ITPR1_BOVIN
ID ITPR1_BOVIN Reviewed; 2709 AA.
AC Q9TU34; Q7M2U0;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Inositol 1,4,5-trisphosphate receptor type 1;
DE AltName: Full=IP3 receptor isoform 1;
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Adrenal medulla;
RX PubMed=11584008; DOI=10.1074/jbc.m107532200;
RA Yoo S.H., Oh Y.S., Kang M.K., Huh Y.H., So S.H., Park H.S., Park H.Y.;
RT "Localization of three types of the inositol 1,4,5-trisphosphate
RT receptor/Ca2+ channel in the secretory granules and coupling with the Ca2+
RT storage proteins chromogranins A and B.";
RL J. Biol. Chem. 276:45806-45812(2001).
RN [2]
RP PROTEIN SEQUENCE OF 75-87; 149-167; 429-440; 833-843; 936-955; 1000-1012;
RP 1130-1135; 1547-1554; 2071-2078 AND 2207-2217.
RX PubMed=2174422; DOI=10.1016/s0021-9258(17)45273-2;
RA Marks A.R., Tempst P., Chadwick C.C., Riviere L., Fleischer S.,
RA Nadal-Ginard B.;
RT "Smooth muscle and brain inositol 1,4,5-trisphosphate receptors are
RT structurally and functionally similar.";
RL J. Biol. Chem. 265:20719-20722(1990).
RN [3]
RP INTERACTION WITH IRAG1.
RX PubMed=10724174; DOI=10.1038/35004606;
RA Schlossmann J., Ammendola A., Ashman K., Zong X., Huber A., Neubauer G.,
RA Wang G.-X., Allescher H.-D., Korth M., Wilm M., Hofmann F., Ruth P.;
RT "Regulation of intracellular calcium by a signalling complex of IRAG, IP3
RT receptor and cGMP kinase Ibeta.";
RL Nature 404:197-201(2000).
RN [4]
RP INTERACTION WITH IRAG1.
RX PubMed=11309393; DOI=10.1074/jbc.m101530200;
RA Ammendola A., Geiselhoeringer A., Hofmann F., Schlossmann J.;
RT "Molecular determinants of the interaction between the inositol 1,4,5-
RT trisphosphate receptor-associated cGMP kinase substrate (IRAG) and cGMP
RT kinase Ibeta.";
RL J. Biol. Chem. 276:24153-24159(2001).
RN [5]
RP SUBUNIT.
RX PubMed=12480535; DOI=10.1016/s0006-291x(02)02799-7;
RA Koller A., Schlossmann J., Ashman K., Uttenweiler-Joseph S., Ruth P.,
RA Hofmann F.;
RT "Association of phospholamban with a cGMP kinase signaling complex.";
RL Biochem. Biophys. Res. Commun. 300:155-160(2003).
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, ECO:0000269|PubMed:11584008}.
CC -!- SUBUNIT: Homotetramer (PubMed:12480535). Interacts with TRPC4. 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
CC (PubMed:10724174, PubMed:11309393). Interacts with CABP1 (via N-
CC terminus) (By similarity). Interacts with TESPA1. Interacts (when not
CC phosphorylated) with AHCYL1 (when phosphorylated); the interaction
CC suppresses inositol 1,4,5-trisphosphate binding to ITPR1 and is
CC increased in the presence of BCL2L10. Interacts with AHCYL2 (with lower
CC affinity than with AHCYL1) (By similarity). Interacts with BCL2L10; the
CC interaction is increased in the presence of AHCLY1 (By similarity).
CC Interacts with BOK (via BH4 domain); protects ITPR1 from proteolysis by
CC CASP3 during apoptosis (By similarity). {ECO:0000250|UniProtKB:P11881,
CC ECO:0000250|UniProtKB:P29994, ECO:0000250|UniProtKB:Q14643,
CC ECO:0000269|PubMed:10724174, ECO:0000269|PubMed:11309393,
CC ECO:0000269|PubMed:12480535}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11584008}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000269|PubMed:11584008}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q14643}. Note=Endoplasmic reticulum and
CC secretory granules (PubMed:11584008). {ECO:0000269|PubMed:11584008}.
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 (By similarity). {ECO:0000250|UniProtKB:P29994}.
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; AF157625; AAF00613.1; -; mRNA.
DR PIR; A38318; A38318.
DR RefSeq; NP_777266.1; NM_174841.2.
DR CORUM; Q9TU34; -.
DR STRING; 9913.ENSBTAP00000047903; -.
DR PaxDb; Q9TU34; -.
DR PRIDE; Q9TU34; -.
DR GeneID; 317697; -.
DR KEGG; bta:317697; -.
DR CTD; 3708; -.
DR eggNOG; KOG3533; Eukaryota.
DR InParanoid; Q9TU34; -.
DR OrthoDB; 94996at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030424; C:axon; IDA:SynGO-UCL.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SynGO-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IDA:SynGO-UCL.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:CACAO.
DR GO; GO:0030141; C:secretory granule; IDA:CACAO.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015278; F:calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IEA:InterPro.
