ID NLGN1_MOUSE Reviewed; 843 AA. AC Q99K10; DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 23-MAY-2003, sequence version 2. DT 14-OCT-2015, entry version 128. DE RecName: Full=Neuroligin-1; DE Flags: Precursor; GN Name=Nlgn1; Synonyms=Kiaa1070; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=12693553; DOI=10.1093/dnares/10.1.35; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., RA Nakajima D., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT II. The complete nucleotide sequences of 400 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:35-48(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [3] RP FUNCTION. RX PubMed=10892652; DOI=10.1016/S0092-8674(00)80877-6; RA Scheiffele P., Fan J., Choih J., Fetter R., Serafini T.; RT "Neuroligin expressed in nonneuronal cells triggers presynaptic RT development in contacting axons."; RL Cell 101:657-669(2000). RN [4] RP TISSUE SPECIFICITY. RX PubMed=11329178; DOI=10.1002/glia.1050; RA Gilbert M., Smith J., Roskams A.J., Auld V.J.; RT "Neuroligin 3 is a vertebrate gliotactin expressed in the olfactory RT ensheathing glia, a growth-promoting class of macroglia."; RL Glia 34:151-164(2001). RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15620359; DOI=10.1016/j.cell.2004.11.035; RA Graf E.R., Zhang X., Jin S.X., Linhoff M.W., Craig A.M.; RT "Neurexins induce differentiation of GABA and glutamate postsynaptic RT specializations via neuroligins."; RL Cell 119:1013-1026(2004). RN [6] RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=16982420; DOI=10.1016/j.neuron.2006.09.003; RA Varoqueaux F., Aramuni G., Rawson R.L., Mohrmann R., Missler M., RA Gottmann K., Zhang W., Sudhof T.C., Brose N.; RT "Neuroligins determine synapse maturation and function."; RL Neuron 51:741-754(2006). RN [7] RP INTERACTION WITH NLGN3. RX PubMed=17897391; DOI=10.1111/j.1460-9568.2007.05842.x; RA Budreck E.C., Scheiffele P.; RT "Neuroligin-3 is a neuronal adhesion protein at GABAergic and RT glutamatergic synapses."; RL Eur. J. Neurosci. 26:1738-1748(2007). RN [8] RP TISSUE SPECIFICITY. RX PubMed=18434543; DOI=10.1073/pnas.0801383105; RA Bolliger M.F., Pei J., Maxeiner S., Boucard A.A., Grishin N.V., RA Sudhof T.C.; RT "Unusually rapid evolution of neuroligin-4 in mice."; RL Proc. Natl. Acad. Sci. U.S.A. 105:6421-6426(2008). RN [9] 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 [10] 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). RN [11] RP DISRUPTION PHENOTYPE. RX PubMed=20147539; DOI=10.1523/JNEUROSCI.4517-09.2010; RA Blundell J., Blaiss C.A., Etherton M.R., Espinosa F., Tabuchi K., RA Walz C., Bolliger M.F., Sudhof T.C., Powell C.M.; RT "Neuroligin-1 deletion results in impaired spatial memory and RT increased repetitive behavior."; RL J. Neurosci. 30:2115-2129(2010). RN [12] RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION. RX PubMed=23716671; DOI=10.1073/pnas.1221381110; RA El Helou J., Belanger-Nelson E., Freyburger M., Dorsaz S., Curie T., RA La Spada F., Gaudreault P.O., Beaumont E., Pouliot P., Lesage F., RA Frank M.G., Franken P., Mongrain V.; RT "Neuroligin-1 links neuronal activity to sleep-wake regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 110:9974-9979(2013). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 39-635 IN COMPLEX WITH HUMAN RP NRX1B, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-109 AND ASN-547. 