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Database: UniProt
Entry: P58400
LinkDB: P58400
Original site: P58400 
ID   NRX1B_HUMAN             Reviewed;         472 AA.
AC   P58400; E7ETA5;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2017, sequence version 3.
DT   07-APR-2021, entry version 166.
DE   RecName: Full=Neurexin-1-beta;
DE   AltName: Full=Neurexin I-beta;
DE   Flags: Precursor;
GN   Name=NRXN1;
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 3B).
RC   TISSUE=Brain;
RX   PubMed=9921901; DOI=10.1007/s004390050889;
RA   Kleiderlein J.J., Nisson P.E., Jessee J., Li W.B., Becker K.G., Derby M.L.,
RA   Ross C.A., Margolis R.L.;
RT   "CCG repeats in cDNAs from human brain.";
RL   Hum. Genet. 103:666-673(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   INTERACTION WITH STAPHYLOCOCCUS AUREUS PROTEIN SDRC (MICROBIAL INFECTION).
RX   PubMed=20090838; DOI=10.1371/journal.ppat.1000726;
RA   Barbu E.M., Ganesh V.K., Gurusiddappa S., Mackenzie R.C., Foster T.J.,
RA   Sudhof T.C., Hoeoek M.;
RT   "beta-Neurexin is a ligand for the Staphylococcus aureus MSCRAMM SdrC.";
RL   PLoS Pathog. 6:E1000726-E1000726(2010).
RN   [4]
RP   INTERACTION WITH CBLN1, AND REGION.
RX   PubMed=27418511; DOI=10.1126/science.aae0104;
RA   Elegheert J., Kakegawa W., Clay J.E., Shanks N.F., Behiels E., Matsuda K.,
RA   Kohda K., Miura E., Rossmann M., Mitakidis N., Motohashi J., Chang V.T.,
RA   Siebold C., Greger I.H., Nakagawa T., Yuzaki M., Aricescu A.R.;
RT   "Structural basis for integration of GluD receptors within synaptic
RT   organizer complexes.";
RL   Science 353:295-299(2016).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 85-296 IN COMPLEX WITH MOUSE
RP   NLRG1, AND CALCIUM-BINDING SITES.
RX   PubMed=18084303; DOI=10.1038/nsmb1350;
RA   Chen X., Liu H., Shim A.H., Focia P.J., He X.;
RT   "Structural basis for synaptic adhesion mediated by neuroligin-neurexin
RT   interactions.";
RL   Nat. Struct. Mol. Biol. 15:50-56(2008).
CC   -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC       recognition and cell adhesion by forming intracellular junctions
CC       through binding to neuroligins. May play a role in formation or
CC       maintenance of synaptic junctions. May mediate intracellular signaling.
CC       May play a role in angiogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The cytoplasmic C-terminal region binds to CASK. Binds NLGN1,
CC       NLGN2 and NLGN3, DAG1 (alpha-dystroglycan) and alpha-latrotoxin.
CC       Binding to neuroligins is calcium-dependent, and the binding preference
CC       ranks as follow: NLGN1 > NLGN4 >> NLGN3 > NLGN2 (By similarity).
CC       Interacts with CBLN2 and more weakly with CBLN4 (By similarity).
CC       Interacts with CBLN1; interaction is CBLN1 hexamer form-dependent;
CC       CBLN1-binding is calcium-independent; isoform 1b does not interact with
CC       CBLN1 (PubMed:27418511). {ECO:0000250|UniProtKB:P0DI97,
CC       ECO:0000250|UniProtKB:Q63373, ECO:0000269|PubMed:27418511}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC       protein SdrC; this interaction increases S. aureus adherence to cells.
CC       {ECO:0000269|PubMed:20090838}.
