri A., Itoh N., Fukata M., Nakagawa M., Yamaga M., Iwamatsu A.,
RA   Kaibuchi K.;
RT   "Identification of a novel beta-catenin-interacting protein.";
RL   Biochem. Biophys. Res. Commun. 273:712-717(2000).
CC   -!- FUNCTION: Functions as a guanine nucleotide exchange factor (GEF),
CC       which activates Rap and Ras family of small GTPases by exchanging
CC       bound GDP for free GTP in a cAMP-dependent manner. Serves as a
CC       link between cell surface receptors and Rap/Ras GTPases in
CC       intracellular signaling cascades. Acts also as an effector for
CC       Rap1 by direct association with Rap1-GTP thereby leading to the
CC       amplification of Rap1-mediated signaling. Shows weak activity on
CC       HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP or
CC       not. Its binding to ligand-activated beta-1 adrenergic receptor
CC       ADRB1 leads to the Ras activation through the G(s)-alpha signaling
CC       pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling
CC       pathway that leads to sustained inhibition of long term
CC       melanogenesis by reducing dendrite extension and melanin
CC       synthesis. Provides also inhibitory signals for cell proliferation
CC       of melanoma cells and promotes their apoptosis in a cAMP-
CC       independent nanner. Regulates cAMP-induced neuritogenesis by
CC       mediating the Rap1/B-Raf/ERK signaling through a pathway that is
CC       independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron
CC       migration and in the formation of the major forebrain fiber
CC       connections forming the corpus callosum, the anterior commissure
CC       and the hippocampal commissure during brain development. Involved
CC       in neuronal growth factor (NGF)-induced sustained activation of
CC       Rap1 at late endosomes and in brain-derived neurotrophic factor
CC       (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role
CC       in the regulation of embryonic blood vessel formation and in the
CC       establishment of basal junction integrity and endothelial barrier
CC       function. May be involved in the regulation of the vascular
CC       endothelial growth factor receptor KDR and cadherin CDH5
CC       expression at allantois endothelial cell-cell junctions.
CC   -!- SUBUNIT: Found in a complex, at least composed of KIDINS220,
CC       MAGI2, NTRK1 and RAPGEF2; the complex is mainly formed at late
CC       endosomes in a neuronal growth factor (NGF)-dependent manner.
CC       Interacts (via C-terminal domain) with NEDD4 (via WW domains);
CC       this interaction leads to ubiquitination and degradation via the
CC       proteasome pathway in a cAMP-independent manner. Interacts with
CC       MAGI1 (via PDZ domain). Interacts with ADRB1 (via C-terminal PDZ
CC       motif); the interaction is direct. Interacts (via Ras-associating
CC       domain) with RAP1A (via GTP-bound active form). Interacts weakly
CC       with HRAS (via GDP- and GTP-bound forms). Interacts (via C-
CC       terminal domain) with MAGI2 (via PDZ and WW domains) (By
CC       similarity). Interacts with CDH1, CTNNB1 and TJP1. {ECO:0000250,
CC       ECO:0000269|PubMed:10873669}.
CC   -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:10873669}.
CC       Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region
CC       {ECO:0000250}. Cell membrane {ECO:0000250}. Late endosome
CC       {ECO:0000250}. Note=Associated with the synaptic plasma membrane.
CC       Localized diffusely in the cytoplasm before neuronal growth factor
CC       (NGF) stimulation. Recruited to late endosomes after NGF
CC       stimulation. Colocalized with the high affinity nerve growth
CC       factor receptor NTRK1 at late endosomes. Translocated to the
CC       perinuclear region in a RAP1A-dependent manner. Translocated to
CC       the cell membrane (By similarity). Colocalized with CTNNB1 and
CC       TJP1 at cell-cell contacts. {ECO:0000250}.
CC   -!- DOMAIN: The Ras-associating domain is necessary for the Rap
CC       guanine nucleotide exchange activity. The N-terminal regionis
CC       necessary for cAMP-binding. The PDZ domain is necessary for its
CC       targeting to the cell membrane (By similarity). {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by NEDD4, leading to proteasomal degradation.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylation by PLK2 promotes its activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RAPGEF2 family. {ECO:0000305}.
DR   EMBL; AAEX03010088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003639545.1; XM_003639497.3.
