GenomeNet

Database: UniProt
Entry: Q6P9K9
LinkDB: Q6P9K9
Original site: Q6P9K9 
ID   NRX3A_MOUSE             Reviewed;        1571 AA.
AC   Q6P9K9; E9PW93; E9Q466; Q8CCT8;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 2.
DT   16-JAN-2019, entry version 120.
DE   RecName: Full=Neurexin-3;
DE   AltName: Full=Neurexin III-alpha;
DE   AltName: Full=Neurexin-3-alpha;
DE   Flags: Precursor;
GN   Name=Nrxn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2A).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=19926856; DOI=10.1073/pnas.0809510106;
RA   Bottos A., Destro E., Rissone A., Graziano S., Cordara G.,
RA   Assenzio B., Cera M.R., Mascia L., Bussolino F., Arese M.;
RT   "The synaptic proteins neurexins and neuroligins are widely expressed
RT   in the vascular system and contribute to its functions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:20782-20787(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Neuronal cell surface protein that may be involved in
CC       cell recognition and cell adhesion. May mediate intracellular
CC       signaling (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The laminin G-like domain 2 binds to NXPH1. Specific
CC       isoforms bind to alpha-dystroglycan. The cytoplasmic C-terminal
CC       region binds to CASK (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       O14522:PTPRT (xeno); NbExp=2; IntAct=EBI-7281557, EBI-728180;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC         Comment=A number of isoforms, alpha-type and beta-type are
CC         produced by alternative promoter usage. Beta-type isoforms
CC         differ from alpha-type isoforms in their N-terminus.;
CC       Name=1a;
CC         IsoId=Q6P9K9-1; Sequence=Displayed;
CC       Name=2a;
CC         IsoId=Q6P9K9-2; Sequence=VSP_041710, VSP_041711, VSP_041712;
CC         Note=Produced by alternative splicing.;
CC       Name=1b;
CC         IsoId=Q8C985-1; Sequence=External;
CC   -!- TISSUE SPECIFICITY: Brain and arteries (at protein level).
CC       {ECO:0000269|PubMed:19926856}.
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH60719.1; Type=Miscellaneous discrepancy; Note=Contains an insert which is not supported by any other transcript and which does not match with the genome.; Evidence={ECO:0000305};
DR   EMBL; AK032126; BAC27716.1; -; mRNA.
DR   EMBL; AC115709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC115744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC115910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC120383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC155231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC155274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC156637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC161049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC171335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAAA01025627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR974428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR974583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT009613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT009725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT010588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU041252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC060719; AAH60719.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS49134.1; -. [Q6P9K9-2]
DR   CCDS; CCDS56856.1; -. [Q6P9K9-1]
DR   RefSeq; NP_001185516.2; NM_001198587.3. [Q6P9K9-1]
DR   RefSeq; NP_766132.2; NM_172544.3. [Q6P9K9-2]
DR   RefSeq; XP_006515620.1; XM_006515557.1. [Q6P9K9-1]
DR   UniGene; Mm.425766; -.
DR   UniGene; Mm.487864; -.
DR   PDB; 3MW4; X-ray; 2.00 A; A/B/C=1090-1293.
DR   PDBsum; 3MW4; -.
DR   ProteinModelPortal; Q6P9K9; -.
DR   SMR; Q6P9K9; -.
DR   IntAct; Q6P9K9; 2.
DR   MINT; Q6P9K9; -.
DR   STRING; 10090.ENSMUSP00000129678; -.
DR   iPTMnet; Q6P9K9; -.
DR   PhosphoSitePlus; Q6P9K9; -.
DR   PaxDb; Q6P9K9; -.
DR   PeptideAtlas; Q6P9K9; -.
DR   PRIDE; Q6P9K9; -.
DR   Ensembl; ENSMUST00000057634; ENSMUSP00000050075; ENSMUSG00000066392. [Q6P9K9-2]
DR   Ensembl; ENSMUST00000163134; ENSMUSP00000129678; ENSMUSG00000066392. [Q6P9K9-1]
DR   Ensembl; ENSMUST00000167887; ENSMUSP00000127926; ENSMUSG00000066392. [Q6P9K9-2]
DR   GeneID; 18191; -.
DR   KEGG; mmu:18191; -.
DR   UCSC; uc007okc.2; mouse. [Q6P9K9-2]
DR   UCSC; uc033ger.1; mouse. [Q6P9K9-1]
DR   CTD; 9369; -.
DR   MGI; MGI:1096389; Nrxn3.
DR   eggNOG; KOG3514; Eukaryota.
