NLGN2_HUMAN
ID NLGN2_HUMAN Reviewed; 835 AA.
AC Q8NFZ4; Q9P2I1;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Neuroligin-2;
DE Flags: Precursor;
GN Name=NLGN2; Synonyms=KIAA1366;
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].
RX PubMed=12669065; DOI=10.1038/ng1136;
RA Jamain S., Quach H., Betancur C., Rastam M., Colineaux C., Gillberg I.C.,
RA Soderstrom H., Giros B., Leboyer M., Gillberg C., Bourgeron T., Nyden A.,
RA Philippe A., Cohen D., Chabane N., Mouren-Simeoni M.C., Brice A.,
RA Sponheim E., Spurkland I., Skjeldal O.H., Coleman M., Pearl P.L.,
RA Cohen I.L., Tsiouris J., Zappella M., Menchetti G., Pompella A.,
RA Aschauer H., Van Maldergem L.;
RT "Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are
RT associated with autism.";
RL Nat. Genet. 34:27-29(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-835.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP INTERACTION WITH DLG4.
RX PubMed=9278515; DOI=10.1126/science.277.5331.1511;
RA Irie M., Hata Y., Takeuchi M., Ichtchenko K., Toyoda A., Hirao K.,
RA Takai Y., Rosahl T.W., Suedhof T.C.;
RT "Binding of neuroligins to PSD-95.";
RL Science 277:1511-1515(1997).
RN [4]
RP TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=18755801; DOI=10.1210/en.2008-0274;
RA Suckow A.T., Comoletti D., Waldrop M.A., Mosedale M., Egodage S.,
RA Taylor P., Chessler S.D.;
RT "Expression of neurexin, neuroligin, and their cytoplasmic binding partners
RT in the pancreatic beta-cells and the involvement of neuroligin in insulin
RT secretion.";
RL Endocrinology 149:6006-6017(2008).
RN [5]
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 [6]
RP IDENTIFICATION IN A COMPLEX WITH MAGI2 AND IGSF9B.
RX PubMed=23751499; DOI=10.1083/jcb.201209132;
RA Woo J., Kwon S.K., Nam J., Choi S., Takahashi H., Krueger D., Park J.,
RA Lee Y., Bae J.Y., Lee D., Ko J., Kim H., Kim M.H., Bae Y.C., Chang S.,
RA Craig A.M., Kim E.;
RT "The adhesion protein IgSF9b is coupled to neuroligin 2 via S-SCAM to
RT promote inhibitory synapse development.";
RL J. Cell Biol. 201:929-944(2013).
CC -!- FUNCTION: Transmembrane scaffolding protein involved in cell-cell
CC interactions via its interactions with neurexin family members.
CC Mediates cell-cell interactions both in neurons and in other types of
CC cells, such as Langerhans beta cells. Plays a role in synapse function
CC and synaptic signal transmission, especially via gamma-aminobutyric
CC acid receptors (GABA(A) receptors). Functions by recruiting and
CC clustering synaptic proteins. Promotes clustering of postsynaptic
CC GABRG2 and GPHN. Promotes clustering of postsynaptic LHFPL4 (By
CC similarity). Modulates signaling by inhibitory synapses, and thereby
CC plays a role in controlling the ratio of signaling by excitatory and
CC inhibitory synapses and information processing. Required for normal
CC signal amplitude from inhibitory synapses, but is not essential for
CC normal signal frequency. May promote the initial formation of synapses,
CC but is not essential for this. In vitro, triggers the de novo formation
CC of presynaptic structures. Mediates cell-cell interactions between
CC Langerhans beta cells and modulates insulin secretion (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q69ZK9}.
CC -!- SUBUNIT: Interacts with NRXN1, NRXN2 and NRXN3 (By similarity).
CC Interacts (via its C-terminus) with DLG4/PSD-95 (via PDZ domain 3)
CC (PubMed:9278515). Interacts with PATJ (By similarity). Interacts with
CC GPHN (By similarity). Interacts with MDGA1 and MDGA2 (By similarity).
CC Found in a complex with MAGI2 and IGSF9B, where it interacts with MAGI2
CC (via WW 1, WW 2 and PDZ 2 domains) (PubMed:23751499). Identified in a
CC complex of 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2
CC and GABRB3 (By similarity). Interacts with LHFPL4; leading to mutual
CC regulation of the protein level and synaptic clustering (By
CC similarity). Interacts with NLGN2 (By similarity).