CC   -!- INTERACTION:
CC       P58400-1; Q99K10-1: Nlgn1; Xeno; NbExp=3; IntAct=EBI-16513622, EBI-15675933;
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, presynaptic cell membrane
CC       {ECO:0000250|UniProtKB:Q63373}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:Q63373}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
CC         Comment=A number of isoforms are produced by alternative promoter
CC         usage including the alpha-type and beta-type isoforms which differ in
CC         their N-terminus. Additional isoforms may be produced by alternative
CC         splicing.;
CC       Name=1b;
CC         IsoId=P58400-2; Sequence=Displayed;
CC       Name=3b;
CC         IsoId=P58400-1; Sequence=VSP_059057;
CC       Name=1a;
CC         IsoId=Q9ULB1-1; Sequence=External;
CC       Name=2a;
CC         IsoId=Q9ULB1-2; Sequence=External;
CC       Name=3a;
CC         IsoId=Q9ULB1-3; Sequence=External;
CC       Name=4;
CC         IsoId=Q9ULB1-4; Sequence=External;
CC   -!- PTM: Highly O-glycosylated and minor N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AF064842; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF064842; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC007462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC007560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC007680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC007682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC009234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC010721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC068715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC068725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC069550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC078994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS1845.1; -. [P58400-1]
DR   CCDS; CCDS82446.1; -. [P58400-2]
DR   RefSeq; NP_001317021.1; NM_001330092.1. [P58400-2]
DR   RefSeq; NP_620072.1; NM_138735.4. [P58400-1]
DR   PDB; 3B3Q; X-ray; 2.40 A; E/F=85-296.
DR   PDB; 5Z8Y; X-ray; 3.40 A; B/D/F/H=86-296.
DR   PDBsum; 3B3Q; -.
DR   PDBsum; 5Z8Y; -.
DR   SMR; P58400; -.
DR   BioGRID; 114779; 16.
DR   ComplexPortal; CPX-4101; NLGN1(+SSA+SSB) - NRXN1-beta(-SS4) complex. [P58400-1]
DR   ComplexPortal; CPX-909; NLGN1(-SSA-SSB) - NRXN1-beta(-SS4) complex. [P58400-1]
DR   DIP; DIP-46402N; -.
DR   IntAct; P58400; 1.
DR   iPTMnet; P58400; -.
DR   BioMuta; NRXN1; -.
DR   DMDM; 322510054; -.
DR   MassIVE; P58400; -.
DR   PeptideAtlas; P58400; -.
DR   PRIDE; P58400; -.
DR   ProteomicsDB; 18162; -.
DR   ProteomicsDB; 57071; -. [P58400-1]
DR   ABCD; P58400; 2 sequenced antibodies.
DR   Antibodypedia; 30173; 280 antibodies.
DR   Ensembl; ENST00000342183; ENSP00000341184; ENSG00000179915. [P58400-1]
DR   Ensembl; ENST00000401710; ENSP00000385580; ENSG00000179915. [P58400-2]
DR   GeneID; 9378; -.
DR   KEGG; hsa:9378; -.
DR   UCSC; uc010fbp.4; human. [P58400-2]
DR   CTD; 9378; -.
DR   DisGeNET; 9378; -.
DR   GeneCards; NRXN1; -.
DR   HGNC; HGNC:8008; NRXN1.
DR   HPA; ENSG00000179915; Tissue enriched (brain).
DR   MalaCards; NRXN1; -.
DR   MIM; 600565; gene.
DR   neXtProt; NX_P58400; -.
DR   OpenTargets; ENSG00000179915; -.
DR   VEuPathDB; HostDB:ENSG00000179915.21; -.
DR   GeneTree; ENSGT00940000154292; -.
DR   PathwayCommons; P58400; -.
DR   Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR   SIGNOR; P58400; -.
DR   BioGRID-ORCS; 9378; 1 hit in 978 CRISPR screens.
DR   ChiTaRS; NRXN1; human.
DR   EvolutionaryTrace; P58400; -.
DR   GeneWiki; NRXN1; -.
DR   GenomeRNAi; 9378; -.