DR   IntAct; F1PBJ0; 1.
DR   STRING; 9612.ENSCAFP00000012838; -.
DR   PaxDb; F1PBJ0; -.
DR   PRIDE; F1PBJ0; -.
DR   Ensembl; ENSCAFT00000013877; ENSCAFP00000012838; ENSCAFG00000008719.
DR   GeneID; 100856359; -.
DR   KEGG; cfa:100856359; -.
DR   CTD; 9693; -.
DR   VGNC; VGNC:45347; RAPGEF2.
DR   eggNOG; KOG3542; Eukaryota.
DR   eggNOG; ENOG410XS6B; LUCA.
DR   GeneTree; ENSGT00940000156418; -.
DR   InParanoid; F1PBJ0; -.
DR   KO; K08018; -.
DR   OMA; EVCSEHN; -.
DR   OrthoDB; 31139at2759; -.
DR   TreeFam; TF313184; -.
DR   Reactome; R-CFA-5673001; RAF/MAP kinase cascade.
DR   Proteomes; UP000002254; Chromosome 15.
DR   Bgee; ENSCAFG00000008719; Expressed in 3 organ(s), highest expression level in prefrontal cortex.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
DR   GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0031697; F:beta-1 adrenergic receptor binding; ISS:UniProtKB.
DR   GO; GO:0030552; F:cAMP binding; ISS:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
DR   GO; GO:0070300; F:phosphatidic acid binding; IEA:Ensembl.
DR   GO; GO:0017034; F:Rap guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0050699; F:WW domain binding; ISS:UniProtKB.
DR   GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001568; P:blood vessel development; ISS:UniProtKB.
DR   GO; GO:0031547; P:brain-derived neurotrophic factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR   GO; GO:0071321; P:cellular response to cGMP; ISS:UniProtKB.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0061028; P:establishment of endothelial barrier; ISS:UniProtKB.
DR   GO; GO:0090557; P:establishment of endothelial intestinal barrier; IEA:Ensembl.
DR   GO; GO:0021884; P:forebrain neuron development; ISS:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030033; P:microvillus assembly; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048022; P:negative regulation of melanin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0038180; P:nerve growth factor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR   GO; GO:2000481; P:positive regulation of cAMP-dependent protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR   GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; ISS:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:2001224; P:positive regulation of neuron migration; ISS:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR   GO; GO:0032092; P:positive regulation of protein binding; ISS:UniProtKB.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:2001214; P:positive regulation of vasculogenesis; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
DR   GO; GO:1901888; P:regulation of cell junction assembly; ISS:UniProtKB.
DR   GO; GO:0021591; P:ventricular system development; ISS:UniProtKB.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00155; RasGEF; 1.
DR   CDD; cd06224; REM; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR030739; RapGEF2.
DR   InterPro; IPR008937; Ras-like_GEF.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR023578; Ras_GEF_dom_sf.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23113; PTHR23113; 1.
DR   PANTHER; PTHR23113:SF217; PTHR23113:SF217; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SUPFAM; SSF48366; SSF48366; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Complete proteome; Cytoplasm;
KW   Developmental protein; Differentiation; Endosome; GTPase activation;
KW   Guanine-nucleotide releasing factor; Membrane; Neurogenesis;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN         1   1498       Rap guanine nucleotide exchange factor 2.
FT                                /FTId=PRO_0000423854.
FT   DOMAIN      267    380       N-terminal Ras-GEF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00135}.
FT   DOMAIN      385    468       PDZ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00143}.
FT   DOMAIN      606    692       Ras-associating. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00166}.
FT   DOMAIN      717    944       Ras-GEF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00168}.
FT   NP_BIND     135    252       cNMP.
FT   COMPBIAS     87     90       Poly-Asp.
FT   COMPBIAS   1038   1045       Poly-Pro.
FT   COMPBIAS   1107   1165       Ser-rich.
FT   MOD_RES     501    501       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1M386}.
FT   MOD_RES     644    644       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:F1M386}.
FT   MOD_RES     806    806       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1M386}.
FT   MOD_RES     930    930       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1M386}.
FT   MOD_RES     933    933       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1M386}.
FT   MOD_RES    1022   1022       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CHG7}.
