GenomeNet

Database: UniProt
Entry: NRX2A_HUMAN
LinkDB: NRX2A_HUMAN
Original site: NRX2A_HUMAN 
ID   NRX2A_HUMAN             Reviewed;        1712 AA.
AC   Q9P2S2; A7E2C1; Q9Y2D6;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 199.
DE   RecName: Full=Neurexin-2;
DE   AltName: Full=Neurexin II-alpha;
DE   AltName: Full=Neurexin-2-alpha;
DE   Flags: Precursor;
GN   Name=NRXN2; Synonyms=KIAA0921;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
RC   TISSUE=Fetal brain;
RA   Seki N., Yoshikawa T., Azuma T., Muramatsu M., Saito T.;
RT   "Human neurexin II.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2A).
RC   TISSUE=Brain;
RX   PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:63-70(1999).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2A).
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC       recognition and cell adhesion. May mediate intracellular signaling.
CC   -!- SUBUNIT: The laminin G-like domain 1 binds to NXPH1. Interacts with
CC       PATJ (By similarity). Interacts with CBLN1, CBLN2 and, less avidly,
CC       with CBLN4 (By similarity). Specific isoforms bind neuroligins NLGN1,
CC       NLGN2 and NLGN3 (By similarity). Specific isoforms bind to alpha-
CC       dystroglycan (By similarity). Interacts (via Laminin G-like 1 domain)
CC       with IGSF21 (Ig-like 1 domain) in a trans-interaction manner (By
CC       similarity). Interacts with CLSTN3 (By similarity).
CC       {ECO:0000250|UniProtKB:E9Q7X7, ECO:0000250|UniProtKB:Q63374,
CC       ECO:0000250|UniProtKB:Q63376}.
CC   -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC       {ECO:0000250|UniProtKB:Q9CS84}; Single-pass type I membrane protein
CC       {ECO:0000255}.
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 produced
CC         by alternative promoter usage. Beta-type isoforms differ from
CC         alpha-type isoforms in their N-terminus. Additional isoforms produced
CC         by alternative splicing seem to exist.;
CC       Name=1a;
CC         IsoId=Q9P2S2-1; Sequence=Displayed;
CC       Name=2a; Synonyms=Alpha-2B;
CC         IsoId=Q9P2S2-2; Sequence=VSP_003505, VSP_003506, VSP_003507,
CC                                  VSP_003508;
CC       Name=1b;
CC         IsoId=P58401-1; Sequence=External;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in brain.
CC   -!- PTM: O-glycosylated; contains heparan sulfate. Heparan sulfate
CC       attachment is required for synapse development by mediating
CC       interactions with neuroligins. {ECO:0000250|UniProtKB:E9Q7X7}.
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA76765.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB035266; BAA94075.1; -; mRNA.
DR   EMBL; AB023138; BAA76765.2; ALT_INIT; mRNA.
DR   EMBL; AC044790; AAK68154.1; -; Genomic_DNA.
DR   EMBL; BC150275; AAI50276.1; -; mRNA.
DR   CCDS; CCDS31597.1; -. [Q9P2S2-2]
DR   CCDS; CCDS8077.1; -. [Q9P2S2-1]
DR   RefSeq; NP_055895.1; NM_015080.3. [Q9P2S2-1]
DR   RefSeq; NP_620060.1; NM_138732.2. [Q9P2S2-2]
DR   AlphaFoldDB; Q9P2S2; -.
DR   SMR; Q9P2S2; -.
DR   BioGRID; 114780; 6.
DR   IntAct; Q9P2S2; 4.
DR   MINT; Q9P2S2; -.
DR   STRING; 9606.ENSP00000265459; -.
DR   GlyCosmos; Q9P2S2; 5 sites, 2 glycans.
DR   GlyGen; Q9P2S2; 8 sites, 3 O-linked glycans (2 sites).
DR   iPTMnet; Q9P2S2; -.
DR   PhosphoSitePlus; Q9P2S2; -.
DR   BioMuta; NRXN2; -.
DR   DMDM; 17369343; -.
DR   jPOST; Q9P2S2; -.
DR   MassIVE; Q9P2S2; -.
DR   PaxDb; 9606-ENSP00000265459; -.
DR   PeptideAtlas; Q9P2S2; -.
DR   ProteomicsDB; 83887; -. [Q9P2S2-1]
DR   ProteomicsDB; 83888; -. [Q9P2S2-2]
DR   Antibodypedia; 63686; 62 antibodies from 7 providers.
DR   DNASU; 9379; -.
DR   Ensembl; ENST00000265459.11; ENSP00000265459.5; ENSG00000110076.21. [Q9P2S2-1]
DR   Ensembl; ENST00000377559.7; ENSP00000366782.3; ENSG00000110076.21. [Q9P2S2-2]
DR   GeneID; 9379; -.
DR   KEGG; hsa:9379; -.
DR   MANE-Select; ENST00000265459.11; ENSP00000265459.5; NM_015080.4; NP_055895.1.