CC {ECO:0000250|UniProtKB:Q62888, ECO:0000250|UniProtKB:Q69ZK9,
CC ECO:0000269|PubMed:23751499, ECO:0000269|PubMed:9278515}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Postsynaptic cell membrane
CC {ECO:0000250}. Presynaptic cell membrane {ECO:0000250}. Note=Detected
CC at postsynaptic membranes in brain. Detected at dendritic spines in
CC cultured neurons. Colocalizes with GPHN and ARHGEF9 at neuronal cell
CC membranes (By similarity). Localized at presynaptic membranes in
CC retina. Colocalizes with GABRG2 at inhibitory synapses in the retina
CC (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the blood vessel walls. Detected in
CC colon, brain and pancreas islets of Langerhans (at protein level).
CC Detected in brain, and at lower levels in pancreas islet beta cells.
CC {ECO:0000269|PubMed:18755801, ECO:0000269|PubMed:19926856}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; AF376802; AAM46111.1; -; mRNA.
DR EMBL; AB037787; BAA92604.1; -; mRNA.
DR CCDS; CCDS11103.1; -.
DR RefSeq; NP_065846.1; NM_020795.3.
DR PDB; 5XEQ; X-ray; 3.14 A; A=42-611.
DR PDBsum; 5XEQ; -.
DR AlphaFoldDB; Q8NFZ4; -.
DR SMR; Q8NFZ4; -.
DR BioGRID; 121611; 107.
DR IntAct; Q8NFZ4; 10.
DR STRING; 9606.ENSP00000305288; -.
DR ESTHER; human-NLGN2; Neuroligin.
DR MEROPS; S09.995; -.
DR TCDB; 8.A.117.1.1; the neuroligin (nlg) family.
DR GlyGen; Q8NFZ4; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NFZ4; -.
DR PhosphoSitePlus; Q8NFZ4; -.
DR BioMuta; NLGN2; -.
DR DMDM; 31076824; -.
DR jPOST; Q8NFZ4; -.
DR MassIVE; Q8NFZ4; -.
DR PaxDb; Q8NFZ4; -.
DR PeptideAtlas; Q8NFZ4; -.
DR PRIDE; Q8NFZ4; -.
DR ProteomicsDB; 73397; -.
DR ABCD; Q8NFZ4; 1 sequenced antibody.
DR Antibodypedia; 24107; 116 antibodies from 32 providers.
DR DNASU; 57555; -.
DR Ensembl; ENST00000302926.7; ENSP00000305288.2; ENSG00000169992.10.
DR Ensembl; ENST00000575301.5; ENSP00000461168.1; ENSG00000169992.10.
DR Ensembl; ENST00000639647.1; ENSP00000492323.1; ENSG00000283859.2.
DR Ensembl; ENST00000640620.2; ENSP00000492198.1; ENSG00000283859.2.
DR GeneID; 57555; -.
DR KEGG; hsa:57555; -.
DR MANE-Select; ENST00000302926.7; ENSP00000305288.2; NM_020795.4; NP_065846.1.
DR UCSC; uc002ggt.3; human.
DR CTD; 57555; -.
DR DisGeNET; 57555; -.
DR GeneCards; NLGN2; -.
DR HGNC; HGNC:14290; NLGN2.
DR HPA; ENSG00000169992; Low tissue specificity.
DR MIM; 606479; gene.
DR neXtProt; NX_Q8NFZ4; -.
DR OpenTargets; ENSG00000169992; -.
DR PharmGKB; PA31648; -.
DR VEuPathDB; HostDB:ENSG00000169992; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000160598; -.
DR HOGENOM; CLU_006586_5_1_1; -.
DR InParanoid; Q8NFZ4; -.
DR OMA; APPGIMK; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q8NFZ4; -.
DR TreeFam; TF326187; -.
DR PathwayCommons; Q8NFZ4; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; Q8NFZ4; -.
DR SIGNOR; Q8NFZ4; -.
DR BioGRID-ORCS; 57555; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; NLGN2; human.
DR GeneWiki; NLGN2; -.
DR GenomeRNAi; 57555; -.
DR Pharos; Q8NFZ4; Tbio.
DR PRO; PR:Q8NFZ4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8NFZ4; protein.
DR Bgee; ENSG00000169992; Expressed in cortical plate and 95 other tissues.
DR ExpressionAtlas; Q8NFZ4; baseline and differential.
DR Genevisible; Q8NFZ4; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
DR GO; GO:0098691; C:dopaminergic synapse; IEA:Ensembl.
DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
DR GO; GO:0098690; C:glycinergic synapse; IEA:Ensembl.
DR GO; GO:0060077; C:inhibitory synapse; ISS:BHF-UCL.
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; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045211; C:postsynaptic membrane; NAS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097470; C:ribbon synapse; IEA:Ensembl.
DR GO; GO:0089717; C:spanning component of membrane; TAS:ARUK-UCL.
DR GO; GO:0098983; C:symmetric, GABA-ergic, inhibitory synapse; TAS:ARUK-UCL.
DR GO; GO:0045202; C:synapse; ISS:BHF-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0042043; F:neurexin family protein binding; ISS:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB.