DR GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
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 Apoptosis; Calcium; Calcium channel; Calcium transport; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; 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..2709
FT /note="Inositol 1,4,5-trisphosphate receptor type 1"
FT /id="PRO_0000153919"
FT TOPO_DOM 1..2233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2234..2254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2255..2266
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2267..2287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2288..2312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2313..2333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2334..2356
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2357..2377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2378..2399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2400..2420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2421..2528
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2529..2549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2550..2709
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..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1711..1751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1841..1866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2423..2488
FT /note="Interaction with ERP44"
FT /evidence="ECO:0000250"
FT REGION 2682..2709
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..1161
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 1588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14643"
FT MOD_RES 1715
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q14643, ECO:0000255"
FT MOD_RES 2615
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:0000250|UniProtKB:P29994"
FT CROSSLNK 962
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P29994"
FT CROSSLNK 1571
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P29994"
FT CROSSLNK 1731
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P29994"
FT CROSSLNK 1844
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P29994"
FT CROSSLNK 1845
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P29994"
FT CROSSLNK 1846
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P29994"
FT CROSSLNK 1861
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P29994"
FT CROSSLNK 1884
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P29994"
FT CROSSLNK 2078
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P29994"
FT CROSSLNK 2217
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P29994"
SQ SEQUENCE 2709 AA; 308318 MW; 87E9F69422AE9356 CRC64;
MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PETGDLNNPP 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
SPVKEDKEAF 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 EDEEEVWVFW RDSNKEVRSK SVRELAQDAK
EGQKEDRDVL GYYRYQLNLF ARMCLDRQYL AINEISGQLD VDLILRCMSD ENLPSDLRAS
FCRLMLHMHV DRDPQEQVTP VKYARLWSEI PSEIAIDDYD SSGTSKDEIK ERFAQTMEFV
EEYLRDVVCQ RFPFSDKEKN KLTFEVVNLA RNLIYFGFYN FSDLLRLTKI LLAILDCVHV
TTIFPISKMA KGEENKGSNV MRSIHGVGEL MTQVVLRGGG FLPMTPTATA PEGNVKQAEP
EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE FDESNSQTSE TSSGNSSQEG
PSNVPGALDF EHIEEQAEGI FGGSEETTPL DLDDHGGRTF LRVLLHLTMH DYPPLVSGAL
QLLFRHFSQR QEVLQAFKQV QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE LWVYKGQGPD
EAMDGASGEN EHKKTEEGNN KSQQHESTSS YNYRVVKEIL IRLSKLCVQE SASVRKSRKQ
QQRLLRNMGA HAVVLELLQI PYEKAEDTMM QEIMRLAHEF LQNFCAGNHP NQALLHKHIN
LFLNPGILEA VTMQHIFMNN FQLCSEINER VVQHFVHCIE THGRNVQYIK FLQTIVKAEG
KFIKKCQDMV MAELVNSGED VLVFYNDRAS FQTLIQMMRS ERDRMDENSP LMYHIHLVEL
LAVCTEGKNV YTEIKCNSLL PLDDIVRVVT HEDCIPEVKI AYINFLNHCY VDPEVEMKEI
YTSNHMWKLF ENFLVDICRA CNNTSDRKHA DSILEKYVTE IVMSIVTTFF SSPFSDQSTT
LQTRQPVFVQ LLQGVFRVYH CNWLMPSQKA SVESCIRVLS DVAKSRAIAI PVDLDSQVNN
LFLKSHNLVQ KTAMNWRLTA RNAARRDSVL PVSRDYRNII ERLQDIVSAL EDRLRPLVQA
ELSVLVDVLH RPELLFPENT DARRKCESGG FICKLIKHTK QLLEENEEKL CIKVLQTLRE
MMTKDRGYGE KGEALRQILV NRYYGNIRPS GRRESLTSFG NGPLSPGGPS KPGGGGGGSG
SSPMSRGEMS LAEVQCHLDK EGASNLVIDL IMNASSDRVF HESILLAIAL LEGGNTTIQH
SFFCRLTEDK KSEKFFKVFY DRMKVAQQEI KATVTVNTSD LGNKKKDDEV DRDAPSRKKA
KEPATQITEE VRDQLLEASA ATRKAFTTFR READPDDHYQ SGEGAQAAAD KSKDDLEMSA
VITIMQPILR FLQLLCENHN RDLQNFLRCQ NNKTNYNLVC ETLQFLDCIC GSTTGGLGLL
GLYINEKNVA LINQTLESLT EYCQGPCHEN QNCIATHESN GIDIITALIL NDINPLGKKR
MDLVLELKNN ASKLLLAIME SRHDSENAER ILYNMRPKEL VEVIKKAYMQ GEVEFEDGEN
GEDGAASPRN VGHNIYILAH QLARHNKELQ TMLKPGGQVD GDETLDFYAQ PTGPNEIVRL
DRTMEQIVFP VPSICEFLTK ESKLRIYYTT ERDEQGSKIN DFFLRSEDLF NEMNWQKKLR
AQPVLYWCAR NMSFWSSISF NLAVLMNLLV AFFYPFKGVR GGTLEPHWSG LLWTAMLISL
AIVIALPKPH GIRALIASTI LRLIFSVGLQ PTLFLLGAFN VCNKIIFLMS FVGNCGTFTR
GYRAMVLDVE FLYHLLXLLI CAMGLFVHEF FYSLLLFDLV YREETLLNVI KSVTRNGRSI
ILMAVLALIL VYLFSIVGYL FFKDDFILEV DRLPNETSLP EASESLASEF LYSDVCRVET
GENCSSPAPK EELVPAEETE QDKEHTCETL LMCIVTVLSH GLRSGGGVGD VLRKPSKEEP
LFAARVIYDL LFFFMVIIIV LNLIFGVIID TFADLRSEKQ KKEEILKTTC FICGLERDKF
DNKTVTFEEH IKEEHNMWHY LCFIVLVKVK DSTEYTGPES YVAEMIKERN LDWFPRMRAM
SLVSSDSEGE QNELRNLQEK LESTMKLVTN LSGLLSELKD QMTDQRKQKQ RMGLLGHPPH
INVNPQQPA