DR   UCSC; uc021qkw.2; human. [Q9P2S2-1]
DR   AGR; HGNC:8009; -.
DR   CTD; 9379; -.
DR   DisGeNET; 9379; -.
DR   GeneCards; NRXN2; -.
DR   HGNC; HGNC:8009; NRXN2.
DR   HPA; ENSG00000110076; Tissue enriched (brain).
DR   MIM; 600566; gene.
DR   neXtProt; NX_Q9P2S2; -.
DR   OpenTargets; ENSG00000110076; -.
DR   PharmGKB; PA31787; -.
DR   VEuPathDB; HostDB:ENSG00000110076; -.
DR   eggNOG; KOG3514; Eukaryota.
DR   GeneTree; ENSGT00940000155978; -.
DR   HOGENOM; CLU_001710_1_0_1; -.
DR   InParanoid; Q9P2S2; -.
DR   OMA; XHAGIGH; -.
DR   OrthoDB; 2999458at2759; -.
DR   PhylomeDB; Q9P2S2; -.
DR   TreeFam; TF321302; -.
DR   PathwayCommons; Q9P2S2; -.
DR   Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR   SignaLink; Q9P2S2; -.
DR   SIGNOR; Q9P2S2; -.
DR   BioGRID-ORCS; 9379; 16 hits in 1149 CRISPR screens.
DR   ChiTaRS; NRXN2; human.
DR   GenomeRNAi; 9379; -.
DR   Pharos; Q9P2S2; Tbio.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q9P2S2; Protein.
DR   Bgee; ENSG00000110076; Expressed in right hemisphere of cerebellum and 139 other cell types or tissues.
DR   ExpressionAtlas; Q9P2S2; baseline and differential.
DR   Genevisible; Q9P2S2; HS.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0005246; F:calcium channel regulator activity; ISS:BHF-UCL.
DR   GO; GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0097109; F:neuroligin family protein binding; ISS:BHF-UCL.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:BHF-UCL.
DR   GO; GO:0030534; P:adult behavior; IMP:BHF-UCL.
DR   GO; GO:0007268; P:chemical synaptic transmission; ISS:BHF-UCL.
DR   GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; ISS:BHF-UCL.
DR   GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; ISS:BHF-UCL.
DR   GO; GO:0007158; P:neuron cell-cell adhesion; TAS:BHF-UCL.
DR   GO; GO:0007269; P:neurotransmitter secretion; ISS:BHF-UCL.
DR   GO; GO:0097119; P:postsynaptic density protein 95 clustering; ISS:BHF-UCL.
DR   GO; GO:0097104; P:postsynaptic membrane assembly; ISS:BHF-UCL.
DR   GO; GO:0007165; P:signal transduction; ISS:BHF-UCL.
DR   GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
DR   GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL.
DR   GO; GO:0042297; P:vocal learning; IMP:BHF-UCL.
DR   GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00110; LamG; 6.
DR   Gene3D; 2.60.120.200; -; 6.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR003585; Neurexin-like.
DR   PANTHER; PTHR15036:SF52; NEUREXIN-2; 1.
DR   PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR   Pfam; PF02210; Laminin_G_2; 6.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00282; LamG; 6.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 6.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE   2: Evidence at transcript level;
KW   Alternative promoter usage; Alternative splicing; Calcium; Cell adhesion;
KW   Cell membrane; Cell projection; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Heparan sulfate; Membrane; Metal-binding; Proteoglycan;
KW   Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..1712
FT                   /note="Neurexin-2"
FT                   /id="PRO_0000019495"
FT   TOPO_DOM        29..1636
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1637..1657
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1658..1712
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..206
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          202..242
FT                   /note="EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          289..486
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          493..686
FT                   /note="Laminin G-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          690..727
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          732..904
FT                   /note="Laminin G-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          918..1093
FT                   /note="Laminin G-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          1096..1133
FT                   /note="EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          1137..1345
FT                   /note="Laminin G-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REGION          1373..1392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1458..1489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1525..1626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1679..1712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1575..1601
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1696..1712
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         335
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q28146"
FT   BINDING         352
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q28146"
FT   BINDING         420
