ITPR1_RAT
ID ITPR1_RAT Reviewed; 2750 AA.
AC P29994; Q62869;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor type 1;
DE AltName: Full=IP3 receptor isoform 1;
DE Short=IP-3-R;
DE Short=IP3R 1;
DE Short=InsP3R1;
DE AltName: Full=Type 1 inositol 1,4,5-trisphosphate receptor;
DE Short=Type 1 InsP3 receptor;
GN Name=Itpr1; Synonyms=Insp3r;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, AND
RP VARIANT PHE-1372 DEL.
RX PubMed=2165071; DOI=10.1016/s0021-9258(19)38397-8;
RA Mignery G.A., Newton C.L., Archer B.T. III, Suedhof T.C.;
RT "Structure and expression of the rat inositol 1,4,5-trisphosphate
RT receptor.";
RL J. Biol. Chem. 265:12679-12685(1990).
RN [2]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 7), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1849282; DOI=10.1073/pnas.88.7.2951;
RA Danoff S.K., Ferris C.D., Donath C., Fischer G.A., Munemitsu S.,
RA Ullrich A., Snyder S.H., Ross C.A.;
RT "Inositol 1,4,5-trisphosphate receptors: distinct neuronal and nonneuronal
RT forms derived by alternative splicing differ in phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2951-2955(1991).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 7 AND 8).
RC STRAIN=Sprague-Dawley;
RX PubMed=9073177; DOI=10.1016/s0169-328x(96)00282-3;
RA Smutzer G., Zimmerman J.E., Hahn C.-G., Ruscheinsky D.D., Rodriguez A.,
RA Han L.-Y., Arnold S.E.;
RT "Inositol 1,4,5-trisphosphate receptor expression in mammalian olfactory
RT tissue.";
RL Brain Res. Mol. Brain Res. 44:347-354(1997).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10506212; DOI=10.1074/jbc.274.41.29483;
RA Galvan D.L., Borrego-Diaz E., Perez P.J., Mignery G.A.;
RT "Subunit oligomerization, and topology of the inositol 1,4, 5-trisphosphate
RT receptor.";
RL J. Biol. Chem. 274:29483-29492(1999).
RN [5]
RP INTERACTION WITH TRPC4.
RX PubMed=11163362; DOI=10.1016/s0014-5793(00)02362-0;
RA Mery L., Magnino F., Schmidt K., Krause K.-H., Dufour J.-F.;
RT "Alternative splice variants of hTrp4 differentially interact with the C-
RT terminal portion of the inositol 1,4,5-trisphosphate receptors.";
RL FEBS Lett. 487:377-383(2001).
RN [6]
RP INTERACTION WITH CABP1.
RX PubMed=12032348; DOI=10.1073/pnas.102006299;
RA Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K., Haeseleer F.,
RA Foskett J.K.;
RT "Identification of a family of calcium sensors as protein ligands of
RT inositol trisphosphate receptor Ca(2+) release channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002).
RN [7]
RP UBIQUITINATION AT LYS-916; LYS-962; LYS-1572; LYS-1772; LYS-1885; LYS-1886;
RP LYS-1887; LYS-1902; LYS-1925; LYS-2119 AND LYS-2258.
RX PubMed=18955483; DOI=10.1074/jbc.m807288200;
RA Sliter D.A., Kubota K., Kirkpatrick D.S., Alzayady K.J., Gygi S.P.,
RA Wojcikiewicz R.J.;
RT "Mass spectrometric analysis of type 1 inositol 1,4,5-trisphosphate
RT receptor ubiquitination.";
RL J. Biol. Chem. 283:35319-35328(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1589 AND SER-1756, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Intracellular channel that mediates calcium release from the
CC endoplasmic reticulum following stimulation by inositol 1,4,5-
CC trisphosphate. Involved in the regulation of epithelial secretion of
CC electrolytes and fluid through the interaction with AHCYL1 Plays a role
CC in ER stress-induced apoptosis. Cytoplasmic calcium released from the
CC ER triggers apoptosis by the activation of CaM kinase II, eventually
CC leading to the activation of downstream apoptosis pathways.