DR   Pharos; P58400; Tbio.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000179915; Expressed in corpus callosum and 196 other tissues.
DR   ExpressionAtlas; P58400; baseline and differential.
DR   Genevisible; P58400; HS.
DR   GO; GO:0044295; C:axonal growth cone; ISS:BHF-UCL.
DR   GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR   GO; GO:0030139; C:endocytic vesicle; ISS:BHF-UCL.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL.
DR   GO; GO:0099056; C:integral component of presynaptic membrane; TAS:BHF-UCL.
DR   GO; GO:0043025; C:neuronal cell body; ISS:BHF-UCL.
DR   GO; GO:0031965; C:nuclear membrane; ISS:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR   GO; GO:0098793; C:presynapse; NAS:ARUK-UCL.
DR   GO; GO:0042734; C:presynaptic membrane; ISS:BHF-UCL.
DR   GO; GO:0031982; C:vesicle; ISS:BHF-UCL.
DR   GO; GO:0048306; F:calcium-dependent protein binding; 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:ARUK-UCL.
DR   GO; GO:0005102; F:signaling receptor binding; ISS:BHF-UCL.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:BHF-UCL.
DR   GO; GO:0005105; F:type 1 fibroblast growth factor receptor binding; IDA:ARUK-UCL.
DR   GO; GO:0030534; P:adult behavior; IMP:BHF-UCL.
DR   GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:BHF-UCL.
DR   GO; GO:0071277; P:cellular response to calcium ion; ISS:ARUK-UCL.
DR   GO; GO:0021707; P:cerebellar granule cell differentiation; ISS:BHF-UCL.
DR   GO; GO:0045184; P:establishment of protein localization; ISS:BHF-UCL.
DR   GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; ISS:BHF-UCL.
DR   GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; ISS:BHF-UCL.
DR   GO; GO:0097117; P:guanylate kinase-associated protein clustering; ISS:BHF-UCL.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:BHF-UCL.
DR   GO; GO:0007612; P:learning; IMP:BHF-UCL.
DR   GO; GO:0051490; P:negative regulation of filopodium assembly; ISS:BHF-UCL.
DR   GO; GO:0010629; P:negative regulation of gene expression; IDA:ARUK-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; ISS:BHF-UCL.
DR   GO; GO:0031175; P:neuron projection development; IGI:ARUK-UCL.
DR   GO; GO:0023041; P:neuronal signal transduction; TAS:BHF-UCL.
DR   GO; GO:0097114; P:NMDA glutamate receptor clustering; ISS:BHF-UCL.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:ARUK-UCL.
DR   GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
DR   GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IDA:ARUK-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:ARUK-UCL.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:ARUK-UCL.
DR   GO; GO:1905520; P:positive regulation of presynaptic active zone assembly; TAS:BHF-UCL.
DR   GO; GO:0010739; P:positive regulation of protein kinase A signaling; IDA:ARUK-UCL.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:ARUK-UCL.
DR   GO; GO:1900020; P:positive regulation of protein kinase C activity; IDA:ARUK-UCL.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:BHF-UCL.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; TAS:BHF-UCL.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; 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:0097105; P:presynaptic membrane assembly; ISS:BHF-UCL.
DR   GO; GO:0035418; P:protein localization to synapse; ISS:BHF-UCL.
DR   GO; GO:0090126; P:protein-containing complex assembly involved in synapse maturation; ISS:BHF-UCL.
DR   GO; GO:0097120; P:receptor localization to synapse; ISS:BHF-UCL.
DR   GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:BHF-UCL.
DR   GO; GO:2000310; P:regulation of NMDA receptor activity; 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:0097091; P:synaptic vesicle clustering; ISS:BHF-UCL.
DR   GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR003585; Neurexin-like.
