SYNJ1_RAT
ID SYNJ1_RAT Reviewed; 1574 AA.
AC Q62910; O89092; Q62911; Q810Z8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Synaptojanin-1;
DE EC=3.1.3.36;
DE AltName: Full=Synaptic inositol 1,4,5-trisphosphate 5-phosphatase 1;
GN Name=Synj1;
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 1; 2; 4 AND 5).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8552192; DOI=10.1038/379353a0;
RA McPherson P.S., Garcia E.P., Slepnev V.I., David C., Zhang X., Grabs D.,
RA Sossin W.S., Bauerfeind R., Nemoto Y., De Camilli P.;
RT "A presynaptic inositol-5-phosphatase.";
RL Nature 379:353-357(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=9710239; DOI=10.1016/s0014-5793(98)00820-5;
RA Woscholski R., Finan P.M., Radley E., Parker P.J.;
RT "Identification and characterisation of a novel splice variant of
RT synaptojanin1.";
RL FEBS Lett. 432:5-8(1998).
RN [3]
RP ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=8798761; DOI=10.1074/jbc.271.40.24856;
RA Ramjaun A.R., McPherson P.S.;
RT "Tissue-specific alternative splicing generates two synaptojanin isoforms
RT with differential membrane binding properties.";
RL J. Biol. Chem. 271:24856-24861(1996).
RN [4]
RP FUNCTION.
RX PubMed=9428629; DOI=10.1016/s0014-5793(97)01451-8;
RA Haffner C., Takei K., Chen H., Ringstad N., Hudson A., Butler M.H.,
RA Salcini A.E., Di Fiore P.P., De Camilli P.;
RT "Synaptojanin 1: localization on coated endocytic intermediates in nerve
RT terminals and interaction of its 170 kDa isoform with Eps15.";
RL FEBS Lett. 419:175-180(1997).
RN [5]
RP INTERACTION WITH SH3GL1; SH3GL2 AND SH3GL3.
RC TISSUE=Brain;
RX PubMed=9238017; DOI=10.1073/pnas.94.16.8569;
RA Ringstad N., Nemoto Y., De Camilli P.;
RT "The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin
RT and dynamin via a Grb2-like Src homology 3 domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8569-8574(1997).
RN [6]
RP INTERACTION WITH SH3GL2; AMPH; DNM1 AND BIN1.
RX PubMed=9341169; DOI=10.1074/jbc.272.43.27239;
RA Micheva K.D., Kay B.K., McPherson P.S.;
RT "Synaptojanin forms two separate complexes in the nerve terminal.
RT Interactions with endophilin and amphiphysin.";
RL J. Biol. Chem. 272:27239-27245(1997).
RN [7]
RP INTERACTION WITH MYO1E.
RX PubMed=17257598; DOI=10.1016/j.febslet.2007.01.021;
RA Krendel M., Osterweil E.K., Mooseker M.S.;
RT "Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in
RT endocytosis.";
RL FEBS Lett. 581:644-650(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820; SER-1053; SER-1175;
RP SER-1350 AND SER-1566, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Phosphatase that acts on various phosphoinositides, including
CC phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-
CC bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate (By
CC similarity). Has a role in clathrin-mediated endocytosis
CC (PubMed:9428629). Hydrolyzes PIP2 bound to actin regulatory proteins
CC resulting in the rearrangement of actin filaments downstream of
CC tyrosine kinase and ASH/GRB2 (By similarity).
CC {ECO:0000250|UniProtKB:O18964, ECO:0000250|UniProtKB:O43426,
CC ECO:0000269|PubMed:9428629}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456; EC=3.1.3.36;
CC -!- SUBUNIT: Interacts with ASH/GRB2. Interacts with PACSIN1, PACSIN2 and
CC PACSIN3 (By similarity). Binds AMPH, SH3GL1, SH3GL2 and SH3GL3
CC (PubMed:9238017, PubMed:9341169). Interacts with MYO1E (via SH3 domain)
CC (PubMed:17257598). Interacts with BIN1 and DNM1 (PubMed:9341169).
