ID   NLGN3_MOUSE             Reviewed;         825 AA.
AC   Q8BYM5; A2AGI1; Q8BXR4;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 174.
DE   RecName: Full=Neuroligin-3;
DE   AltName: Full=Gliotactin homolog;
DE   Flags: Precursor;
GN   Name=Nlgn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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   [4]
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   [5]
RP   INTERACTION WITH NLGN1 AND NLGN2, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
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 glutamatergic
RT   synapses.";
RL   Eur. J. Neurosci. 26:1738-1748(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-769, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
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   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19243448; DOI=10.1111/j.1601-183x.2009.00487.x;
RA   Radyushkin K., Hammerschmidt K., Boretius S., Varoqueaux F., El-Kordi A.,
RA   Ronnenberg A., Winter D., Frahm J., Fischer J., Brose N., Ehrenreich H.;
RT   "Neuroligin-3-deficient mice: model of a monogenic heritable form of autism
RT   with an olfactory deficit.";
RL   Genes Brain Behav. 8:416-425(2009).
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=19926856; DOI=10.1073/pnas.0809510106;
RA   Bottos A., Destro E., Rissone A., Graziano S., Cordara G., Assenzio B.,
RA   Cera M.R., Mascia L., Bussolino F., Arese M.;
RT   "The synaptic proteins neurexins and neuroligins are widely expressed in
RT   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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [11]
RP   FUNCTION, INTERACTION WITH NEUREXINS, AND MUTAGENESIS OF 586-LYS--ARG-590.
RX   PubMed=30100184; DOI=10.1016/j.cell.2018.07.002;
RA   Zhang P., Lu H., Peixoto R.T., Pines M.K., Ge Y., Oku S., Siddiqui T.J.,
RA   Xie Y., Wu W., Archer-Hartmann S., Yoshida K., Tanaka K.F., Aricescu A.R.,
RA   Azadi P., Gordon M.D., Sabatini B.L., Wong R.O.L., Craig A.M.;
RT   "Heparan Sulfate Organizes Neuronal Synapses through Neurexin
RT   Partnerships.";
RL   Cell 174:1450-1464(2018).
CC   -!- FUNCTION: Cell surface protein involved in cell-cell-interactions via
CC       its interactions with neurexin family members. Plays a role in synapse
CC       function and synaptic signal transmission, and probably mediates its
CC       effects by recruiting and clustering other synaptic proteins. May
CC       promote the initial formation of synapses, but is not essential for
CC       this. May also play a role in glia-glia or glia-neuron interactions in
CC       the developing peripheral nervous system. {ECO:0000269|PubMed:16982420,
CC       ECO:0000269|PubMed:30100184}.
CC   -!- SUBUNIT: Homodimer, and heterodimer with NLGN1 and NLGN2 (By
CC       similarity). Interacts with neurexins NRXN1, NRXN2 and NRXN3 (By
CC       similarity). Interaction with neurexins is mediated by heparan sulfate
CC       glycan modification on neurexin (PubMed:30100184). Interacts (via its
CC       C-terminus) with DLG4/PSD-95 (via PDZ domain 3) (By similarity).
CC       {ECO:0000250|UniProtKB:Q62889, ECO:0000269|PubMed:30100184}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17897391};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:17897391}.
CC       Synapse {ECO:0000269|PubMed:17897391}. Note=Detected at both
CC       glutamatergic and GABAergic synapses.
CC   -!- TISSUE SPECIFICITY: Brain and arteries (at protein level). Detected in
CC       heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis.
CC       Expressed in olfactory bulb and olfactory epithelium. Found in
CC       olfactory ensheathing glia but not in olfactory neurons, and in
CC       developing peripheral glia. {ECO:0000269|PubMed:11329178,
CC       ECO:0000269|PubMed:16982420, ECO:0000269|PubMed:17897391,
CC       ECO:0000269|PubMed:18434543, ECO:0000269|PubMed:19926856}.
CC   -!- DEVELOPMENTAL STAGE: Detected at embryonic day 17 dpc and postnatal day
CC       P1 in retinal astrocytes, spinal cord astrocytes and Schwann cells of
CC       the dorsal root ganglion. {ECO:0000269|PubMed:11329178}.
CC   -!- DISRUPTION PHENOTYPE: No obvious phenotype, but mice present subtle
CC       behavorial changes with reduced ultrasound vocalization and impaired
CC       response to olfactory cues. In addition, mice have reduced brain
CC       volume. Mice lacking both NLGN1 and NLGN3, or NLGN2 and NLGN3, are
CC       viable, but have impaired breathing, drastically reduced reproduction
CC       rates and striking deficits in raising their offspring. Mice lacking
CC       NLGN1, NLGN2 and NLGN3 are born at the expected Mendelian rate, but die
CC       shortly after birth due to respiratory failure. They do not show a
CC       significant change in the number of synapses, but synapse function is
CC       strongly impaired. {ECO:0000269|PubMed:16982420,
CC       ECO:0000269|PubMed:19243448}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AK039018; BAC30207.1; -; mRNA.