DR   eggNOG; ENOG410XNU6; LUCA.
DR   GeneTree; ENSGT00940000154618; -.
DR   HOGENOM; HOG000230481; -.
DR   HOVERGEN; HBG052670; -.
DR   InParanoid; Q6P9K9; -.
DR   KO; K07377; -.
DR   OrthoDB; 35129at2759; -.
DR   TreeFam; TF321302; -.
DR   Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR   ChiTaRS; Nrxn3; mouse.
DR   EvolutionaryTrace; Q6P9K9; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   Bgee; ENSMUSG00000066392; Expressed in 227 organ(s), highest expression level in rostral migratory stream.
DR   ExpressionAtlas; Q6P9K9; baseline and differential.
DR   Genevisible; Q6P9K9; MM.
DR   GO; GO:0098982; C:GABA-ergic synapse; IMP:SynGO.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042734; C:presynaptic membrane; ISA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR   GO; GO:0005246; F:calcium channel regulator activity; IGI:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007268; P:chemical synaptic transmission; IGI:MGI.
DR   GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:SynGO.
DR   GO; GO:0007416; P:synapse assembly; IGI:MGI.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR037440; Neurexin.
DR   InterPro; IPR003585; Neurexin-like.
DR   InterPro; IPR027789; Syndecan/Neurexin_dom.
DR   PANTHER; PTHR44287; PTHR44287; 2.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF02210; Laminin_G_2; 6.
DR   Pfam; PF01034; Syndecan; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00282; LamG; 6.
DR   SUPFAM; SSF49899; SSF49899; 6.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative promoter usage; Alternative splicing;
KW   Calcium; Cell adhesion; Complete proteome; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Metal-binding;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     27       {ECO:0000255}.
FT   CHAIN        28   1571       Neurexin-3.
FT                                /FTId=PRO_0000412557.
FT   TOPO_DOM     28   1496       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1497   1517       Helical. {ECO:0000255}.
FT   TOPO_DOM   1518   1571       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       28    202       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      198    235       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      258    440       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      447    639       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      643    680       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      685    857       Laminin G-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN      871   1046       Laminin G-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     1049   1086       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1090   1290       Laminin G-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   COMPBIAS   1302   1328       Thr-rich.
FT   METAL       304    304       Calcium. {ECO:0000250}.
FT   METAL       321    321       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       374    374       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   CARBOHYD     58     58       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    105    105       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    757    757       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1189   1189       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1287   1287       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1331   1331       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    202    213       {ECO:0000250}.
FT   DISULFID    207    222       {ECO:0000250}.
FT   DISULFID    224    234       {ECO:0000250}.
FT   DISULFID    404    440       {ECO:0000250}.
FT   DISULFID    610    639       {ECO:0000250}.
FT   DISULFID    647    658       {ECO:0000250}.
FT   DISULFID    652    667       {ECO:0000250}.
FT   DISULFID    669    679       {ECO:0000250}.
FT   DISULFID   1018   1046       {ECO:0000250}.
FT   DISULFID   1053   1064       {ECO:0000250}.
FT   DISULFID   1058   1073       {ECO:0000250}.
FT   DISULFID   1075   1085       {ECO:0000250}.
FT   VAR_SEQ       1    373       Missing (in isoform 2a).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_041710.
FT   VAR_SEQ    1047   1047       E -> EVALTKADLQ (in isoform 2a).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_041711.
FT   VAR_SEQ    1364   1470       Missing (in isoform 2a).
FT                                {ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_041712.
FT   CONFLICT    390    390       A -> T (in Ref. 1; BAC27716).
FT                                {ECO:0000305}.
FT   STRAND     1091   1104       {ECO:0000244|PDB:3MW4}.
FT   HELIX      1107   1109       {ECO:0000244|PDB:3MW4}.
FT   STRAND     1113   1123       {ECO:0000244|PDB:3MW4}.
FT   STRAND     1127   1137       {ECO:0000244|PDB:3MW4}.
FT   STRAND     1143   1149       {ECO:0000244|PDB:3MW4}.
FT   STRAND     1152   1162       {ECO:0000244|PDB:3MW4}.
FT   STRAND     1164   1167       {ECO:0000244|PDB:3MW4}.
FT   STRAND     1175   1177       {ECO:0000244|PDB:3MW4}.
FT   STRAND     1179   1186       {ECO:0000244|PDB:3MW4}.
FT   STRAND     1189   1194       {ECO:0000244|PDB:3MW4}.
