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Interleukin-1 receptor accessory protein-like 1 (IL-1-RAPL-1) (IL-1RAPL-1) (IL1RAPL-1) (Oligophrenin-4) (Three immunoglobulin domain-containing IL-1 receptor-related 2) (TIGIRR-2) (X-linked interleukin-1 receptor accessory protein-like 1)

 IRPL1_HUMAN             Reviewed;         696 AA.
Q9NZN1; A0AVG4; Q9UJ53;
22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
22-AUG-2003, sequence version 2.
18-JUL-2018, entry version 160.
RecName: Full=Interleukin-1 receptor accessory protein-like 1;
Short=IL-1-RAPL-1;
Short=IL-1RAPL-1;
Short=IL1RAPL-1;
AltName: Full=Oligophrenin-4;
AltName: Full=Three immunoglobulin domain-containing IL-1 receptor-related 2;
Short=TIGIRR-2;
AltName: Full=X-linked interleukin-1 receptor accessory protein-like 1;
Flags: Precursor;
Name=IL1RAPL1; Synonyms=OPHN4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN NONSPECIFIC XLMR, TISSUE
SPECIFICITY, AND ALTERNATIVE SPLICING.
TISSUE=Fetal brain;
PubMed=10471494; DOI=10.1038/12623;
Carrie A., Jun L., Bienvenu T., Vinet M.-C., McDonell N., Couvert P.,
Zemni R., Cardona A., Van Buggenhout G., Frints S., Hamel B.C.J.,
Moraine C., Ropers H.-H., Strom T., Howell G.R., Whittaker A.,
Ross M.T., Kahn A., Fryns J.-P., Beldjord C., Marynen P., Chelly J.;
"A new member of the IL-1 receptor family highly expressed in
hippocampus and involved in X-linked mental retardation.";
Nat. Genet. 23:25-31(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN MRX21.
PubMed=10757639; DOI=10.1038/sj.ejhg.5200415;
Jin H., Gardner R.J., Viswesvaraiah R., Muntoni F., Roberts R.G.;
"Two novel members of the interleukin-1 receptor gene family, one
deleted in Xp22.3-Xp21.3 mental retardation.";
Eur. J. Hum. Genet. 8:87-94(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain, and Testis;
PubMed=10882729; DOI=10.1074/jbc.M004077200;
Born T.L., Smith D.E., Garka K.E., Renshaw B.R., Bertles J.S.,
Sims J.E.;
"Identification and characterization of two members of a novel class
of the interleukin-1 receptor (IL-1R) family. Delineation of a new
class of IL-1R-related proteins based on signaling.";
J. Biol. Chem. 275:29946-29954(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12777533; DOI=10.1093/molbev/msg134;
Kitano T., Schwarz C., Nickel B., Paeaebo S.;
"Gene diversity patterns at 10 X-chromosomal loci in humans and
chimpanzees.";
Mol. Biol. Evol. 20:1281-1289(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NCS1.
PubMed=12783849; DOI=10.1093/hmg/ddg147;
Bahi N., Friocourt G., Carrie A., Graham M.E., Weiss J.L., Chafey P.,
Fauchereau F., Burgoyne R.D., Chelly J.;
"IL1 receptor accessory protein like, a protein involved in X-linked
mental retardation, interacts with Neuronal Calcium Sensor-1 and
regulates exocytosis.";
Hum. Mol. Genet. 12:1415-1425(2003).
[9]
INVOLVEMENT IN MRX21.
PubMed=16470793; DOI=10.1002/ajmg.a.31107;
Tabolacci E., Pomponi M.G., Pietrobono R., Terracciano A.,
Chiurazzi P., Neri G.;
"A truncating mutation in the IL1RAPL1 gene is responsible for X-
linked mental retardation in the MRX21 family.";
Am. J. Med. Genet. A 140:482-487(2006).
[10]
VARIANTS ARG-379; HIS-618; SER-637 AND VAL-643.
PubMed=18801879; DOI=10.1093/hmg/ddn300;
Piton A., Michaud J.L., Peng H., Aradhya S., Gauthier J., Mottron L.,
Champagne N., Lafreniere R.G., Hamdan F.F., Joober R., Fombonne E.,
Marineau C., Cossette P., Dube M.P., Haghighi P., Drapeau P.,
Barker P.A., Carbonetto S., Rouleau G.A.;
"Mutations in the calcium-related gene IL1RAPL1 are associated with
autism.";
Hum. Mol. Genet. 17:3965-3974(2008).
[11]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 403-561, FUNCTION, AND
DIMERIZATION.