DR   EMBL; AK044438; BAC31918.1; -; mRNA.
DR   EMBL; AL683892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS30313.1; -.
DR   RefSeq; NP_766520.2; NM_172932.4.
DR   PDB; 7CEE; X-ray; 2.76 A; A/B=36-684.
DR   PDB; 7CEG; X-ray; 3.85 A; B=37-615.
DR   PDBsum; 7CEE; -.
DR   PDBsum; 7CEG; -.
DR   AlphaFoldDB; Q8BYM5; -.
DR   SMR; Q8BYM5; -.
DR   BioGRID; 232793; 7.
DR   IntAct; Q8BYM5; 3.
DR   MINT; Q8BYM5; -.
DR   STRING; 10090.ENSMUSP00000066304; -.
DR   ESTHER; mouse-3neur; Neuroligin.
DR   MEROPS; S09.987; -.
DR   GlyCosmos; Q8BYM5; 2 sites, No reported glycans.
DR   GlyGen; Q8BYM5; 3 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BYM5; -.
DR   PhosphoSitePlus; Q8BYM5; -.
DR   SwissPalm; Q8BYM5; -.
DR   MaxQB; Q8BYM5; -.
DR   PaxDb; 10090-ENSMUSP00000066304; -.
DR   ProteomicsDB; 293575; -.
DR   ABCD; Q8BYM5; 1 sequenced antibody.
DR   Antibodypedia; 561; 345 antibodies from 37 providers.
DR   DNASU; 245537; -.
DR   Ensembl; ENSMUST00000065858.3; ENSMUSP00000066304.3; ENSMUSG00000031302.17.
DR   GeneID; 245537; -.
DR   KEGG; mmu:245537; -.
DR   UCSC; uc009txj.3; mouse.
DR   AGR; MGI:2444609; -.
DR   CTD; 54413; -.
DR   MGI; MGI:2444609; Nlgn3.
DR   VEuPathDB; HostDB:ENSMUSG00000031302; -.
DR   eggNOG; KOG1516; Eukaryota.
DR   GeneTree; ENSGT00940000159580; -.
DR   InParanoid; Q8BYM5; -.
DR   OMA; QCGHEGA; -.
DR   OrthoDB; 4386at2759; -.
DR   TreeFam; TF326187; -.
DR   Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR   BioGRID-ORCS; 245537; 2 hits in 62 CRISPR screens.
DR   PRO; PR:Q8BYM5; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q8BYM5; Protein.
DR   Bgee; ENSMUSG00000031302; Expressed in dentate gyrus of hippocampal formation granule cell and 116 other cell types or tissues.
DR   ExpressionAtlas; Q8BYM5; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR   GO; GO:0030139; C:endocytic vesicle; ISS:BHF-UCL.
DR   GO; GO:0060076; C:excitatory synapse; ISS:BHF-UCL.
DR   GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0060077; C:inhibitory synapse; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISS:BHF-UCL.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; ISO:MGI.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0045202; C:synapse; ISO:MGI.
DR   GO; GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL.
DR   GO; GO:0042043; F:neurexin family protein binding; ISS:BHF-UCL.
DR   GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR   GO; GO:0038023; F:signaling receptor activity; ISO:MGI.
DR   GO; GO:0030534; P:adult behavior; ISO:MGI.
DR   GO; GO:0048675; P:axon extension; ISS:BHF-UCL.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0042745; P:circadian sleep/wake cycle; ISO:MGI.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; IMP:BHF-UCL.
DR   GO; GO:0060080; P:inhibitory postsynaptic potential; IMP:BHF-UCL.
DR   GO; GO:0007612; P:learning; ISO:MGI.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IMP:CACAO.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IGI:MGI.
DR   GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; IMP:CACAO.
DR   GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IMP:CACAO.
DR   GO; GO:0007158; P:neuron cell-cell adhesion; ISS:BHF-UCL.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
DR   GO; GO:2000969; P:positive regulation of AMPA receptor activity; IMP:BHF-UCL.
DR   GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
DR   GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:BHF-UCL.
DR   GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; ISO:MGI.
DR   GO; GO:1902474; P:positive regulation of protein localization to synapse; ISO:MGI.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IMP:CACAO.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:BHF-UCL.
DR   GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; IMP:CACAO.
DR   GO; GO:0097104; P:postsynaptic membrane assembly; IMP:BHF-UCL.
DR   GO; GO:0098698; P:postsynaptic specialization assembly; ISO:MGI.
DR   GO; GO:0060134; P:prepulse inhibition; ISO:MGI.
DR   GO; GO:0097105; P:presynaptic membrane assembly; ISS:BHF-UCL.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISS:BHF-UCL.
DR   GO; GO:2000311; P:regulation of AMPA receptor activity; IMP:BHF-UCL.
DR   GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:BHF-UCL.
