NRX1B_HUMAN
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 03-AUG-2022, entry version 171.
DE RecName: Full=Neurexin-1-beta {ECO:0000305};
DE AltName: Full=Neurexin I-beta;
DE Flags: Precursor;
GN Name=NRXN1 {ECO:0000312|HGNC:HGNC:8008};
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 IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-454;
RP SER-455 AND SER-458.
RX PubMed=18423203; DOI=10.1016/j.cell.2008.02.036;
RA Mukherjee K., Sharma M., Urlaub H., Bourenkov G.P., Jahn R., Suedhof T.C.,
RA Wahl M.C.;
RT "CASK functions as a Mg2+-independent neurexin kinase.";
RL Cell 133:328-339(2008).
RN [4]
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 [5]
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 [6]
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: 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 AlphaFoldDB; P58400; -.
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; 296 antibodies from 37 providers.
DR DNASU; 9378; -.
DR Ensembl; ENST00000342183.9; ENSP00000341184.5; ENSG00000179915.25. [P58400-1]
DR Ensembl; ENST00000401710.5; ENSP00000385580.2; ENSG00000179915.25. [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; -.
DR GeneTree; ENSGT00940000154292; -.
DR PathwayCommons; P58400; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; P58400; -.
DR SIGNOR; P58400; -.
DR BioGRID-ORCS; 9378; 10 hits in 1062 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 sural nerve and 162 other tissues.
DR ExpressionAtlas; P58400; baseline and differential.
DR Genevisible; P58400; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0060076; C:excitatory synapse; IC:ComplexPortal.
DR GO; GO:0098982; C:GABA-ergic synapse; IC:ComplexPortal.
DR GO; GO:0098978; C:glutamatergic synapse; IC:ComplexPortal.
DR GO; GO:0060077; C:inhibitory synapse; IC:ComplexPortal.
DR GO; GO:0099056; C:integral component of presynaptic membrane; TAS:BHF-UCL.
DR GO; GO:0031594; C:neuromuscular junction; IC:ComplexPortal.
DR GO; GO:0098984; C:neuron to neuron synapse; IC:ComplexPortal.
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:0098635; C:protein complex involved in cell-cell adhesion; IC:ComplexPortal.
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:0090125; P:cell-cell adhesion involved in synapse maturation; IC:ComplexPortal.
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:0099558; P:maintenance of synapse structure; IC:ComplexPortal.
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:0048812; P:neuron projection morphogenesis; IC:ComplexPortal.
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:1900075; P:positive regulation of neuromuscular synaptic transmission; IC:ComplexPortal.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IC:ComplexPortal.
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:0032230; P:positive regulation of synaptic transmission, GABAergic; IC:ComplexPortal.
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:0060074; P:synapse maturation; IC:ComplexPortal.
DR GO; GO:0097091; P:synaptic vesicle clustering; ISS:BHF-UCL.
DR GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL.
DR CDD; cd00110; LamG; 1.
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 membrane; Cell projection;
KW Glycoprotein; Membrane; Metal-binding; Phosphoprotein; 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 REGION 353..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT MOD_RES 454
FT /note="Phosphoserine; by CASK"
FT /evidence="ECO:0000269|PubMed:18423203"
FT MOD_RES 455
FT /note="Phosphoserine; by CASK"
FT /evidence="ECO:0000269|PubMed:18423203"
FT MOD_RES 458
FT /note="Phosphoserine; by CASK"
FT /evidence="ECO:0000269|PubMed:18423203"
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:0007829|PDB:3B3Q"
FT STRAND 112..123
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 244..250
FT /evidence="ECO:0007829|PDB:3B3Q"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:3B3Q"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:3B3Q"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:3B3Q"
FT STRAND 283..290
FT /evidence="ECO:0007829|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