CC {ECO:0000250|UniProtKB:P11881}.
CC -!- SUBUNIT: Homotetramer. Interacts with TRPC4 (PubMed:11163362). The
CC PPXXF motif binds HOM1, HOM2 and HOM3. Interacts with RYR1, RYR2,
CC ITPR1, SHANK1 and SHANK3. Interacts with ERP44 in a pH-, redox
CC state- and calcium-dependent manner which results in the inhibition the
CC calcium channel activity. The strength of this interaction inversely
CC correlates with calcium concentration. Part of cGMP kinase signaling
CC complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1,
CC PLN/phospholamban, PRKG1 and ITPR1. Interacts with IRAG1 (By
CC similarity). Interacts with CABP1 (via N-terminus) (PubMed:12032348).
CC Interacts with TESPA1. Interacts (when not phosphorylated) with AHCYL1
CC (when phosphorylated); the interaction suppresses inositol 1,4,5-
CC trisphosphate binding to ITPR1 and is increased in the presence of
CC BCL2L10. Interacts with AHCYL2 (with lower affinity than with AHCYL1)
CC (By similarity). Interacts with BCL2L10; the interaction is increased
CC in the presence of AHCLY1 (By similarity). Interacts with BOK (via BH4.
CC domain); protects ITPR1 from proteolysis by CASP3 during apoptosis (By
CC similarity). {ECO:0000250|UniProtKB:P11881,
CC ECO:0000250|UniProtKB:Q14643, ECO:0000250|UniProtKB:Q9TU34,
CC ECO:0000269|PubMed:11163362, ECO:0000269|PubMed:12032348}.
CC -!- INTERACTION:
CC P29994; P54256-1: Hap1; NbExp=2; IntAct=EBI-8614640, EBI-994549;
CC P29994; P54256-2: Hap1; NbExp=4; IntAct=EBI-8614640, EBI-994554;
CC P29994; P51111: Htt; NbExp=4; IntAct=EBI-8614640, EBI-9674649;
CC P29994; P42858: HTT; Xeno; NbExp=2; IntAct=EBI-8614640, EBI-466029;
CC P29994-1; P29994-1: Itpr1; NbExp=2; IntAct=EBI-15683709, EBI-15683709;
CC P29994-1; Q3U182: Crtc2; Xeno; NbExp=2; IntAct=EBI-15683709, EBI-8018890;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9TU34}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000250|UniProtKB:Q9TU34}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q14643}. Note=Endoplasmic reticulum and
CC secretory granules (By similarity). {ECO:0000250|UniProtKB:Q9TU34}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=There is a combination of two alternatively spliced domains
CC at site SI and site SII (A, B and C). Experimental confirmation may
CC be lacking for some isoforms.;
CC Name=1; Synonyms=SISIIABC;
CC IsoId=P29994-1; Sequence=Displayed;
CC Name=2; Synonyms=SI-SIIABC;
CC IsoId=P29994-2; Sequence=VSP_002695;
CC Name=3; Synonyms=SISIIAC;
CC IsoId=P29994-3; Sequence=VSP_002697;
CC Name=4; Synonyms=SI-SIIAC;
CC IsoId=P29994-4; Sequence=VSP_002695, VSP_002697;
CC Name=5; Synonyms=SISIIA;
CC IsoId=P29994-5; Sequence=VSP_002697, VSP_002698;
CC Name=6; Synonyms=SI-SIIA;
CC IsoId=P29994-6; Sequence=VSP_002695, VSP_002697, VSP_002698;
CC Name=7; Synonyms=SISII;
CC IsoId=P29994-7; Sequence=VSP_002696, VSP_002697, VSP_002698;
CC Name=8; Synonyms=SI-SII;
CC IsoId=P29994-8; Sequence=VSP_002695, VSP_002696, VSP_002697,
CC VSP_002698;
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in the brain.