PubMed=15123616; DOI=10.1074/jbc.M403434200;
Khan J.A., Brint E.K., O'Neill L.A.J., Tong L.;
"Crystal structure of the Toll/interleukin-1 receptor domain of human
IL-1RAPL.";
J. Biol. Chem. 279:31664-31670(2004).
-!- FUNCTION: May regulate secretion and presynaptic differentiation
through inhibition of the activity of N-type voltage-gated calcium
channel (PubMed:12783849). May activate the MAP kinase JNK
(PubMed:15123616). Plays a role in neurite outgrowth (By
similarity). During dendritic spine formation can bidirectionally
induce pre- and post-synaptic differentiation of neurons by trans-
synaptically binding to PTPRD (By similarity).
{ECO:0000250|UniProtKB:P59823, ECO:0000250|UniProtKB:P59824,
ECO:0000269|PubMed:12783849, ECO:0000269|PubMed:15123616}.
-!- SUBUNIT: Homodimer (PubMed:15123616). Interacts (calcium-
independent) with NCS1 (PubMed:12783849). Interacts (via the first
immunoglobilin domain) with PTPRD (via the second immunoglobilin
domain); this interaction is PTPRD-splicing-dependent and induces
pre- and post-synaptic differentiation of neurons and is required
for IL1RAPL1-mediated synapse formation (By similarity).
{ECO:0000250|UniProtKB:P59823, ECO:0000269|PubMed:12783849,
ECO:0000269|PubMed:15123616}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12783849};
Single-pass type I membrane protein {ECO:0000269|PubMed:12783849}.
Cytoplasm {ECO:0000269|PubMed:12783849}. Cell projection, axon
{ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Note=May
localize to the cell body and growth cones of dendrite-like
processes. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=1;
Comment=A number of isoforms are produced.;
Name=1;
IsoId=Q9NZN1-1; Sequence=Displayed;
-!- TISSUE SPECIFICITY: Detected at low levels in heart, skeletal
muscle, ovary, skin, amygdala, caudate nucleus, corpus callosum,
hippocampus, substantia nigra and thalamus. Detected at very low
levels in tonsil, prostate, testis, small intestine, placenta,
colon and fetal liver. {ECO:0000269|PubMed:10471494,
ECO:0000269|PubMed:10882729}.
-!- DISEASE: Mental retardation, X-linked 21 (MRX21) [MIM:300143]: A
disorder characterized by significantly below average general
intellectual functioning associated with impairments in adaptive
behavior and manifested during the developmental period.
Intellectual deficiency is the only primary symptom of non-
syndromic X-linked mental retardation, while syndromic mental
retardation presents with associated physical, neurological and/or
psychiatric manifestations. {ECO:0000269|PubMed:10757639,
ECO:0000269|PubMed:16470793}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the interleukin-1 receptor family.
{ECO:0000305}.
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EMBL; AJ243874; CAB56046.1; -; mRNA.
EMBL; AF181284; AAF59411.1; -; mRNA.
EMBL; AF284435; AAG21369.1; -; mRNA.
EMBL; AB102650; BAC81119.1; -; mRNA.
EMBL; AC005748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC121343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC129852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL031466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL031575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471074; EAW99046.1; -; Genomic_DNA.
EMBL; BC126345; AAI26346.1; -; mRNA.
EMBL; BC126347; AAI26348.1; -; mRNA.
CCDS; CCDS14218.1; -. [Q9NZN1-1]
RefSeq; NP_055086.1; NM_014271.3. [Q9NZN1-1]
RefSeq; XP_016884729.1; XM_017029240.1. [Q9NZN1-1]
UniGene; Hs.658912; -.
PDB; 1T3G; X-ray; 2.30 A; A/B=403-561.
PDB; 4M92; X-ray; 1.60 A; B=207-222.
PDB; 5WY8; X-ray; 3.07 A; B=27-349.
PDBsum; 1T3G; -.
PDBsum; 4M92; -.
PDBsum; 5WY8; -.
ProteinModelPortal; Q9NZN1; -.
SMR; Q9NZN1; -.
BioGrid; 116313; 2.
IntAct; Q9NZN1; 1.
STRING; 9606.ENSP00000305200; -.
iPTMnet; Q9NZN1; -.
PhosphoSitePlus; Q9NZN1; -.
BioMuta; IL1RAPL1; -.
DMDM; 34222654; -.
EPD; Q9NZN1; -.
PaxDb; Q9NZN1; -.
PeptideAtlas; Q9NZN1; -.
PRIDE; Q9NZN1; -.
ProteomicsDB; 83457; -.
DNASU; 11141; -.
Ensembl; ENST00000378993; ENSP00000368278; ENSG00000169306. [Q9NZN1-1]
GeneID; 11141; -.
KEGG; hsa:11141; -.
CTD; 11141; -.