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q28146"
FT   BINDING         779
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q28146"
FT   BINDING         796
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q28146"
FT   BINDING         854
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q28146"
FT   BINDING         1189
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT   BINDING         1206
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT   BINDING         1288
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT   BINDING         1290
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        841
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1400
FT                   /note="O-linked (Xyl...) (heparan sulfate) serine"
FT                   /evidence="ECO:0000250|UniProtKB:E9PUN2"
FT   DISULFID        206..219
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        213..229
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        231..241
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        450..486
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DISULFID        657..686
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DISULFID        694..705
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        699..714
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        716..726
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1065..1093
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DISULFID        1100..1111
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1105..1120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        1122..1132
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   VAR_SEQ         260..283
FT                   /note="Missing (in isoform 2a)"
FT                   /evidence="ECO:0000303|PubMed:10231032,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_003505"
FT   VAR_SEQ         393..399
FT                   /note="Missing (in isoform 2a)"
FT                   /evidence="ECO:0000303|PubMed:10231032,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_003506"
FT   VAR_SEQ         797..806
FT                   /note="DCLRVGCAPS -> G (in isoform 2a)"
FT                   /evidence="ECO:0000303|PubMed:10231032,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_003507"
FT   VAR_SEQ         1253..1282
FT                   /note="Missing (in isoform 2a)"
FT                   /evidence="ECO:0000303|PubMed:10231032,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_003508"
FT   VARIANT         81
FT                   /note="L -> Q (in dbSNP:rs12273892)"
FT                   /id="VAR_050266"
SQ   SEQUENCE   1712 AA;  184982 MW;  E4E8EC404DA1D0B0 CRC64;
     MASGSRWRPT PPPLLLLLLL ALAARADGLE FGGGPGQWAR YARWAGAASS GELSFSLRTN
     ATRALLLYLD DGGDCDFLEL LLVDGRLRLR FTLSCAEPAT LQLDTPVADD RWHMVLLTRD
     ARRTALAVDG EARAAEVRSK RREMQVASDL FVGGIPPDVR LSALTLSTVK YEPPFRGLLA
     NLKLGERPPA LLGSQGLRGA TADPLCAPAR NPCANGGLCT VLAPGEVGCD CSHTGFGGKF
     CSEEEHPMEG PAHLTLNSEV GSLLFSEGGA GRGGAGDVHQ PTKGKEEFVA TFKGNEFFCY
     DLSHNPIQSS TDEITLAFRT LQRNGLMLHT GKSADYVNLS LKSGAVWLVI NLGSGAFEAL
     VEPVNGKFND NAWHDVRVTR NLRQHAGIGH AMVNKLHYLV TISVDGILTT TGYTQEDYTM
     LGSDDFFYIG GSPNTADLPG SPVSNNFMGC LKDVVYKNND FKLELSRLAK EGDPKMKLQG
     DLSFRCEDVA ALDPVTFESP EAFVALPRWS AKRTGSISLD FRTTEPNGLL LFSQGRRAGG
     GAGSHSSAQR ADYFAMELLD GHLYLLLDMG SGGIKLRASS RKVNDGEWCH VDFQRDGRKG
     SISVNSRSTP FLATGDSEIL DLESELYLGG LPEGGRVDLP LPPEVWTAAL RAGYVGCVRD
     LFIDGRSRDL RGLAEAQGAV GVAPFCSRET LKQCASAPCR NGGVCREGWN RFICDCIGTG
     FLGRVCEREA TVLSYDGSMY MKIMLPNAMH TEAEDVSLRF MSQRAYGLMM ATTSRESADT
     LRLELDGGQM KLTVNLDCLR VGCAPSKGPE TLFAGHKLND NEWHTVRVVR RGKSLQLSVD
     NVTVEGQMAG AHMRLEFHNI ETGIMTERRF ISVVPSNFIG HLSGLVFNGQ PYMDQCKDGD
     ITYCELNARF GLRAIVADPV TFKSRSSYLA LATLQAYASM HLFFQFKTTA PDGLLLFNSG
     NGNDFIVIEL VKGYIHYVFD LGNGPSLMKG NSDKPVNDNQ WHNVVVSRDP GNVHTLKIDS
     RTVTQHSNGA RNLDLKGELY IGGLSKNMFS NLPKLVASRD GFQGCLASVD LNGRLPDLIA
     DALHRIGQVE RGCDGPSTTC TEESCANQGV CLQQWDGFTC DCTMTSYGGP VCNDPGTTYI
     FGKGGALITY TWPPNDRPST RMDRLAVGFS THQRSAVLVR VDSASGLGDY LQLHIDQGTV
     GVIFNVGTDD ITIDEPNAIV SDGKYHVVRF TRSGGNATLQ VDSWPVNERY PAGNFDNERL
     AIARQRIPYR LGRVVDEWLL DKGRQLTIFN SQAAIKIGGR DQGRPFQGQV SGLYYNGLKV
     LALAAESDPN VRTEGHLRLV GEGPSVLLSA ETTATTLLAD MATTIMETTT TMATTTTRRG
     RSPTLRDSTT QNTDDLLVAS AECPSDDEDL EECEPSTGGE LILPIITEDS LDPPPVATRS
     PFVPPPPTFY PFLTGVGATQ DTLPPPAARR PPSGGPCQAE RDDSDCEEPI EASGFASGEV
     FDSSLPPTDD EDFYTTFPLV TDRTTLLSPR KPAPRPNLRT DGATGAPGVL FAPSAPAPNL
     PAGKMNHRDP LQPLLENPPL GPGAPTSFEP RRPPPLRPGV TSAPGFPHLP TANPTGPGER
     GPPGAVEVIR ESSSTTGMVV GIVAAAALCI LILLYAMYKY RNRDEGSYQV DQSRNYISNS
     AQSNGAVVKE KAPAAPKTPS KAKKNKDKEY YV
//
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