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- RT neurexin interactions."; RL Nat. Struct. Mol. Biol. 15:50-56(2008). CC -!- FUNCTION: Cell surface protein involved in cell-cell-interactions CC via its interactions with neurexin family members. Plays a role in CC synapse function and synaptic signal transmission, and probably CC mediates its effects by recruiting and clustering other synaptic CC proteins. May promote the initial formation of synapses, but is CC not essential for this. In vitro, triggers the de novo formation CC of presynaptic structures. May be involved in specification of CC excitatory synapses. Required to maintain wakefulness quality and CC normal synchrony of cerebral cortex activity during wakefulness CC and sleep (PubMed:23716671). {ECO:0000269|PubMed:10892652, CC ECO:0000269|PubMed:15620359, ECO:0000269|PubMed:16982420, CC ECO:0000269|PubMed:23716671}. CC -!- SUBUNIT: Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its CC C-terminus) with DLG4/PSD-95 (via PDZ domain 3). Interacts with CC AIP1, GOPC and PDZRN3 (By similarity). Interacts with NLGN3. CC {ECO:0000250, ECO:0000269|PubMed:17897391, CC ECO:0000269|PubMed:18084303}. CC -!- INTERACTION: CC O14522:PTPRT (xeno); NbExp=2; IntAct=EBI-775037, EBI-728180; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass CC type I membrane protein {ECO:0000250}. Cell junction, synapse CC {ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane, CC postsynaptic density {ECO:0000250}. Note=Enriched in synaptic CC plasma membranes and clustered in synaptic clefts and postsynaptic CC densities. Detected at dendritic spines. Colocalized with CC DLG4/PSD-95 and GRIN1/NMDAR1 (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q99K10-1; Sequence=Displayed; CC Note=No experimental confirmation available.; CC Name=2; CC IsoId=Q99K10-2; Sequence=VSP_007528, VSP_007529, VSP_007530; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Brain and arteries (at protein level). CC Expressed in olfactory bulb. Detected in brain. CC {ECO:0000269|PubMed:11329178, ECO:0000269|PubMed:16982420, CC ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:19926856}. CC -!- INDUCTION: Expressed in a circadian manner in the brain with CC highest expression seen at Zeitgeber time (ZT) 6 hours. CC {ECO:0000269|PubMed:23716671}. CC -!- DISRUPTION PHENOTYPE: No obvious phenotype, but mice present CC subtle behavorial changes with some deficits in spatial learning CC and memory. In addition, mice have reduced brain volume. Mice CC lacking both NLGN1 and NLGN2, or NLGN1 and NLGN3, are viable, but CC have impaired breathing, drastically reduced reproduction rates CC and striking deficits in raising their offspring. Mice lacking CC NLGN1, NLGN2 and NLGN3 are born at the expected Mendelian rate, CC but die shortly after birth due to respiratory failure. They do CC not show a significant change in the number of synapses, but CC synapse function is strongly impaired. Mice exhibit social novelty CC and fear-conditioning deficits and also show reduced wakefulness CC duration and altered EEG during wakefulness and sleep. CC {ECO:0000269|PubMed:16982420, ECO:0000269|PubMed:20147539, CC ECO:0000269|PubMed:23716671}. CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC65715.