CC {ECO:0000250|UniProtKB:Q8CHC4, ECO:0000269|PubMed:17257598,
CC ECO:0000269|PubMed:9238017, ECO:0000269|PubMed:9341169}.
CC -!- INTERACTION:
CC Q62910; O35179: Sh3gl2; NbExp=2; IntAct=EBI-1149123, EBI-1149197;
CC Q62910; O35180: Sh3gl3; NbExp=2; IntAct=EBI-1149123, EBI-1149266;
CC Q62910; Q12965: MYO1E; Xeno; NbExp=2; IntAct=EBI-1149123, EBI-4279548;
CC Q62910; Q99962: SH3GL2; Xeno; NbExp=2; IntAct=EBI-1149123, EBI-77938;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O18964}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=A stop codon is created in position 1309 of isoform 1 due to
CC alternative splicing. {ECO:0000269|PubMed:8798761};
CC Name=1; Synonyms=170 kDa;
CC IsoId=Q62910-1; Sequence=Displayed;
CC Name=2; Synonyms=145 kDa;
CC IsoId=Q62910-2; Sequence=VSP_002686;
CC Name=3; Synonyms=Delta-SAC;
CC IsoId=Q62910-3; Sequence=VSP_002684;
CC Name=4; Synonyms=170 kDa-16AA;
CC IsoId=Q62910-4; Sequence=VSP_002685;
CC Name=5; Synonyms=145 kDa-16AA;
CC IsoId=Q62910-5; Sequence=VSP_002685, VSP_002686;
CC Name=6; Synonyms=Delta-SAC-16AA;
CC IsoId=Q62910-6; Sequence=VSP_002684, VSP_002685;
CC -!- TISSUE SPECIFICITY: Isoform 1 is found in neonatal brain, and in a wide
CC variety of adult non-neuronal tissues. Isoform 2 is expressed
CC predominantly in the neurons, but is also found in all other tissues at
CC much lower levels. Isoform 1 and isoform 2 are detected in the lung and
CC heart. Isoform 1 is expressed at higher levels than isoform 2 in the
CC testis and liver and both isoforms are not detected in the skeletal
CC muscle. Isoform 3 with the 16-amino-acid insert is only found in the
CC brain while isoform 3 without the 16-amino-acid insert is found in the
CC lung.
CC -!- DEVELOPMENTAL STAGE: At embryonic day 12 (E12) only isoform 1 is seen
CC while at E16 and E18 isoform 1 and isoform 2 are seen. In the adult
CC brain expression of isoform 2 increases dramatically as compared with
CC its expression in embryonic brain where as isoform 1 decreases to
CC undetectable levels.
CC -!- DOMAIN: Binds to EPS15 (a clathrin coat-associated protein) via a C-
CC terminal domain containing three Asn-Pro-Phe (NPF) repeats.
CC {ECO:0000250}.
CC -!- DOMAIN: The C-terminal proline-rich region mediates binding to a
CC variety of SH3 domain-containing proteins including AMPH, SH3GL1,
CC SH3GL2, SH3GL3 and GRB2.
CC -!- DOMAIN: Splicing of the SAC1 domain does not alter the catalytic
CC activity of synaptojanin 1.
CC -!- SIMILARITY: Belongs to the synaptojanin family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the inositol 1,4,5-
CC trisphosphate 5-phosphatase family. {ECO:0000305}.
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DR EMBL; U45479; AAB60525.2; -; mRNA.
DR EMBL; U91836; AAO24807.1; -; mRNA.
DR EMBL; AJ006855; CAA07267.1; ALT_TERM; mRNA.
DR PIR; S68448; S68448.
DR RefSeq; NP_445928.2; NM_053476.2. [Q62910-5]
DR AlphaFoldDB; Q62910; -.
DR SMR; Q62910; -.
DR BioGRID; 250042; 21.
DR CORUM; Q62910; -.
DR ELM; Q62910; -.
DR IntAct; Q62910; 15.
DR MINT; Q62910; -.
DR STRING; 10116.ENSRNOP00000045019; -.