DisGeNET; 11141; -.
EuPathDB; HostDB:ENSG00000169306.9; -.
GeneCards; IL1RAPL1; -.
HGNC; HGNC:5996; IL1RAPL1.
MalaCards; IL1RAPL1; -.
MIM; 300143; phenotype.
MIM; 300206; gene.
neXtProt; NX_Q9NZN1; -.
OpenTargets; ENSG00000169306; -.
Orphanet; 777; X-linked non-syndromic intellectual disability.
PharmGKB; PA29812; -.
eggNOG; ENOG410IF3G; Eukaryota.
eggNOG; ENOG4110Z8K; LUCA.
GeneTree; ENSGT00760000119071; -.
HOGENOM; HOG000092977; -.
HOVERGEN; HBG052148; -.
InParanoid; Q9NZN1; -.
KO; K05170; -.
OMA; ITHEQVL; -.
OrthoDB; EOG091G0GXW; -.
PhylomeDB; Q9NZN1; -.
TreeFam; TF333913; -.
Reactome; R-HSA-388844; Receptor-type tyrosine-protein phosphatases.
Reactome; R-HSA-9007892; Interleukin-38 signaling.
ChiTaRS; IL1RAPL1; human.
EvolutionaryTrace; Q9NZN1; -.
GeneWiki; IL1RAPL1; -.
GenomeRNAi; 11141; -.
PRO; PR:Q9NZN1; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000169306; -.
CleanEx; HS_IL1RAPL1; -.
ExpressionAtlas; Q9NZN1; baseline and differential.
Genevisible; Q9NZN1; HS.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; ISS:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; NAS:BHF-UCL.
GO; GO:0005102; F:signaling receptor binding; ISS:BHF-UCL.
GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; TAS:Reactome.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:BHF-UCL.
GO; GO:0045920; P:negative regulation of exocytosis; IDA:UniProtKB.
GO; GO:0030182; P:neuron differentiation; ISS:BHF-UCL.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISS:BHF-UCL.
GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
GO; GO:0097105; P:presynaptic membrane assembly; ISS:BHF-UCL.
GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 2.60.40.10; -; 3.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR015621; IL-1_rcpt_fam.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
PANTHER; PTHR11890; PTHR11890; 1.
Pfam; PF00047; ig; 1.
Pfam; PF01582; TIR; 1.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 2.
SMART; SM00255; TIR; 1.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS50104; TIR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Mental retardation; Polymorphism;
Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 696 Interleukin-1 receptor accessory protein-
like 1.
/FTId=PRO_0000015454.
TOPO_DOM 19 357 Extracellular. {ECO:0000255}.
TRANSMEM 358 378 Helical. {ECO:0000255}.
TOPO_DOM 379 696 Cytoplasmic. {ECO:0000255}.
DOMAIN 19 134 Ig-like C2-type 1.
DOMAIN 143 232 Ig-like C2-type 2.
DOMAIN 242 350 Ig-like C2-type 3.
DOMAIN 403 562 TIR. {ECO:0000255|PROSITE-
ProRule:PRU00204}.
REGION 549 644 Interaction with NCS1.
{ECO:0000269|PubMed:12783849}.
SITE 34 34 Essential for interaction with PTPRD.
{ECO:0000250|UniProtKB:P59823}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 213 213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 331 331 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 31 126 {ECO:0000250|UniProtKB:P59823}.
DISULFID 53 118 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 143 185 {ECO:0000250|UniProtKB:P59823}.
DISULFID 164 216 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 267 334 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VARIANT 379 379 K -> R (in dbSNP:rs138267399).
{ECO:0000269|PubMed:18801879}.
/FTId=VAR_062263.
VARIANT 618 618 Q -> H (in dbSNP:rs890627874).
{ECO:0000269|PubMed:18801879}.
/FTId=VAR_062264.
VARIANT 637 637 T -> S (in dbSNP:rs756672167).
{ECO:0000269|PubMed:18801879}.
/FTId=VAR_062265.
VARIANT 643 643 I -> V (in dbSNP:rs746481663).
{ECO:0000269|PubMed:18801879}.
/FTId=VAR_062266.
STRAND 32 34 {ECO:0000244|PDB:5WY8}.
STRAND 40 44 {ECO:0000244|PDB:5WY8}.
STRAND 49 52 {ECO:0000244|PDB:5WY8}.
HELIX 54 58 {ECO:0000244|PDB:5WY8}.
HELIX 64 69 {ECO:0000244|PDB:5WY8}.
STRAND 73 84 {ECO:0000244|PDB:5WY8}.
STRAND 93 99 {ECO:0000244|PDB:5WY8}.
STRAND 102 107 {ECO:0000244|PDB:5WY8}.