DR GO; GO:0045217; P:cell-cell junction maintenance; NAS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; ISS:BHF-UCL.
DR GO; GO:1904862; P:inhibitory synapse assembly; IEA:Ensembl.
DR GO; GO:1901142; P:insulin metabolic process; IEA:Ensembl.
DR GO; GO:0007630; P:jump response; IEA:Ensembl.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:BHF-UCL.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0007158; P:neuron cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:0072578; P:neurotransmitter-gated ion channel clustering; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; ISS:BHF-UCL.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:CACAO.
DR GO; GO:1902474; P:positive regulation of protein localization to synapse; IDA:MGI.
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; IEA:Ensembl.
DR GO; GO:1904034; P:positive regulation of t-SNARE clustering; IEA:Ensembl.
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:0099054; P:presynapse assembly; TAS:ARUK-UCL.
DR GO; GO:0097105; P:presynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0035418; P:protein localization to synapse; ISS:BHF-UCL.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:BHF-UCL.
DR GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; ISS:BHF-UCL.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL.
DR GO; GO:0050808; P:synapse organization; ISS:BHF-UCL.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IEA:Ensembl.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:0072553; P:terminal button organization; ISS:BHF-UCL.
DR GO; GO:0001966; P:thigmotaxis; IEA:Ensembl.
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; IPR030023; NLGN2.
DR PANTHER; PTHR43903:SF3; PTHR43903:SF3; 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; Cell projection;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..835
FT /note="Neuroligin-2"
FT /id="PRO_0000008643"
FT TOPO_DOM 15..677
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 699..835
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 623..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..698
FT /note="Required for interaction with LHFPL4"
FT /evidence="ECO:0000250|UniProtKB:Q69ZK9"
FT REGION 790..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..656
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..822
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZK9"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZK9"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
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 106..141
FT /evidence="ECO:0000250"
FT DISULFID 317..328
FT /evidence="ECO:0000250"
FT DISULFID 487..521
FT /evidence="ECO:0000250"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:5XEQ"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5XEQ"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 127..131
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 233..246
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:5XEQ"
FT TURN 279..283
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:5XEQ"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 322..329
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 334..338
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 377..383
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 403..417
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 424..434
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 444..459
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 461..473
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:5XEQ"
FT TURN 500..503
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 525..544
FT /evidence="ECO:0007829|PDB:5XEQ"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 580..586
FT /evidence="ECO:0007829|PDB:5XEQ"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:5XEQ"
FT HELIX 595..603
FT /evidence="ECO:0007829|PDB:5XEQ"
FT TURN 604..607
FT /evidence="ECO:0007829|PDB:5XEQ"
SQ SEQUENCE 835 AA; 90820 MW; 359938630193EF87 CRC64;
MWLLALCLVG LAGAQRGGGG PGGGAPGGPG LGLGSLGEER FPVVNTAYGR VRGVRRELNN
EILGPVVQFL GVPYATPPLG ARRFQPPEAP ASWPGVRNAT TLPPACPQNL HGALPAIMLP
VWFTDNLEAA ATYVQNQSED CLYLNLYVPT EDGPLTKKRD EATLNPPDTD IRDPGKKPVM
LFLHGGSYME GTGNMFDGSV LAAYGNVIVA TLNYRLGVLG FLSTGDQAAK GNYGLLDQIQ
ALRWLSENIA HFGGDPERIT IFGSGAGASC VNLLILSHHS EGLFQKAIAQ SGTAISSWSV
NYQPLKYTRL LAAKVGCDRE DSAEAVECLR RKPSRELVDQ DVQPARYHIA FGPVVDGDVV
PDDPEILMQQ GEFLNYDMLI GVNQGEGLKF VEDSAESEDG VSASAFDFTV SNFVDNLYGY
PEGKDVLRET IKFMYTDWAD RDNGEMRRKT LLALFTDHQW VAPAVATAKL HADYQSPVYF
YTFYHHCQAE GRPEWADAAH GDELPYVFGV PMVGATDLFP CNFSKNDVML SAVVMTYWTN
FAKTGDPNQP VPQDTKFIHT KPNRFEEVVW SKFNSKEKQY LHIGLKPRVR DNYRANKVAF
WLELVPHLHN LHTELFTTTT RLPPYATRWP PRPPAGAPGT RRPPPPATLP PEPEPEPGPR
AYDRFPGDSR DYSTELSVTV AVGASLLFLN ILAFAALYYK RDRRQELRCR RLSPPGGSGS
GVPGGGPLLP AAGRELPPEE ELVSLQLKRG GGVGADPAEA LRPACPPDYT LALRRAPDDV
PLLAPGALTL LPSGLGPPPP PPPPSLHPFG PFPPPPPTAT SHNNTLPHPH STTRV
