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 27-MAR-2024, entry version 180. 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 NLGN1, 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 involved in cell recognition CC and cell adhesion by forming intracellular junctions through binding to CC neuroligins. Plays a role in formation of synaptic junctions. CC {ECO:0000250|UniProtKB:P0DI97, ECO:0000250|UniProtKB:Q63373}. 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). Interacts with CLSTN3 (By similarity). CC {ECO:0000250|UniProtKB:P0DI97, ECO:0000250|UniProtKB:Q63373, CC 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: O-glycosylated; contains heparan sulfate. Heparan sulfate CC attachment is required for synapse development by mediating CC interactions with neuroligins. {ECO:0000250|UniProtKB:P0DI97}. CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AF064842; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 17. 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 GlyCosmos; P58400; 1 site, No reported glycans. DR iPTMnet; P58400; -. DR BioMuta; NRXN1; -. DR DMDM; 322510054; -. DR MassIVE; P58400; -. DR PeptideAtlas; P58400; -. DR ProteomicsDB; 18162; -. DR ProteomicsDB; 57071; -. [P58400-1] DR ABCD; P58400; 2 sequenced antibodies. DR Antibodypedia; 30173; 334 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 AGR; HGNC:8008; -. 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 OrthoDB; 2999458at2759; -. DR PathwayCommons; P58400; -. DR Reactome; R-HSA-6794361; Neurexins and neuroligins. DR SignaLink; P58400; -. DR SIGNOR; P58400; -. DR BioGRID-ORCS; 9378; 10 hits in 1138 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 164 other cell types or tissues. DR ExpressionAtlas; P58400; baseline and differential. 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; NAS:ComplexPortal. DR GO; GO:0098982; C:GABA-ergic synapse; NAS:ComplexPortal. DR GO; GO:0098978; C:glutamatergic synapse; NAS:ComplexPortal. DR GO; GO:0060077; C:inhibitory synapse; NAS:ComplexPortal. DR GO; GO:0031594; C:neuromuscular junction; NAS:ComplexPortal. DR GO; GO:0098984; C:neuron to neuron synapse; NAS: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; EXP: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; NAS: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; NAS: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; NAS: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; NAS:ComplexPortal. DR GO; GO:0010976; P:positive regulation of neuron projection development; NAS:ComplexPortal. DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:ARUK-UCL. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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: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; NAS: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; NAS: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 Gene3D; 2.60.120.200; -; 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 PANTHER; PTHR15036:SF51; NEUREXIN-1; 1. DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1. 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; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS50025; LAM_G_DOMAIN; 1. DR Genevisible; P58400; HS. 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; Heparan sulfate; Membrane; Metal-binding; Phosphoprotein; KW Proteoglycan; Reference proteome; Repeat; Signal; Synapse; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..50 FT /evidence="ECO:0000250|UniProtKB:Q63373" 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 /evidence="ECO:0000269|PubMed:18084303" FT BINDING 158 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:18084303" FT BINDING 240 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:18084303" FT BINDING 242 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000269|PubMed:18084303" 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 CARBOHYD 350 FT /note="O-linked (Xyl...) (heparan sulfate) serine" FT /evidence="ECO:0000250|UniProtKB:P0DI97" 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 //