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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; AK122433; BAC65715.1; ALT_INIT; mRNA. DR EMBL; BC005523; AAH05523.1; -; mRNA. DR CCDS; CCDS17268.1; -. [Q99K10-1] DR RefSeq; NP_619607.2; NM_138666.3. [Q99K10-1] DR UniGene; Mm.316080; -. DR PDB; 3B3Q; X-ray; 2.40 A; A/B=46-635. DR PDBsum; 3B3Q; -. DR ProteinModelPortal; Q99K10; -. DR SMR; Q99K10; 52-631. DR DIP; DIP-32027N; -. DR IntAct; Q99K10; 2. DR MINT; MINT-5104301; -. DR STRING; 10090.ENSMUSP00000074565; -. DR ESTHER; mouse-1neur; Neuroligin. DR MEROPS; S09.994; -. DR PhosphoSite; Q99K10; -. DR MaxQB; Q99K10; -. DR PaxDb; Q99K10; -. DR PRIDE; Q99K10; -. DR Ensembl; ENSMUST00000075054; ENSMUSP00000074565; ENSMUSG00000063887. [Q99K10-1] DR Ensembl; ENSMUST00000193603; ENSMUSP00000142200; ENSMUSG00000063887. [Q99K10-1] DR GeneID; 192167; -. DR UCSC; uc008otc.1; mouse. [Q99K10-1] DR UCSC; uc008otd.1; mouse. [Q99K10-2] DR CTD; 22871; -. DR MGI; MGI:2179435; Nlgn1. DR eggNOG; COG2272; -. DR GeneTree; ENSGT00760000118946; -. DR HOGENOM; HOG000231424; -. DR HOVERGEN; HBG008839; -. DR InParanoid; Q99K10; -. DR OMA; KFVELIV; -. DR PhylomeDB; Q99K10; -. DR TreeFam; TF326187; -. DR EvolutionaryTrace; Q99K10; -. DR NextBio; 371168; -. DR PRO; PR:Q99K10; -. DR Proteomes; UP000000589; Chromosome 3. DR Bgee; Q99K10; -. DR CleanEx; MM_NLGN1; -. DR ExpressionAtlas; Q99K10; baseline and differential. DR Genevisible; Q99K10; MM. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL. DR GO; GO:0030425; C:dendrite; ISS:BHF-UCL. DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl. DR GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL. DR GO; GO:0060076; C:excitatory synapse; IC:BHF-UCL. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0032433; C:filopodium tip; ISS:BHF-UCL. DR GO; GO:0005794; C:Golgi apparatus; ISS:BHF-UCL. DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB. DR GO; GO:0017146; C:NMDA selective glutamate receptor complex; IEA:Ensembl. DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW. DR GO; GO:0045202; C:synapse; ISS:UniProtKB. DR GO; GO:0042043; F:neurexin family protein binding; IMP:UniProtKB. DR GO; GO:0030165; F:PDZ domain binding; ISO:MGI. DR GO; GO:0046983; F:protein dimerization activity; ISS:BHF-UCL. DR GO; GO:0004872; F:receptor activity; IEA:Ensembl. DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI. DR GO; GO:0097113; P:AMPA glutamate receptor clustering; IDA:BHF-UCL. DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB. DR GO; GO:0048789; P:cytoskeletal matrix organization at active zone; IMP:BHF-UCL. DR GO; GO:0045184; P:establishment of protein localization; IMP:BHF-UCL. DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:BHF-UCL. DR GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl. DR GO; GO:0050804; P:modulation of synaptic transmission; IGI:MGI. DR GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IMP:BHF-UCL. DR GO; GO:0007399; P:nervous system development; IDA:UniProtKB. DR GO; GO:0097115; P:neurexin clustering involved in presynaptic membrane assembly; IDA:BHF-UCL. DR GO; GO:0007158; P:neuron cell-cell adhesion; IDA:BHF-UCL. DR GO; GO:0031175; P:neuron projection development; ISO:MGI. DR GO; GO:0097114; P:NMDA glutamate receptor clustering; ISS:BHF-UCL. DR GO; GO:0010841; P:positive regulation of circadian sleep/wake cycle, wakefulness; IMP:UniProtKB. DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:BHF-UCL. DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:BHF-UCL. DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:BHF-UCL. DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IEA:Ensembl. DR