DR   GO; GO:1900271; P:regulation of long-term synaptic potentiation; IMP:BHF-UCL.
DR   GO; GO:2000310; P:regulation of NMDA receptor activity; IMP:BHF-UCL.
DR   GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IGI:MGI.
DR   GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:BHF-UCL.
DR   GO; GO:2000331; P:regulation of terminal button organization; IMP:BHF-UCL.
DR   GO; GO:0060024; P:rhythmic synaptic transmission; ISS:BHF-UCL.
DR   GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
DR   GO; GO:0007416; P:synapse assembly; ISO:MGI.
DR   GO; GO:0050808; P:synapse organization; IGI:MGI.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   GO; GO:0071625; P:vocalization behavior; ISO:MGI.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR000460; Nlgn.
DR   PANTHER; PTHR43903; NEUROLIGIN; 1.
DR   PANTHER; PTHR43903:SF4; NEUROLIGIN-3; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR01090; NEUROLIGIN.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
DR   Genevisible; Q8BYM5; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW   Membrane; Phosphoprotein; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..825
FT                   /note="Neuroligin-3"
FT                   /id="PRO_0000008646"
FT   TOPO_DOM        35..686
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        687..707
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        708..825
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          151..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..664
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         722
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62889"
FT   MOD_RES         769
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        103..138
FT                   /evidence="ECO:0000250"
FT   DISULFID        317..328
FT                   /evidence="ECO:0000250"
FT   DISULFID        487..521
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         586..590
FT                   /note="KPRVR->APAVA: Reduced presynaptic differentiation."
FT                   /evidence="ECO:0000269|PubMed:30100184"
FT   CONFLICT        64
FT                   /note="D -> E (in Ref. 1; BAC30207)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        459
FT                   /note="Q -> K (in Ref. 1; BAC31918)"
FT                   /evidence="ECO:0000305"
FT   STRAND          40..43
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          46..49
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          91..95
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   TURN            113..115
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           118..121
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           124..131
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          140..146
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          176..183
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          186..190
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           193..195
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           199..205
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          208..212
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           217..221
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          225..228
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           233..248
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           249..252
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          254..264
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           266..275
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   TURN            279..283
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          285..291
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   TURN            297..299
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           304..314
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           322..331
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           334..339
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          350..352
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          357..360
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           364..370
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           372..375
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          376..383
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   TURN            384..387
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           388..390
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           392..394
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           403..418
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           424..434
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          440..442
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           444..459
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           461..471
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          478..483
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          490..492
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   TURN            500..503
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           504..507
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           510..512
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           525..544
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          549..551
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   TURN            575..577
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          579..586
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   STRAND          588..592
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           595..602
FT                   /evidence="ECO:0007829|PDB:7CEE"
FT   HELIX           604..608
FT                   /evidence="ECO:0007829|PDB:7CEE"
SQ   SEQUENCE   825 AA;  91162 MW;  CEF160C63E0A71A4 CRC64;
     MWLQPSLSLS PTPTVGRSLC LTLGFLSLVL RASTQAPAPT VNTHFGKLRG ARVPLPSEIL
     GPVDQYLGVP YAAPPIGEKR FLPPEPPPSW SGIRNATHFP PVCPQNIHTA VPEVMLPVWF
     TANLDIVATY IQEPNEDCLY LNVYVPTEDG SGAKKQGEDL ADNDGDEDED IRDSGAKPVM
     VYIHGGSYME GTGNMIDGSV LASYGNVIVI TLNYRVGVLG FLSTGDQAAK GNYGLLDQIQ
     ALRWVSENIA FFGGDPRRIT VFGSGIGASC VSLLTLSHHS EGLFQRAIIQ SGSALSSWAV
     NYQPVKYTSL LADKVGCNVL DTVDMVDCLR QKSAKELVEQ DIQPARYHVA FGPVIDGDVI
     PDDPEILMEQ GEFLNYDIML GVNQGEGLKF VEGVVDPEDG VSGTDFDYSV SNFVDNLYGY
     PEGKDTLRET IKFMYTDWAD RDNPETRRKT LVALFTDHQW VEPSVVTADL HARYGSPTYF
     YAFYHHCQSL MKPAWSDAAH GDEVPYVFGV PMVGPTDLFP CNFSKNDVML SAVVMTYWTN
     FAKTGDPNKP VPQDTKFIHT KANRFEEVAW SKYNPRDQLY LHIGLKPRVR DHYRATKVAF
     WKHLVPHLYN LHDMFHYTST TTKVPPPDTT HSSHITRRPN GKTWSTKRPA ISPAYSNENA
     PGSWNGDQDA GPLLVENPRD YSTELSVTIA VGASLLFLNV LAFAALYYRK DKRRQEPLRQ
     PSPQRGTGAP ELGTAPEEEL AALQLGPTHH ECEAGPPHDT LRLTALPDYT LTLRRSPDDI
     PLMTPNTITM IPNSLVGLQT LHPYNTFAAG FNSTGLPHSH STTRV
//