DR   InterPro; IPR027789; Syndecan/Neurexin_dom.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   Pfam; PF01034; Syndecan; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00282; LamG; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative promoter usage; Alternative splicing;
KW   Angiogenesis; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW   Cell projection; Glycoprotein; Membrane; Metal-binding; Reference proteome;
KW   Signal; Synapse; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..50
FT                   /evidence="ECO:0000250"
FT   CHAIN           51..472
FT                   /note="Neurexin-1-beta"
FT                   /id="PRO_0000019493"
FT   TOPO_DOM        51..396
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        418..472
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          91..289
FT                   /note="Laminin G-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   REGION          205..234
FT                   /note="Essential for interaction with CBLN1; modulates
FT                   interaction affinity with NLGN1, NLGN2 and NLGN3; prevents
FT                   interaction with DAG1/alpha-dystroglycan; modulates
FT                   interaction with alpha-latrotoxin"
FT                   /evidence="ECO:0000250|UniProtKB:Q63373,
FT                   ECO:0000269|PubMed:27418511"
FT   COMPBIAS        9..29
FT                   /note="Gly-rich"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00008"
FT   COMPBIAS        300..343
FT                   /note="Thr-rich"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00017"
FT   COMPBIAS        404..407
FT                   /note="Poly-Ala"
FT   METAL           141
FT                   /note="Calcium"
FT   METAL           158
FT                   /note="Calcium; via carbonyl oxygen"
FT   METAL           240
FT                   /note="Calcium; via carbonyl oxygen"
FT   METAL           242
FT                   /note="Calcium"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         205..234
FT                   /note="Missing (in isoform 3b)"
FT                   /id="VSP_059057"
FT   CONFLICT        20
FT                   /note="G -> R (in Ref. 1; AF064842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46
FT                   /note="G -> R (in Ref. 1; AF064842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        158
FT                   /note="V -> I (in Ref. 1; AF064842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        288
FT                   /note="N -> D (in Ref. 1; AF064842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        344
FT                   /note="D -> G (in Ref. 1; AF064842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        415
FT                   /note="Y -> C (in Ref. 1; AF064842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        418..420
FT                   /note="YKY -> NKC (in Ref. 1; AF064842)"
FT                   /evidence="ECO:0000305"
FT   STRAND          91..103
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   STRAND          112..123
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   STRAND          126..135
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   STRAND          142..148
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   STRAND          151..160
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   STRAND          163..166
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   STRAND          174..176
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   STRAND          178..185
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   STRAND          188..196
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   STRAND          199..201
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   STRAND          244..250
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   TURN            252..255
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   STRAND          260..267
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   HELIX           272..276
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   TURN            277..279
FT                   /evidence="ECO:0007744|PDB:3B3Q"
FT   STRAND          283..290
FT                   /evidence="ECO:0007744|PDB:3B3Q"
SQ   SEQUENCE   472 AA;  50424 MW;  C86516C0EB7A2D01 CRC64;
     MYQRMLRCGA ELGSPGGGGG GGGGGGAGGR LALLWIVPLT LSGLLGVAWG ASSLGAHHIH
     HFHGSSKHHS VPIAIYRSPA SLRGGHAGTT YIFSKGGGQI TYKWPPNDRP STRADRLAIG
     FSTVQKEAVL VRVDSSSGLG DYLELHIHQG KIGVKFNVGT DDIAIEESNA IINDGKYHVV
     RFTRSGGNAT LQVDSWPVIE RYPAGNNDNE RLAIARQRIP YRLGRVVDEW LLDKGRQLTI
     FNSQATIIIG GKEQGQPFQG QLSGLYYNGL KVLNMAAEND ANIAIVGNVR LVGEVPSSMT
     TESTATAMQS EMSTSIMETT TTLATSTARR GKPPTKEPIS QTTDDILVAS AECPSDDEDI
     DPCEPSSGGL ANPTRAGGRE PYPGSAEVIR ESSSTTGMVV GIVAAAALCI LILLYAMYKY
     RNRDEGSYHV DESRNYISNS AQSNGAVVKE KQPSSAKSSN KNKKNKDKEY YV
//
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