CC {ECO:0000269|PubMed:2165071}.
CC -!- TISSUE SPECIFICITY: [Isoform 7]: Expressed in the fetal brain and
CC peripheral tissues. {ECO:0000269|PubMed:1849282}.
CC -!- DOMAIN: The receptor contains a calcium channel in its C-terminal
CC extremity. Its large N-terminal cytoplasmic region has the ligand-
CC binding site in the N-terminus and modulatory sites in the middle
CC portion immediately upstream of the channel region.
CC -!- PTM: Phosphorylated by cAMP kinase (PKA). Phosphorylation prevents the
CC ligand-induced opening of the calcium channels. Phosphorylation by PKA
CC increases the interaction with inositol 1,4,5-trisphosphate and
CC decreases the interaction with AHCYL1. {ECO:0000250|UniProtKB:P11881}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000250|UniProtKB:Q14643}.
CC -!- PTM: Ubiquitination at multiple lysines targets ITPR1 for proteasomal
CC degradation. Approximately 40% of the ITPR1-associated ubiquitin is
CC monoubiquitin, and polyubiquitins are both 'Lys-48'- and 'Lys-63'-
CC linked. {ECO:0000269|PubMed:18955483}.
CC -!- PTM: Palmitoylated by ZDHHC6 in immune cells, leading to regulation of
CC ITPR1 stability and function. {ECO:0000250|UniProtKB:P11881}.
CC -!- MISCELLANEOUS: Calcium appears to inhibit ligand binding to the
CC receptor, most probably by interacting with a distinct calcium-binding
CC protein which then inhibits the receptor.
CC -!- SIMILARITY: Belongs to the InsP3 receptor family. {ECO:0000305}.
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DR EMBL; J05510; AAA41358.1; -; mRNA.
DR EMBL; J05510; AAA41357.1; -; mRNA.
DR EMBL; M64699; AAA41447.1; -; mRNA.
DR EMBL; M64698; AAA41448.1; -; mRNA.
DR EMBL; U38653; AAC53099.1; -; mRNA.
DR EMBL; U38812; AAC53100.1; -; mRNA.
DR EMBL; U38665; AAB51330.1; -; mRNA.
DR PIR; A36579; A36579.
DR PIR; B36579; B36579.
DR RefSeq; NP_001257526.1; NM_001270597.1.
DR PDB; 3JAV; EM; 4.70 A; A/B/C/D=1-2750.
DR PDB; 3T8S; X-ray; 3.77 A; A/B=7-602.
DR PDB; 3UJ0; X-ray; 3.60 A; A/B=1-604.
DR PDB; 3UJ4; X-ray; 3.00 A; A/B=1-604.
DR PDB; 6MU1; EM; 4.10 A; A/B/C/D=1-2739.
DR PDB; 6MU2; EM; 3.90 A; A/B/C/D=1-2750.
DR PDB; 7LHE; EM; 3.30 A; A/B/C/D=6-2739.
DR PDB; 7LHF; EM; 2.96 A; A/B/C/D=6-2741.
DR PDBsum; 3JAV; -.
DR PDBsum; 3T8S; -.
DR PDBsum; 3UJ0; -.
DR PDBsum; 3UJ4; -.
DR PDBsum; 6MU1; -.
DR PDBsum; 6MU2; -.
DR PDBsum; 7LHE; -.
DR PDBsum; 7LHF; -.
DR SMR; P29994; -.
DR BioGRID; 247302; 15.
DR CORUM; P29994; -.
DR DIP; DIP-29715N; -.
DR IntAct; P29994; 9.
DR MINT; P29994; -.
DR STRING; 10116.ENSRNOP00000063885; -.