HELIX 110 112 {ECO:0000244|PDB:5WY8}.
STRAND 114 121 {ECO:0000244|PDB:5WY8}.
STRAND 126 136 {ECO:0000244|PDB:5WY8}.
STRAND 142 144 {ECO:0000244|PDB:5WY8}.
STRAND 150 155 {ECO:0000244|PDB:5WY8}.
STRAND 160 163 {ECO:0000244|PDB:5WY8}.
HELIX 168 170 {ECO:0000244|PDB:5WY8}.
STRAND 180 183 {ECO:0000244|PDB:5WY8}.
STRAND 200 205 {ECO:0000244|PDB:5WY8}.
HELIX 208 210 {ECO:0000244|PDB:5WY8}.
STRAND 212 220 {ECO:0000244|PDB:5WY8}.
STRAND 223 234 {ECO:0000244|PDB:5WY8}.
STRAND 243 247 {ECO:0000244|PDB:5WY8}.
STRAND 259 261 {ECO:0000244|PDB:5WY8}.
STRAND 263 271 {ECO:0000244|PDB:5WY8}.
STRAND 274 277 {ECO:0000244|PDB:5WY8}.
STRAND 280 285 {ECO:0000244|PDB:5WY8}.
TURN 295 297 {ECO:0000244|PDB:5WY8}.
STRAND 298 300 {ECO:0000244|PDB:5WY8}.
STRAND 304 309 {ECO:0000244|PDB:5WY8}.
STRAND 312 323 {ECO:0000244|PDB:5WY8}.
TURN 326 328 {ECO:0000244|PDB:5WY8}.
STRAND 330 338 {ECO:0000244|PDB:5WY8}.
STRAND 341 348 {ECO:0000244|PDB:5WY8}.
STRAND 405 410 {ECO:0000244|PDB:1T3G}.
HELIX 426 431 {ECO:0000244|PDB:1T3G}.
HELIX 433 440 {ECO:0000244|PDB:1T3G}.
HELIX 449 452 {ECO:0000244|PDB:1T3G}.
HELIX 459 468 {ECO:0000244|PDB:1T3G}.
STRAND 470 477 {ECO:0000244|PDB:1T3G}.
HELIX 479 483 {ECO:0000244|PDB:1T3G}.
TURN 484 487 {ECO:0000244|PDB:1T3G}.
HELIX 488 492 {ECO:0000244|PDB:1T3G}.
HELIX 494 501 {ECO:0000244|PDB:1T3G}.
STRAND 504 511 {ECO:0000244|PDB:1T3G}.
HELIX 518 529 {ECO:0000244|PDB:1T3G}.
STRAND 532 538 {ECO:0000244|PDB:1T3G}.
HELIX 542 545 {ECO:0000244|PDB:1T3G}.
STRAND 546 548 {ECO:0000244|PDB:1T3G}.
HELIX 550 558 {ECO:0000244|PDB:1T3G}.
SEQUENCE 696 AA; 79969 MW; 9B7A0B503D73CCA9 CRC64;
MKAPIPHLIL LYATFTQSLK VVTKRGSADG CTDWSIDIKK YQVLVGEPVR IKCALFYGYI
RTNYSLAQSA GLSLMWYKSS GPGDFEEPIA FDGSRMSKEE DSIWFRPTLL QDSGLYACVI
RNSTYCMKVS ISLTVGENDT GLCYNSKMKY FEKAELSKSK EISCRDIEDF LLPTREPEIL
WYKECRTKTW RPSIVFKRDT LLIREVREDD IGNYTCELKY GGFVVRRTTE LTVTAPLTDK
PPKLLYPMES KLTIQETQLG DSANLTCRAF FGYSGDVSPL IYWMKGEKFI EDLDENRVWE
SDIRILKEHL GEQEVSISLI VDSVEEGDLG NYSCYVENGN GRRHASVLLH KRELMYTVEL
AGGLGAILLL LVCLVTIYKC YKIEIMLFYR NHFGAEELDG DNKDYDAYLS YTKVDPDQWN
QETGEEERFA LEILPDMLEK HYGYKLFIPD RDLIPTGTYI EDVARCVDQS KRLIIVMTPN
YVVRRGWSIF ELETRLRNML VTGEIKVILI ECSELRGIMN YQEVEALKHT IKLLTVIKWH
GPKCNKLNSK FWKRLQYEMP FKRIEPITHE QALDVSEQGP FGELQTVSAI SMAAATSTAL
ATAHPDLRST FHNTYHSQMR QKHYYRSYEY DVPPTGTLPL TSIGNQHTYC NIPMTLINGQ
RPQTKSSREQ NPDEAHTNSA ILPLLPRETS ISSVIW


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