NLGNX_HUMAN
ID NLGNX_HUMAN Reviewed; 816 AA.
AC Q8N0W4; Q6UX10; Q9ULG0;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Neuroligin-4, X-linked;
DE Short=Neuroligin X;
DE AltName: Full=HNLX;
DE Flags: Precursor;
GN Name=NLGN4X; Synonyms=KIAA1260, NLGN4; ORFNames=UNQ365/PRO701;
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 1), AND DISEASE.
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-816 (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP PROTEIN SEQUENCE OF 42-56.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [6]
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 [7]
RP INTERACTION WITH DLG4, AND TISSUE SPECIFICITY.
RX PubMed=11368788; DOI=10.1042/0264-6021:3560581;
RA Bolliger M.F., Frei K., Winterhalter K.H., Gloor S.M.;
RT "Identification of a novel neuroligin in humans which binds to PSD-95 and
RT has a widespread expression.";
RL Biochem. J. 356:581-588(2001).
RN [8]
RP INVOLVEMENT IN ATSX2 AND ASPGX2.
RX PubMed=14963808; DOI=10.1086/382137;
RA Laumonnier F., Bonnet-Brilhault F., Gomot M., Blanc R., David A.,
RA Moizard M.-P., Raynaud M., Ronce N., Lemonnier E., Calvas P., Laudier B.,
RA Chelly J., Fryns J.-P., Ropers H.-H., Hamel B.C.J., Andres C.,
RA Barthelemy C., Moraine C., Briault S.;
RT "X-linked mental retardation and autism are associated with a mutation in
RT the NLGN4 gene, a member of the neuroligin family.";
RL Am. J. Hum. Genet. 74:552-557(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 44-619 ALONE AND IN COMPLEX WITH
RP RAT NRXN1, GLYCOSYLATION AT ASN-102 AND ASN-511, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=18093521; DOI=10.1016/j.neuron.2007.11.013;
RA Fabrichny I.P., Leone P., Sulzenbacher G., Comoletti D., Miller M.T.,
RA Taylor P., Bourne Y., Marchot P.;
RT "Structural analysis of the synaptic protein neuroligin and its beta-
RT neurexin complex: determinants for folding and cell adhesion.";
RL Neuron 56:979-991(2007).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] SER-214.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Putative neuronal cell surface protein involved in cell-cell-
CC interactions.
CC -!- SUBUNIT: Homodimer. Interacts with NRXN1 in a calcium-dependent manner.
CC Interacts through its C-terminus with DLG4/PSD-95 third PDZ domain.
CC {ECO:0000269|PubMed:11368788, ECO:0000269|PubMed:18093521,
CC ECO:0000269|PubMed:9278515}.
CC -!- INTERACTION:
CC Q8N0W4; Q63373-3: Nrxn1; Xeno; NbExp=5; IntAct=EBI-2862707, EBI-20994045;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Postsynaptic density membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N0W4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N0W4-2; Sequence=VSP_013270;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in heart. Expressed at
CC lower levels in liver, skeletal muscle and pancreas and at very low
CC levels in brain. {ECO:0000269|PubMed:11368788}.
CC -!- DISEASE: Autism, X-linked 2 (AUTSX2) [MIM:300495]: A complex
CC multifactorial, pervasive developmental disorder characterized by
CC impairments in reciprocal social interaction and communication,
CC restricted and stereotyped patterns of interests and activities, and
CC the presence of developmental abnormalities by 3 years of age. Most
CC individuals with autism also manifest moderate intellectual disability.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- DISEASE: Asperger syndrome, X-linked, 2 (ASPGX2) [MIM:300497]: A
CC syndrome with features similar to autism. Affected individuals exhibit
CC qualitative impairment in social interaction, as manifest by impairment
CC in the use of non-verbal behaviors such as eye-to-eye gaze, facial
CC expression, body postures, and gestures, failure to develop appropriate
CC peer relationships, and lack of social sharing or reciprocity. Patients
CC also exhibit restricted, repetitive and stereotyped patterns of
CC behavior, interests, and activities, including abnormal preoccupation
CC with certain activities and inflexible adherence to routines or
CC rituals. Asperger syndrome is primarily distinguished from autism by
CC the higher cognitive abilities and a more normal and timely development
CC of language and communicative phrases. {ECO:0000269|PubMed:14963808}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86574.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF376803; AAM46112.1; -; mRNA.
DR EMBL; AB033086; BAA86574.1; ALT_INIT; mRNA.
DR EMBL; BC034018; AAH34018.1; -; mRNA.
DR EMBL; AY358562; AAQ88925.1; -; mRNA.