DR BindingDB; P29994; -.
DR ChEMBL; CHEMBL2804; -.
DR iPTMnet; P29994; -.
DR PhosphoSitePlus; P29994; -.
DR SwissPalm; P29994; -.
DR jPOST; P29994; -.
DR PaxDb; P29994; -.
DR PRIDE; P29994; -.
DR ABCD; P29994; 1 sequenced antibody.
DR GeneID; 25262; -.
DR KEGG; rno:25262; -.
DR CTD; 3708; -.
DR RGD; 2933; Itpr1.
DR eggNOG; KOG3533; Eukaryota.
DR InParanoid; P29994; -.
DR OrthoDB; 94996at2759; -.
DR PhylomeDB; P29994; -.
DR Reactome; R-RNO-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-RNO-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-RNO-418457; cGMP effects.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR Reactome; R-RNO-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR PRO; PR:P29994; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005955; C:calcineurin complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0005637; C:nuclear inner membrane; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0031088; C:platelet dense granule membrane; ISO:RGD.
DR GO; GO:0031094; C:platelet dense tubular network; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0030667; C:secretory granule membrane; IDA:RGD.
DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; IDA:SynGO.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0097060; C:synaptic membrane; IDA:RGD.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019855; F:calcium channel inhibitor activity; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IBA:GO_Central.
DR GO; GO:0098695; F:inositol 1,4,5-trisphosphate receptor activity involved in regulation of postsynaptic cytosolic calcium levels; ISO:RGD.
DR GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:RGD.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0016358; P:dendrite development; IEP:RGD.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; ISO:RGD.
DR GO; GO:0042045; P:epithelial fluid transport; ISO:RGD.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0097421; P:liver regeneration; IMP:RGD.
DR GO; GO:0050849; P:negative regulation of calcium-mediated signaling; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IMP:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:BHF-UCL.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0050882; P:voluntary musculoskeletal movement; ISO:RGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014821; Ins145_P3_rcpt.
DR InterPro; IPR000493; InsP3_rcpt.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR013662; RIH_assoc-dom.
DR InterPro; IPR000699; RIH_dom.
DR InterPro; IPR035910; RyR/IP3R_RIH_dom_sf.
DR Pfam; PF08709; Ins145_P3_rec; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF08454; RIH_assoc; 1.
DR Pfam; PF01365; RYDR_ITPR; 2.
DR PRINTS; PR00779; INSP3RECEPTR.
DR SMART; SM00472; MIR; 4.
DR SUPFAM; SSF100909; SSF100909; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF82109; SSF82109; 2.
DR PROSITE; PS50919; MIR; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Calcium; Calcium channel;
KW Calcium transport; Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Ion channel; Ion transport; Isopeptide bond; Ligand-gated ion channel;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..2750
FT /note="Inositol 1,4,5-trisphosphate receptor type 1"
FT /id="PRO_0000153922"
FT TOPO_DOM 1..2274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2275..2295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2296..2306
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2307..2327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2328..2353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2354..2374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2375..2397
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2398..2418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2419..2440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2441..2461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2462..2569
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2570..2590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2591..2750
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 112..166
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 173..223
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 231..287
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 294..373
FT /note="MIR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 379..435
FT /note="MIR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 1005..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1705..1731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1752..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1882..1907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1933..1953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2464..2529
FT /note="Interaction with ERP44"
FT REGION 2723..2750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265..269
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 508..511
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT BINDING 567..569
FT /ligand="1D-myo-inositol 1,4,5-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:203600"
FT /evidence="ECO:0000250"
FT MOD_RES 482