DR iPTMnet; Q62910; -.
DR PhosphoSitePlus; Q62910; -.
DR jPOST; Q62910; -.
DR PaxDb; Q62910; -.
DR PRIDE; Q62910; -.
DR Ensembl; ENSRNOT00000052033; ENSRNOP00000045019; ENSRNOG00000002051. [Q62910-2]
DR GeneID; 85238; -.
DR KEGG; rno:85238; -.
DR UCSC; RGD:69434; rat. [Q62910-1]
DR CTD; 8867; -.
DR RGD; 69434; Synj1.
DR VEuPathDB; HostDB:ENSRNOG00000002051; -.
DR eggNOG; KOG0566; Eukaryota.
DR GeneTree; ENSGT00940000157964; -.
DR InParanoid; Q62910; -.
DR OMA; EYVRPRM; -.
DR OrthoDB; 359616at2759; -.
DR PhylomeDB; Q62910; -.
DR Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-RNO-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR Reactome; R-RNO-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q62910; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000002051; Expressed in Ammon's horn and 19 other tissues.
DR ExpressionAtlas; Q62910; baseline and differential.
DR GO; GO:0030132; C:clathrin coat of coated pit; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0030117; C:membrane coat; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0097060; C:synaptic membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043195; C:terminal bouton; ISS:ParkinsonsUK-UCL.
DR GO; GO:0012506; C:vesicle membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:1990175; F:EH domain binding; IDA:RGD.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; IDA:RGD.
DR GO; GO:0034595; F:phosphatidylinositol phosphate 5-phosphatase activity; IDA:RGD.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISO:RGD.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:RGD.
DR GO; GO:0043812; F:phosphatidylinositol-4-phosphate phosphatase activity; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017124; F:SH3 domain binding; IDA:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; ISO:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0006836; P:neurotransmitter transport; ISO:RGD.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISO:RGD.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:RGD.
DR GO; GO:1904980; P:positive regulation of endosome organization; ISO:RGD.
DR GO; GO:0014015; P:positive regulation of gliogenesis; IMP:RGD.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:RGD.
DR GO; GO:0098884; P:postsynaptic neurotransmitter receptor internalization; ISO:RGD.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; IMP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IMP:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0016082; P:synaptic vesicle priming; ISO:RGD.
DR GO; GO:0048489; P:synaptic vesicle transport; ISO:RGD.
DR GO; GO:0016191; P:synaptic vesicle uncoating; ISO:RGD.
DR CDD; cd12719; RRM_SYNJ1; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR002013; SAC_dom.
DR InterPro; IPR034972; SYNJ1.
DR InterPro; IPR015047; SYNJ1/2_RRM.
DR InterPro; IPR034971; SYNJ1_RRM.
DR PANTHER; PTHR11200:SF158; PTHR11200:SF158; 1.
DR Pfam; PF08952; DUF1866; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF02383; Syja_N; 1.
