NLGN3_MOUSE
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 03-AUG-2022, entry version 166.
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).
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.
CC {ECO:0000269|PubMed:16982420}.
CC -!- SUBUNIT: Interacts with NRXN1, NRXN2 and NRXN3. Interacts (via its C-
CC terminus) with DLG4/PSD-95 (via PDZ domain 3) (By similarity).
CC Homodimer, and heterodimer with NLGN1 and NLGN2 (By similarity).
CC {ECO:0000250}.
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 GlyGen; Q8BYM5; 2 sites.
DR iPTMnet; Q8BYM5; -.
DR PhosphoSitePlus; Q8BYM5; -.
DR MaxQB; Q8BYM5; -.
DR PaxDb; Q8BYM5; -.
DR PRIDE; Q8BYM5; -.
DR ProteomicsDB; 293575; -.
DR ABCD; Q8BYM5; 1 sequenced antibody.
DR Antibodypedia; 561; 312 antibodies from 37 providers.
DR DNASU; 245537; -.
DR Ensembl; ENSMUST00000065858; ENSMUSP00000066304; ENSMUSG00000031302.
DR GeneID; 245537; -.
DR KEGG; mmu:245537; -.
DR UCSC; uc009txj.3; mouse.
DR CTD; 54413; -.
DR MGI; MGI:2444609; Nlgn3.
DR VEuPathDB; HostDB:ENSMUSG00000031302; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000159580; -.
DR InParanoid; Q8BYM5; -.
DR OMA; MPVWFTS; -.
DR OrthoDB; 754103at2759; -.
DR TreeFam; TF326187; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 245537; 2 hits in 59 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 115 other tissues.
DR ExpressionAtlas; Q8BYM5; baseline and differential.
DR Genevisible; Q8BYM5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISS:BHF-UCL.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; 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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000460; Nlgn.
DR InterPro; IPR030024; NLGN3.
DR PANTHER; PTHR43903:SF4; PTHR43903:SF4; 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; 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 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