GO; GO:1902474; P:positive regulation of protein localization to synapse; IEA:Ensembl. DR GO; GO:1900029; P:positive regulation of ruffle assembly; IEA:Ensembl. DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:BHF-UCL. DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; ISS:BHF-UCL. DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL. DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; IDA:BHF-UCL. DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:BHF-UCL. DR GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; IMP:BHF-UCL. DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; IDA:BHF-UCL. DR GO; GO:0097104; P:postsynaptic membrane assembly; IDA:BHF-UCL. DR GO; GO:0097105; P:presynaptic membrane assembly; IDA:BHF-UCL. DR GO; GO:0051290; P:protein heterotetramerization; IEA:Ensembl. DR GO; GO:0051260; P:protein homooligomerization; IDA:BHF-UCL. DR GO; GO:0035418; P:protein localization to synapse; IDA:BHF-UCL. DR GO; GO:0006605; P:protein targeting; IEA:Ensembl. DR GO; GO:0097120; P:receptor localization to synapse; IDA:BHF-UCL. DR GO; GO:2000311; P:regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity; ISS:BHF-UCL. DR GO; GO:2000310; P:regulation of N-methyl-D-aspartate selective glutamate receptor activity; IDA:BHF-UCL. DR GO; GO:0045664; P:regulation of neuron differentiation; IDA:UniProtKB. DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IGI:MGI. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0007416; P:synapse assembly; IDA:UniProtKB. DR GO; GO:0050808; P:synapse organization; IGI:MGI. DR GO; GO:0097091; P:synaptic vesicle clustering; IDA:BHF-UCL. DR GO; GO:0016080; P:synaptic vesicle targeting; IMP:UniProtKB. DR GO; GO:0072553; P:terminal button organization; IMP:BHF-UCL. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR019819; Carboxylesterase_B_CS. DR InterPro; IPR000460; Nlgn. DR InterPro; IPR030022; NLGN1. DR PANTHER; PTHR11559:SF52; PTHR11559:SF52; 1. DR Pfam; PF00135; COesterase; 1. DR PRINTS; PR01090; NEUROLIGIN. DR SUPFAM; SSF53474; SSF53474; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Biological rhythms; Cell adhesion; KW Cell junction; Cell membrane; Complete proteome; Disulfide bond; KW Glycoprotein; Membrane; Phosphoprotein; Postsynaptic cell membrane; KW Reference proteome; Signal; Synapse; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 45 {ECO:0000255}. FT CHAIN 46 843 Neuroligin-1. FT /FTId=PRO_0000008641. FT TOPO_DOM 46 697 Extracellular. {ECO:0000255}. FT TRANSMEM 698 718 Helical. {ECO:0000255}. FT TOPO_DOM 719 843 Cytoplasmic. {ECO:0000255}. FT MOD_RES 733 733 Phosphoserine. FT {ECO:0000250|UniProtKB:Q69ZK9}. FT MOD_RES 782 782 Phosphotyrosine. FT {ECO:0000250|UniProtKB:Q8BYM5}. FT CARBOHYD 109 109 N-linked (GlcNAc...) (complex). FT {ECO:0000269|PubMed:18084303}. FT CARBOHYD 303 303 N-linked (GlcNAc...) (complex). FT {ECO:0000250}. FT CARBOHYD 343 343 N-linked (GlcNAc...) (complex). FT {ECO:0000250}. FT CARBOHYD 547 547 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:18084303}. FT CARBOHYD 683 683 O-linked (GalNAc...). {ECO:0000250}. FT CARBOHYD 686 686 O-linked (GalNAc...). {ECO:0000250}. FT DISULFID 117 153 {ECO:0000269|PubMed:18084303}. FT DISULFID 342 353 {ECO:0000269|PubMed:18084303}. FT DISULFID 512 546 {ECO:0000269|PubMed:18084303}. FT VAR_SEQ 165 184 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_007528. FT