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1589
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1756
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2656
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
FT LIPID 56
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P11881"
FT LIPID 849
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P11881"
FT CROSSLNK 916
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18955483"
FT CROSSLNK 962
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18955483"
FT CROSSLNK 1572
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18955483"
FT CROSSLNK 1772
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18955483"
FT CROSSLNK 1885
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18955483"
FT CROSSLNK 1886
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18955483"
FT CROSSLNK 1887
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18955483"
FT CROSSLNK 1902
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18955483"
FT CROSSLNK 1925
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18955483"
FT CROSSLNK 2119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18955483"
FT CROSSLNK 2258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18955483"
FT VAR_SEQ 322..336
FT /note="Missing (in isoform 2, isoform 4, isoform 6 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:2165071"
FT /id="VSP_002695"
FT VAR_SEQ 1693..1715
FT /note="Missing (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_002696"
FT VAR_SEQ 1716
FT /note="Missing (in isoform 3, isoform 4, isoform 5, isoform
FT 6, isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:2165071"
FT /id="VSP_002697"
FT VAR_SEQ 1717..1732
FT /note="Missing (in isoform 5, isoform 6, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_002698"
FT VARIANT 1372
FT /note="Missing (in all but PI17 clones)"
FT /evidence="ECO:0000269|PubMed:2165071"
FT CONFLICT 1764
FT /note="P -> R (in Ref. 2; AAA41447/AAA41448)"
FT /evidence="ECO:0000305"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:3UJ4"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:3UJ4"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:3UJ4"
FT HELIX 87..108
FT /evidence="ECO:0007829|PDB:3UJ4"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:3UJ4"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:3UJ4"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:3UJ4"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:3UJ4"
FT TURN 245..248
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:3UJ4"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 313..318
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:3UJ4"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 368..374
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:3UJ4"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 398..406
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 415..423
FT /evidence="ECO:0007829|PDB:3UJ4"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:3UJ4"
FT HELIX 437..462
FT /evidence="ECO:0007829|PDB:3UJ4"
FT HELIX 467..483
FT /evidence="ECO:0007829|PDB:3UJ4"
FT HELIX 504..512
FT /evidence="ECO:0007829|PDB:3UJ4"
FT HELIX 515..522
FT /evidence="ECO:0007829|PDB:3UJ4"
FT HELIX 537..543
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 552..562
FT /evidence="ECO:0007829|PDB:3UJ4"
FT TURN 563..566
FT /evidence="ECO:0007829|PDB:3UJ4"
FT HELIX 568..575
FT /evidence="ECO:0007829|PDB:3UJ4"
FT TURN 576..584
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 585..589
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 591..598
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 603..608
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 612..620
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 621..624
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 629..638
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 646..656
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 659..661
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 703..706
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 713..717
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 720..722
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 725..727
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 728..741
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 744..747
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 750..753
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 754..757
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 762..767
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 776..785
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 786..788
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 792..794
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 823..825
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 827..829
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 831..850
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 857..859
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 860..875
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 881..891
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 892..894