FT   MOD_RES    1079   1079       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Y4G8}.
FT   MOD_RES    1088   1088       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Y4G8}.
FT   MOD_RES    1094   1094       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Y4G8}.
FT   MOD_RES    1115   1115       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CHG7}.
FT   MOD_RES    1119   1119       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8CHG7}.
FT   MOD_RES    1158   1158       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Y4G8}.
FT   MOD_RES    1175   1175       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:F1M386}.
SQ   SEQUENCE   1498 AA;  167320 MW;  CCA24CD5403DB165 CRC64;
     MKPLAIPANH GVMGQQEKHS LPADFTKLHL TDSLHPQVTH VSSSHSGCSI TSDSGSSSLS
     DIYQATESEA GDMDLSGLPE TAVDSEDDDD EEDIERASDP LMSRDIVRDC LEKDPIDRTD
     DDIEQLLEFM HQLPAFANMT MSVRRELCAV MVFAVVERAG TIVLNDGEEL DSWSVILNGS
     VEVTYPDGKA EILCMGNSFG VSPTMDKEYM KGVMRTKVDD CQFVCIAQQD YCRILNQVEK
     NMQKVEEEGE IVMVKEHREL DRTGTRKGHI VIKGTSERLT MHLVEEHSVV DPTFIEDFLL
     TYRTFLSSPM EVGKKLLEWF NDPSLRDKVT RVVLLWVNNH FNDFEGDPAM TRFLEEFENN
     LEREKMGGHL RLLNIACAAK AKRRLMTLTK PSREAPLPFI LLGGSEKGFG IFVDSVDSGS
     KATEAGLKRG DQILEVNGQN FENIQLSKAM EILRNNTHLS ITVKTNLFVF KELLTRLSEE
     KRNGAPHLPK IGDIKKASRY SIPDLAVDVE QVIGLEKVNK KSKANTVGGR NKLKKILDKT
     RISILPQKPY NDIGIGQSQD DSIVGLRQTK HIPTALPVSG TLSSSNPDLL QSHHRILDFS
     TTPDLPDQVL RVFKADQQSR YIMISKDTTA KEVVIQAIRE FAVTATPDQY SLCEVSVTPE
     GVIKQRRLPD QLSKLADRIQ LSGRYYLKNN METETLCSDE DAQELLRESQ ISLLQLSTVE
     VATQLSMRNF ELFRNIEPTE YIDDLFKLKS KTSCANLKKF EEVINQETFW VASEILRETN
     QLKRMKIIKH FIKIALHCRE CKNFNSMFAI ISGLNLAPVA RLRTTWEKLP NKYEKLFQDL
     QDLFDPSRNM AKYRNVLNSQ NLQPPIIPLF PVIKKDLTFL HEGNDSKVDG LVNFEKLRMI
     AKEIRHVGRM ASVNMDPALM FRTRKKKWRS LGSLSQGSTN ATVLDVAQTG GHKKRVRRSS
     FLNAKKLYED AQMARKVKQY LSNLELEMDE ESLQTLSLQC EPATNTLPKN PGDKKPVKSE
     TSPVAPRAGS QQKAQAQPPP PQPQPQHKIN QGLQVPAVSL YPSRKKVPVK DLPPFGINSP
     QALKKILSLS EEGSLERHKK QAEDTISNAS SQLSSPPTSP QSSPRKGYTL APSGTVDNFS
     DSGHSEISSR SSIVSNSSFD SVPVSLHEER RQRHSVSIVE TNLGVGRMER RTMMEPDQYS
     LGSYAPMAES RGLYATATVI SSPSTEELSQ DQGDRASLDA ADSGRGSWTS CSSGSHDNIQ
     TIQHQRSWET LPFGHTHFDY SGDPAGLWAS SSHMDQIMFS DHSTKYNRQN QSRESLEQAQ
     SRASWASSTG YWGEDSEGDT GTIKRRGGKD VSIEAESSSV TSVTTEETKP VPMPAHVAVT
     SSTAKGLIVR KEGRYREPPP TPPGYIGIPI TDFPEGHSHP ARKPPDYNVA LQRSRMVARP
     TDTAAPSPIQ QPHGHPASGR PVNKPQWHKP NECDPRLAPY QSQGFSTEED EDEQVSAV
//
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