DR CCDS; CCDS14126.1; -. [Q8N0W4-1]
DR RefSeq; NP_001269074.1; NM_001282145.1. [Q8N0W4-1]
DR RefSeq; NP_001269075.1; NM_001282146.1. [Q8N0W4-1]
DR RefSeq; NP_065793.1; NM_020742.3. [Q8N0W4-1]
DR RefSeq; NP_851849.1; NM_181332.2. [Q8N0W4-1]
DR RefSeq; XP_005274621.1; XM_005274564.2. [Q8N0W4-2]
DR RefSeq; XP_005274622.1; XM_005274565.2. [Q8N0W4-2]
DR RefSeq; XP_005274623.1; XM_005274566.4. [Q8N0W4-2]
DR RefSeq; XP_006724567.1; XM_006724504.3. [Q8N0W4-2]
DR RefSeq; XP_011543849.1; XM_011545547.2. [Q8N0W4-2]
DR RefSeq; XP_011543850.1; XM_011545548.2. [Q8N0W4-2]
DR RefSeq; XP_016885179.1; XM_017029690.1.
DR RefSeq; XP_016885180.1; XM_017029691.1. [Q8N0W4-1]
DR RefSeq; XP_016885181.1; XM_017029692.1. [Q8N0W4-1]
DR RefSeq; XP_016885182.1; XM_017029693.1. [Q8N0W4-1]
DR PDB; 2WQZ; X-ray; 3.90 A; A/B=43-619.
DR PDB; 2XB6; X-ray; 2.60 A; A/B=44-619.
DR PDB; 3BE8; X-ray; 2.20 A; A/B=44-619.
DR PDBsum; 2WQZ; -.
DR PDBsum; 2XB6; -.
DR PDBsum; 3BE8; -.
DR AlphaFoldDB; Q8N0W4; -.
DR SMR; Q8N0W4; -.
DR BioGRID; 121567; 3.
DR IntAct; Q8N0W4; 4.
DR MINT; Q8N0W4; -.
DR STRING; 9606.ENSP00000370485; -.
DR ESTHER; human-NLGN4X; Neuroligin.
DR MEROPS; S09.988; -.
DR TCDB; 8.A.117.1.3; the neuroligin (nlg) family.
DR GlyGen; Q8N0W4; 2 sites.
DR iPTMnet; Q8N0W4; -.
DR PhosphoSitePlus; Q8N0W4; -.
DR BioMuta; NLGN4X; -.
DR DMDM; 31076821; -.
DR EPD; Q8N0W4; -.
DR jPOST; Q8N0W4; -.
DR MassIVE; Q8N0W4; -.
DR PaxDb; Q8N0W4; -.
DR PeptideAtlas; Q8N0W4; -.
DR PRIDE; Q8N0W4; -.
DR ProteomicsDB; 71472; -. [Q8N0W4-1]
DR ProteomicsDB; 71473; -. [Q8N0W4-2]
DR Antibodypedia; 469; 209 antibodies from 30 providers.
DR DNASU; 57502; -.
DR Ensembl; ENST00000275857.10; ENSP00000275857.6; ENSG00000146938.16. [Q8N0W4-1]
DR Ensembl; ENST00000381092.1; ENSP00000370482.1; ENSG00000146938.16. [Q8N0W4-1]
DR Ensembl; ENST00000381093.6; ENSP00000370483.3; ENSG00000146938.16. [Q8N0W4-1]
DR Ensembl; ENST00000381095.8; ENSP00000370485.3; ENSG00000146938.16. [Q8N0W4-1]
DR Ensembl; ENST00000538097.6; ENSP00000439203.3; ENSG00000146938.16. [Q8N0W4-2]
DR GeneID; 57502; -.
DR KEGG; hsa:57502; -.
DR MANE-Select; ENST00000381095.8; ENSP00000370485.3; NM_181332.3; NP_851849.1.
DR UCSC; uc004crq.5; human. [Q8N0W4-1]
DR CTD; 57502; -.
DR DisGeNET; 57502; -.
DR GeneCards; NLGN4X; -.
DR HGNC; HGNC:14287; NLGN4X.
DR HPA; ENSG00000146938; Tissue enhanced (brain, lymphoid tissue).
DR MalaCards; NLGN4X; -.
DR MIM; 300427; gene.
DR MIM; 300495; phenotype.
DR MIM; 300497; phenotype.
DR neXtProt; NX_Q8N0W4; -.
DR OpenTargets; ENSG00000146938; -.
DR Orphanet; 1162; NON RARE IN EUROPE: Asperger syndrome.
DR Orphanet; 106; NON RARE IN EUROPE: Autism.
DR PharmGKB; PA31650; -.
DR VEuPathDB; HostDB:ENSG00000146938; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000156607; -.
DR InParanoid; Q8N0W4; -.
DR OMA; WGCKSAS; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q8N0W4; -.
DR TreeFam; TF326187; -.
DR PathwayCommons; Q8N0W4; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; Q8N0W4; -.
DR SIGNOR; Q8N0W4; -.
DR BioGRID-ORCS; 57502; 7 hits in 685 CRISPR screens.
DR ChiTaRS; NLGN4X; human.
DR EvolutionaryTrace; Q8N0W4; -.
DR GeneWiki; NLGN4X; -.
DR GenomeRNAi; 57502; -.
DR Pharos; Q8N0W4; Tbio.
DR PRO; PR:Q8N0W4; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8N0W4; protein.
DR Bgee; ENSG00000146938; Expressed in middle temporal gyrus and 157 other tissues.
DR ExpressionAtlas; Q8N0W4; baseline and differential.