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 965..1003
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1027..1040
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1059..1068
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1069..1072
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1075..1086
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1089..1100
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1113..1123
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1125..1127
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1173..1188
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1195..1198
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1199..1203
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1204..1206
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 1207..1211
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1212..1218
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1226..1228
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1231..1244
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1245..1247
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1249..1255
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1256..1258
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1261..1264
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1270..1276
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1281..1283
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1289..1291
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1292..1294
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1296..1299
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 1306..1310
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1312..1315
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 1316..1321
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1327..1336
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 1347..1358
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1363..1365
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1371..1373
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1374..1377
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1380..1383
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 1384..1386
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1387..1389
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1395..1399
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1404..1411
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1417..1431
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1441..1461
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1600..1612
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1615..1629
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1635..1638
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 1642..1647
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1648..1650
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1652..1660
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1663..1667
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1670..1683
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1685..1688
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1728..1744
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1792..1802
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1804..1811
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 1812..1814
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1818..1832
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1837..1846
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1853..1868
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 1869..1873
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 1961..1965
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1966..1976
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1978..1980
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1982..1986
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 1987..1989
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 1993..1995
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 1999..2011
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 2013..2016
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 2017..2019
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 2022..2024
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 2027..2029
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2030..2042
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 2049..2052
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2053..2056
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 2057..2060
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2063..2066
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2068..2071
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2079..2081
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2082..2099
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2106..2113
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2119..2131
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2151..2163
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 2164..2166