VAR_SEQ 236 269 GFLSTGDQAAKGNYGLLDLIQALRWTSENIGFFG -> EKE FT TIKETISVALQALRTKGGGFIPKQATYKRCE (in FT isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_007529. FT VAR_SEQ 270 843 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_007530. FT STRAND 54 57 {ECO:0000244|PDB:3B3Q}. FT STRAND 60 63 {ECO:0000244|PDB:3B3Q}. FT STRAND 65 67 {ECO:0000244|PDB:3B3Q}. FT STRAND 77 84 {ECO:0000244|PDB:3B3Q}. FT HELIX 91 93 {ECO:0000244|PDB:3B3Q}. FT STRAND 105 109 {ECO:0000244|PDB:3B3Q}. FT STRAND 122 124 {ECO:0000244|PDB:3B3Q}. FT TURN 128 130 {ECO:0000244|PDB:3B3Q}. FT HELIX 133 137 {ECO:0000244|PDB:3B3Q}. FT HELIX 139 145 {ECO:0000244|PDB:3B3Q}. FT STRAND 147 149 {ECO:0000244|PDB:3B3Q}. FT STRAND 155 160 {ECO:0000244|PDB:3B3Q}. FT STRAND 193 198 {ECO:0000244|PDB:3B3Q}. FT STRAND 202 206 {ECO:0000244|PDB:3B3Q}. FT HELIX 209 211 {ECO:0000244|PDB:3B3Q}. FT HELIX 215 221 {ECO:0000244|PDB:3B3Q}. FT STRAND 224 228 {ECO:0000244|PDB:3B3Q}. FT HELIX 233 237 {ECO:0000244|PDB:3B3Q}. FT STRAND 241 245 {ECO:0000244|PDB:3B3Q}. FT HELIX 249 264 {ECO:0000244|PDB:3B3Q}. FT HELIX 266 268 {ECO:0000244|PDB:3B3Q}. FT STRAND 270 280 {ECO:0000244|PDB:3B3Q}. FT HELIX 282 290 {ECO:0000244|PDB:3B3Q}. FT STRAND 310 316 {ECO:0000244|PDB:3B3Q}. FT STRAND 319 321 {ECO:0000244|PDB:3B3Q}. FT STRAND 324 327 {ECO:0000244|PDB:3B3Q}. FT HELIX 329 339 {ECO:0000244|PDB:3B3Q}. FT HELIX 347 356 {ECO:0000244|PDB:3B3Q}. FT HELIX 359 363 {ECO:0000244|PDB:3B3Q}. FT STRAND 375 377 {ECO:0000244|PDB:3B3Q}. FT STRAND 382 385 {ECO:0000244|PDB:3B3Q}. FT HELIX 389 395 {ECO:0000244|PDB:3B3Q}. FT STRAND 402 408 {ECO:0000244|PDB:3B3Q}. FT TURN 409 412 {ECO:0000244|PDB:3B3Q}. FT HELIX 413 416 {ECO:0000244|PDB:3B3Q}. FT HELIX 417 419 {ECO:0000244|PDB:3B3Q}. FT STRAND 422 424 {ECO:0000244|PDB:3B3Q}. FT HELIX 428 443 {ECO:0000244|PDB:3B3Q}. FT HELIX 451 459 {ECO:0000244|PDB:3B3Q}. FT HELIX 469 484 {ECO:0000244|PDB:3B3Q}. FT HELIX 486 498 {ECO:0000244|PDB:3B3Q}. FT STRAND 503 508 {ECO:0000244|PDB:3B3Q}. FT TURN 525 528 {ECO:0000244|PDB:3B3Q}. FT HELIX 529 532 {ECO:0000244|PDB:3B3Q}. FT TURN 536 538 {ECO:0000244|PDB:3B3Q}. FT STRAND 542 544 {ECO:0000244|PDB:3B3Q}. FT HELIX 550 569 {ECO:0000244|PDB:3B3Q}. FT STRAND 572 576 {ECO:0000244|PDB:3B3Q}. FT TURN 600 602 {ECO:0000244|PDB:3B3Q}. FT STRAND 604 611 {ECO:0000244|PDB:3B3Q}. FT STRAND 613 617 {ECO:0000244|PDB:3B3Q}. FT HELIX 620 627 {ECO:0000244|PDB:3B3Q}. FT HELIX 630 633 {ECO:0000244|PDB:3B3Q}. SQ SEQUENCE 843 AA; 94149 MW; 69E50709CF7D2E1F CRC64; MALPRCMWPN YVWRAMMACV VHRGSGAPLT LCLLGCLLQT FHVLSQKLDD VDPLVTTNFG KIRGIKKELN NEILGPVIQF LGVPYAAPPT GEHRFQPPEP PSPWSDIRNA TQFAPVCPQN IIDGRLPEVM LPVWFTNNLD VVSSYVQDQS EDCLYLNIYV PTEDGPLTKK HTDDLGDNDG AEDEDIRDSG GPKPVMVYIH GGSYMEGTGN LYDGSVLASY GNVIVITVNY RLGVLGFLST GDQAAKGNYG LLDLIQALRW TSENIGFFGG DPLRITVFGS GAGGSCVNLL TLSHYSEGNR WSNSTKGLFQ RAIAQSGTAL SSWAVSFQPA KYARILATKV GCNVSDTVEL VECLQKKPYK ELVDQDVQPA RYHIAFGPVI DGDVIPDDPQ ILMEQGEFLN YDIMLGVNQG EGLKFVENIV DSDDGVSASD FDFAVSNFVD NLYGYPEGKD VLRETIKFMY TDWADRHNPE TRRKTLLALF TDHQWVAPAV ATADLHSNFG SPTYFYAFYH HCQTDQVPAW ADAAHGDEVP YVLGIPMIGP TELFPCNFSK NDVMLSAVVM TYWTNFAKTG DPNQPVPQDT KFIHTKPNRF EEVAWTRYSQ KDQLYLHIGL KPRVKEHYRA NKVNLWLELV PHLHNLNDIS QYTSTTTKVP STDITLRPTR KNSTPVTSAF PTAKQDDPKQ QPSPFSVDQR DYSTELSVTI AVGASLLFLN ILAFAALYYK KDKRRHDVHR RCSPQRTTTN DLTHAPEEEI MSLQMKHTDL DHECESIHPH EVVLRTACPP DYTLAMRRSP DDIPLMTPNT ITMIPNTIPG IQPLHTFNTF TGGQNNTLPH PHPHPHSHST TRV //