DR SMART; SM01165; DUF1866; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50275; SAC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endocytosis; Hydrolase; Lipid metabolism;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1574
FT /note="Synaptojanin-1"
FT /id="PRO_0000209732"
FT DOMAIN 119..442
FT /note="SAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00183"
FT DOMAIN 894..971
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 1401..1403
FT /note="1"
FT REPEAT 1410..1412
FT /note="2"
FT REPEAT 1421..1423
FT /note="3"
FT REGION 500..899
FT /note="Catalytic"
FT /evidence="ECO:0000255"
FT REGION 1029..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1401..1423
FT /note="3 X 3 AA repeats of N-P-F"
FT REGION 1532..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1253
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1487..1501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1533..1550
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1551..1574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 830
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43426"
FT MOD_RES 1053
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHC4"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1198
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHC4"
FT MOD_RES 1217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43426"
FT MOD_RES 1289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43426"
FT MOD_RES 1350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1354
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8CHC4"
FT MOD_RES 1566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..400
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:9710239"
FT /id="VSP_002684"
FT VAR_SEQ 1141..1156
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:8552192"
FT /id="VSP_002685"
FT VAR_SEQ 1309..1574
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:8552192"
FT /id="VSP_002686"
SQ SEQUENCE 1574 AA; 172881 MW; F24B90CE48F55508 CRC64;
MAFSKGFRIY HKLDPPPFSL IVETRHKEEC LMFESGAVAV LSSAEKEAIK GTYAKVLDAY
GLLGVLRLNL GDTMLHYLVL VTGCMSVGKI QESEVFRVTS TEFISLRVDA SDEDRISEVR
KVLNSGNFYF AWSASGVSLD LSLNAHRSMQ EHTTDNRFFW NQSLHLHLKH YGVNCDDWLL
RLMCGGVEIR TIYAAHKQAK ACLISRLSCE RAGTRFNVRG TNDDGHVANF VETEQVIYLD
DCVSSFIQIR GSVPLFWEQP GLQVGSHRVR MSRGFEANAP AFDRHFRTLK DLYGKQIVVN
LLGSKEGEHM LSKAFQSHLK ASEHASDIHM VSFDYHQMVK GGKAEKLHSV LKPQVQKFLD
YGFFYFDGSA VQRCQSGTVR TNCLDCLDRT NSVQAFLGLE MLAKQLEALG LAEKPQLVTR
FQEVFRSMWS VNGDSISKIY AGTGALEGKA KLKDGARSVT RTIQNNFFDS SKQEAIDVLL
LGNTLNSDLA DKARALLTTG SLRVSEQTLQ SASSKVLKNM CENFYKYSKP KKIRVCVGTW
NVNGGKQFRS IAFKNQTLTD WLLDAPKLAG IQEFQDKRSK PTDIFAIGFE EMVELNAGNI
VNASTTNQKL WAVELQKTIS RDNKYVLLAS EQLVGVCLFV FIRPQHAPFI RDVAVDTVKT
GMGGATGNKG AVAIRMLFHT TSLCFVCSHF AAGQSQVKER NEDFVEIARK LSFPMGRMLF
SHDYVFWCGD FNYRIDLPNE EVKELIRQQN WDSLIAGDQL INQKNAGQIF RGFLEGKVTF
APTYKYDLFS EDYDTSEKCR TPAWTDRVLW RRRKWPFDRS AEDLDLLNAS FQDESKILYT
WTPGTLLHYG RAELKTSDHR PVVALIDIDI FEVEAEERQK IYKEVIAVQG PPDGTVLVSI
KSSAQENTFF DDALIDELLQ QFAHFGEVIL IRFVEDKMWV TFLEGSSALN VLSLNGKELL
NRTITITLKS PDWIKTLEEE MSLEKISVTL PSSTSSTLLG EDAEVSADFD MEGDVDDYSA
EVEELLPQHL QPSSSSGLGT SPSSSPRTSP CQSPTAPEYS APSLPIRPSR APSRTPGPLS
SQGAPVDTQP AAQKESSQTI EPKRPPPPRP VAPPARPAPP QRPPPPSGAR SPAPARKEFG
GVGAPPSPGV TRREMEAPKS PGTARKDNIG RNQPSPQAGL AGPGPSGYGA ARPTIPARAG
VISAPQSQAR VSAGRLTPES QSKPLETSKG PAVLPEPLKP QAAFPPQPSL PTPAQKLQDP
LVPIAAPMPP SIPQSNLETP PLPPPRSRSS QSLPSDSSPQ LQQEQPTGQQ VKINGACGVK
QEPTLKSDPF EDLSLSVLAV SKAQPSAQIS PVLTPDPKML IQLPSASQSK VNSLSSVSCM
LTMPPVPEQS KSQESVGSSA NPFPSLPTRN PFTDRTAAPG NPFRVQSQES EATSWLSKEE
PVSNSPFPPL MPLSHDMSKP SSSLDGFEDN FDLQSQSTVK TSNPKGWVTF DEDEDFPTKG
KSRSVYPDSL GNTAASFDDD WSKGTNVSFC VLPARRPPPP PPPVPLLPPG TTSSAGPSTT
LSSKASPTLD FTER