DR Genevisible; Q8N0W4; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098985; C:asymmetric, glutamatergic, excitatory synapse; TAS:ARUK-UCL.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
DR GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
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; TAS:BHF-UCL.
DR GO; GO:0031404; F:chloride ion binding; IDA:UniProtKB.
DR GO; GO:0042043; F:neurexin family protein binding; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0030534; P:adult behavior; IMP:BHF-UCL.
DR GO; GO:0003360; P:brainstem development; ISS:BHF-UCL.
DR GO; GO:0045216; P:cell-cell junction organization; NAS:UniProtKB.
DR GO; GO:0021549; P:cerebellum development; ISS:BHF-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007612; P:learning; IMP:BHF-UCL.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IDA:BHF-UCL.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0030182; P:neuron differentiation; NAS:BHF-UCL.
DR GO; GO:0035265; P:organ growth; ISS:BHF-UCL.
DR GO; GO:0097104; P:postsynaptic membrane assembly; IBA:GO_Central.
DR GO; GO:0099054; P:presynapse assembly; TAS:ARUK-UCL.
DR GO; GO:0097105; P:presynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0035176; P:social behavior; IMP:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IMP:UniProtKB.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:0071625; P:vocalization behavior; 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; IPR030025; NLGN4.
DR PANTHER; PTHR43903:SF5; PTHR43903:SF5; 2.
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; Asperger syndrome; Autism;
KW Autism spectrum disorder; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Signal;
KW Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..41
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 42..816
FT /note="Neuroligin-4, X-linked"
FT /id="PRO_0000008648"
FT TOPO_DOM 42..676
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 677..697
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 698..816
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 359..364
FT /note="Interaction with NRXN1"
FT REGION 636..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62889"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18093521"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18093521"
FT DISULFID 110..146
FT /evidence="ECO:0000269|PubMed:18093521"
FT DISULFID 306..317
FT /evidence="ECO:0000269|PubMed:18093521"
FT DISULFID 476..510
FT /evidence="ECO:0000269|PubMed:18093521"
FT VAR_SEQ 157
FT /note="D -> DGANTKKNADDITSNDRGEDE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_013270"
FT VARIANT 214
FT /note="G -> S (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs749477993)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036576"
FT CONFLICT 456
FT /note="Missing (in Ref. 4; AAQ88925)"
FT /evidence="ECO:0000305"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:3BE8"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2XB6"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:3BE8"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 222..237
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 243..253
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:3BE8"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:2XB6"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:3BE8"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 293..303
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 323..327
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 353..358
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 365..372
FT /evidence="ECO:0007829|PDB:3BE8"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:3BE8"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 392..406
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:2XB6"
FT HELIX 413..423
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 433..448
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 450..461
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 478..481
FT /evidence="ECO:0007829|PDB:2XB6"
FT TURN 489..492
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 514..533
FT /evidence="ECO:0007829|PDB:3BE8"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 568..575
FT /evidence="ECO:0007829|PDB:3BE8"
FT STRAND 577..581
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 584..591
FT /evidence="ECO:0007829|PDB:3BE8"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:3BE8"
SQ SEQUENCE 816 AA; 91915 MW; EA1320D690F76BBD CRC64;
MSRPQGLLWL PLLFTPVCVM LNSNVLLWLT ALAIKFTLID SQAQYPVVNT NYGKIRGLRT
PLPNEILGPV EQYLGVPYAS PPTGERRFQP PEPPSSWTGI RNTTQFAAVC PQHLDERSLL
HDMLPIWFTA NLDTLMTYVQ DQNEDCLYLN IYVPTEDDIH DQNSKKPVMV YIHGGSYMEG
TGNMIDGSIL ASYGNVIVIT INYRLGILGF LSTGDQAAKG NYGLLDQIQA LRWIEENVGA
FGGDPKRVTI FGSGAGASCV SLLTLSHYSE GLFQKAIIQS GTALSSWAVN YQPAKYTRIL
ADKVGCNMLD TTDMVECLRN KNYKELIQQT ITPATYHIAF GPVIDGDVIP DDPQILMEQG
EFLNYDIMLG VNQGEGLKFV DGIVDNEDGV TPNDFDFSVS NFVDNLYGYP EGKDTLRETI
KFMYTDWADK ENPETRRKTL VALFTDHQWV APAVATADLH AQYGSPTYFY AFYHHCQSEM
KPSWADSAHG DEVPYVFGIP MIGPTELFSC NFSKNDVMLS AVVMTYWTNF AKTGDPNQPV
PQDTKFIHTK PNRFEEVAWS KYNPKDQLYL HIGLKPRVRD HYRATKVAFW LELVPHLHNL
NEIFQYVSTT TKVPPPDMTS FPYGTRRSPA KIWPTTKRPA ITPANNPKHS KDPHKTGPED
TTVLIETKRD YSTELSVTIA VGASLLFLNI LAFAALYYKK DKRRHETHRR PSPQRNTTND
IAHIQNEEIM SLQMKQLEHD HECESLQAHD TLRLTCPPDY TLTLRRSPDD IPLMTPNTIT
MIPNTLTGMQ PLHTFNTFSG GQNSTNLPHG HSTTRV