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2170..2173
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2183..2191
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 2193..2199
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 2205..2211
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 2214..2217
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2221..2230
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 2235..2237
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2240..2260
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2265..2271
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2273..2293
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2306..2326
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2333..2347
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2350..2374
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2383..2388
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2390..2407
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 2408..2410
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2413..2421
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2425..2435
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2438..2461
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2464..2466
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 2531..2533
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2534..2541
FT /evidence="ECO:0007829|PDB:7LHE"
FT TURN 2550..2552
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2563..2608
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 2618..2620
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2628..2634
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2638..2650
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 2653..2655
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2658..2668
FT /evidence="ECO:0007829|PDB:7LHE"
FT STRAND 2681..2683
FT /evidence="ECO:0007829|PDB:7LHE"
FT HELIX 2688..2735
FT /evidence="ECO:0007829|PDB:7LHE"
SQ SEQUENCE 2750 AA; 313264 MW; 174BB77CBF6F21AC CRC64;
MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PEAGDLNNPP KKFRDCLFKL
CPMNRYSAQK QFWKAAKPGA NSTTDAVLLN KLHHAADLEK KQNETENRKL LGTVIQYGNV
IQLLHLKSNK YLTVNKRLPA LLEKNAMRVT LDEAGNEGSW FYIQPFYKLR SIGDSVVIGD
KVVLNPVNAG QPLHASSHQL VDNPGCNEVN SVNCNTSWKI VLFMKWSDNK DDILKGGDVV
RLFHAEQEKF LTCDEHRKKQ HVFLRTTGRQ SATSATSSKA LWEVEVVQHD PCRGGAGYWN
SLFRFKHLAT GHYLAAEVDP DFEEECLEFQ PSVDPDQDAS RSRLRNAQEK MVYSLVSVPE
GNDISSIFEL DPTTLRGGDS LVPRNSYVRL RHLCTNTWVH STNIPIDKEE EKPVMLKIGT
SPLKEDKEAF AIVPVSPAEV RDLDFANDAS KVLGSIAGKL EKGTITQNER RSVTKLLEDL
VYFVTGGTNS GQDVLEVVFS KPNRERQKLM REQNILKQIF KLLQAPFTDC GDGPMLRLEE
LGDQRHAPFR HICRLCYRVL RHSQQDYRKN QEYIAKQFGF MQKQIGYDVL AEDTITALLH
NNRKLLEKHI TAAEIDTFVS LVRKNREPRF LDYLSDLCVS MNKSIPVTQE LICKAVLNPT
NADILIETKL VLSRFEFEGV STGENALEAG EDEEEVWLFW RDSNKEIRSK SVRELAQDAK
EGQKEDRDVL SYYRYQLNLF ARMCLDRQYL AINEISGQLD VDLILRCMSD ENLPYDLRAS
FCRLMLHMHV DRDPQEQVTP VKYARLWSEI PSEIAIDDYD SSGASKDEIK ERFAQTMEFV
EEYLRDVVCQ RFPFSDKEKN KLTFEVVNLA RNLIYFGFYN FSDLLRLTKI LLAILDCVHV
TTIFPISKMT KGEENKGSNV MRSIHGVGEL MTQVVLRGGG FLPMTPMAAA PEGNVKQAEP
EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE FDESNSQSSE TSSGNSSQEG
PSNVPGALDF EHIEEQAEGI FGGSEENTPL DLDDHGGRTF LRVLLHLTMH DYPPLVSGAL
QLLFRHFSQR QEVLQAFKQV QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE LWVYKGQGPD
EPMDGASGEN EHKKTEEGTS KPLKHESTSS YNYRVVKEIL IRLSKLCVQE SASVRKSRKQ
QQRLLRNMGA HAVVLELLQI PYEKAEDTKM QEIMRLAHEF LQNFCAGNQQ NQALLHKHIN
LFLNPGILEA VTMQHIFMNN FQLCSEINER VVQHFVHCIE THGRNVQYIK FLQTIVKAEG
KFIKKCQDMV MAELVNSGED VLVFYNDRAS FQTLIQMMRS ERDRMDENSP LFMYHIHLVE
LLAVCTEGKN VYTEIKCNSL LPLDDIVRVV THEDCIPEVK IAYINFLNHC YVDTEVEMKE
IYTSNHMWKL FENFLVDICR ACNNTSDRKH ADSVLEKYVT EIVMSIVTTF FSSPFSDQST
TLQTRQPVFV QLLQGVFRVY HCNWLMPSQK ASVESCIRVL SDVAKSRAIA IPVDLDSQVN
NLFLKSHNIV QKTAMNWRLS ARNAARRDSV LAASRDYRNI IERLQDIVSA LEDRLRPLVQ
AELSVLVDVL HRPELLFPEN TDARRKCESG GFICKLIKHT KQLLEENEEK LCIKVLQTLR
EMMTKDRGYG EKQISIDELE NAELPQPPEA ENSTEQELEP SPPLRQLEDH KRGEALRQIL
VNRYYGNIRP SGRRESLTSF GNGPLSPGGP SKPGGGGGGP GSGSTSRGEM SLAEVQCHLD
KEGASNLVID LIMNASSDRV FHESILLAIA LLEGGNTTIQ HSFFCRLTED KKSEKFFKVF
YDRMKVAQQE IKATVTVNTS DLGNKKKDDE VDRDAPSRKK AKEPTTQITE EVRDQLLEAS
AATRKAFTTF RREADPDDHY QSGEGTQATT DKAKDDLEMS AVITIMQPIL RFLQLLCENH
NRDLQNFLRC QNNKTNYNLV CETLQFLDCI CGSTTGGLGL LGLYINEKNV ALINQTLESL
TEYCQGPCHE NQNCIATHES NGIDIITALI LNDINPLGKK RMDLVLELKN NASKLLLAIM
ESRHDSENAE RILYNMRPKE LVEVIKKAYM QGEVEFEDGE NGEDGAASPR NVGHNIYILA
HQLARHNKEL QTMLKPGGQV DGDEALEFYA KHTAQIEIVR LDRTMEQIVF PVPSICEFLT
KESKLRIYYT TERDEQGSKI NDFFLRSEDL FNEMNWQKKL RAQPVLYWCA RNMSFWSSIS
FNLAVLMNLL VAFFYPFKGV RGGTLEPHWS GLLWTAMLIS LAIVIALPKP HGIRALIAST
ILRLIFSVGL QPTLFLLGAF NVCNKIIFLM SFVGNCGTFT RGYRAMVLDV EFLYHLLYLL
ICAMGLFVHE FFYSLLLFDL VYREETLLNV IKSVTRNGRP IILTAALALI LVYLFSIVGY
LFFKDDFILE VDRLPNETAG PETGESLAND FLYSDVCRVE TGENCTSPAP KEELLPVEET
EQDKEHTCET LLMCIVTVLS HGLRSGGGVG DVLRKPSKEE PLFAARVIYD LLFFFMVIII
VLNLIFGVII DTFADLRSEK QKKEEILKTT CFICGLERDK FDNKTVTFEE HIKEEHNMWH
YLCFIVLVKV KDSTEYTGPE SYVAEMIRER NLDWFPRMRA MSLVSSDSEG EQNELRNLQE
KLESTMKLVT NLSGQLSELK DQMTEQRKQK QRIGLLGHPP HMNVNPQQPA