FT   STRAND     1200   1202       {ECO:0000244|PDB:3MW4}.
FT   STRAND     1245   1252       {ECO:0000244|PDB:3MW4}.
FT   HELIX      1253   1255       {ECO:0000244|PDB:3MW4}.
FT   STRAND     1261   1268       {ECO:0000244|PDB:3MW4}.
FT   HELIX      1273   1278       {ECO:0000244|PDB:3MW4}.
FT   STRAND     1284   1293       {ECO:0000244|PDB:3MW4}.
SQ   SEQUENCE   1571 AA;  173428 MW;  98F989F5DD2B71AB CRC64;
     MSFTLHSVFF TLKVSIFLGS LVGLCLGLEF MGLPNQWARY LRWDASTRSD LSFQFKTNVS
     TGLLLYLDDG GVCDFLCLSL VDGRVQLRFS MDCAETTVLS NKQVNDSSWH FLMVSRDRVR
     TGLVIDGEGQ SGELRPQRPY MDVVSDLFLG GVPADIRPSA LTLDGVQSMP GFKGLMLDLK
     YGNSEPRLLG SQSVQLEAEG PCGERPCENG GICFLLDGHP TCDCSTTGYG GTLCSEDVSQ
     GPGLSHLMMS EQAREENVAT FRGSEYLCYD LSQNPIQSSS DEITLSFKTW QRNGLILHTG
     KSADYVNLAL KDGAVSLVIN LGSGAFEAIV EPVNGKFNDN AWHDVKVTRN LRQVTISVDG
     ILTTTGYTQE DYTMLGSDDF FYVGGSPSTA DLPGSPVSNN FMGCLKEVVY KNNDIRLELS
     RLARIGDTKM KIYGEVVFKC ENVATLDPIN FETPEAYISL PKWNTKRMGS ISFDFRTTEP
     NGLILFTHGK PQERKDVRSQ KNTKVDFFAV ELLDGNLYLL LDMGSGTIKV KATQKKANDG
     EWYHVDIQRD GRSGTISVNS RRTPFTASGE SEILDLEGDM YLGGLPENRA GLILPTELWT
     AMLNYGYVGC IRDLFIDGRS KNIRQLAEMQ NAAGVKSSCS RMSAKQCDSY PCKNNAVCKD
     GWNRFICDCT GTGYWGRTCE REASILSYDG SMYMKVIMPM VMHTEAEDVS FRFMSQRAYG
     LLVATTSRDS ADTLRLELDG GRVKLMVNLD CIRINCNSSK GPETLYAGQK LNDNEWHTVR
     VVRRGKSLKL TVDDDVAEGT MVGDHTRLEF HNIETGIMTE KRYISVVPSS FIGHLQSLMF
     NGLLYIDLCK NGDIDYCELK ARFGLRNIIA DPVTFKTKSS YLTLATLQAY TSMHLFFQFK
     TTSADGFILF NSGDGNDFIA VELVKGYIHY VFDLGNGPNV IKGNSDRPLN DNQWHNVVIT
     RDSSNTHSLK VDTKVVTQVI NGAKNLDLKG DLYMAGLAQG MYSNLPKLVA SRDGFQGCLA
     SVDLNGRLPD LINDALHRSG QIERGCEGPS TTCQEDSCAN QGVCMQQWEG FTCDCSMTSY
     SGNQCNDPGA TYIFGKSGGL ILYTWPANDR PSTRSDRLAV GFSTTVKDGI LVRIDSAPGL
     GDFLQLHIEQ GKIGVVFNIG TVDISIKEER TPVNDGKYHV VRFTRNGGNA TLQVDNWPVN
     EHYPTGNTDN ERLQMVKQKI PFKYNRPVEE WLQEKGRQLT IFNTQAQIAI GGKDKGRLFQ
     GQLSGLYYDG LKVLNMAAEN NPNIKINGSV RLVGEVPSVS GTTQTTSMPP EMSTTVMETT
     TTMATTTTRK NRSTASIQPT SDDLVSSAEC SSDDEDFVEC EPSTDKSLST SIFEGGYKAH
     APKWESKDFR PNKVSETSRT TTTSLSPELI RFTASSSSGM VPKLPAGKMN NRDLKPQPDI
     VLLPLPTAYE LDSTKLKSPL ITSPMFRNVP TANPTEPGIR RVPGASEVIR ESSSTTGMVV
     GIVAAAALCI LILLYAMYKY RNRDEGSYQV DETRNYISNS AQSNGTLMKE KQASSKSGHK
     KQKNKDKEYY V
//
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