SI1L1_RAT
ID SI1L1_RAT Reviewed; 1822 AA.
AC O35412;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Signal-induced proliferation-associated 1-like protein 1;
DE Short=SIPA1-like protein 1;
DE AltName: Full=SPA-1-like protein p1294;
DE AltName: Full=Spine-associated Rap GTPase-activating protein;
DE Short=SPAR;
GN Name=Sipa1l1; Synonyms=Spa1;
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].
RA Takeuchi M., Ide N., Hata Y., Takai Y.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, INTERACTION WITH DLG4, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS
RP OF ARG-743 AND 846-ARG-THR-847, AND TISSUE SPECIFICITY.
RX PubMed=11502259; DOI=10.1016/s0896-6273(01)00355-5;
RA Pak D.T., Yang S., Rudolph-Correia S., Kim E., Sheng M.;
RT "Regulation of dendritic spine morphology by SPAR, a PSD-95-associated
RT RapGAP.";
RL Neuron 31:289-303(2001).
RN [3]
RP INTERACTION WITH LZTS3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16522626; DOI=10.1074/jbc.m601101200;
RA Wendholt D., Spilker C., Schmitt A., Dolnik A., Smalla K.H., Proepper C.,
RA Bockmann J., Sobue K., Gundelfinger E.D., Kreutz M.R., Boeckers T.M.;
RT "ProSAP-interacting protein 1 (ProSAPiP1), a novel protein of the
RT postsynaptic density that links the spine-associated Rap-Gap (SPAR) to the
RT scaffolding protein ProSAP2/Shank3.";
RL J. Biol. Chem. 281:13805-13816(2006).
RN [4]
RP PHOSPHORYLATION.
RX PubMed=18094260; DOI=10.1523/jneurosci.2746-07.2007;
RA Richter M., Murai K.K., Bourgin C., Pak D.T., Pasquale E.B.;
RT "The EphA4 receptor regulates neuronal morphology through SPAR-mediated
RT inactivation of Rap GTPases.";
RL J. Neurosci. 27:14205-14215(2007).
RN [5]
RP PHOSPHORYLATION AT SER-1344 AND THR-1348, UBIQUITINATION, AND MUTAGENESIS
RP OF SER-1344 AND THR-1348.
RX PubMed=18723513; DOI=10.1074/jbc.m802475200;
RA Ang X.L., Seeburg D.P., Sheng M., Harper J.W.;
RT "Regulation of postsynaptic RapGAP SPAR by Polo-like kinase 2 and the
RT SCFbeta-TRCP ubiquitin ligase in hippocampal neurons.";
RL J. Biol. Chem. 283:29424-29432(2008).
RN [6]
RP PHOSPHORYLATION AT SER-1367, UBIQUITINATION, AND MUTAGENESIS OF SER-1367.
RX PubMed=18498738; DOI=10.1016/j.neuron.2008.03.021;
RA Seeburg D.P., Feliu-Mojer M., Gaiottino J., Pak D.T., Sheng M.;
RT "Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic
RT plasticity during elevated activity.";
RL Neuron 58:571-583(2008).
RN [7]
RP INTERACTION WITH PDLIM5 AND PDLIM7.
RX PubMed=19900557; DOI=10.1016/j.mcn.2009.10.009;
RA Herrick S., Evers D.M., Lee J.Y., Udagawa N., Pak D.T.;
RT "Postsynaptic PDLIM5/Enigma homolog binds SPAR and causes dendritic spine
RT shrinkage.";
RL Mol. Cell. Neurosci. 43:188-200(2010).
RN [8]
RP PHOSPHORYLATION, AND UBIQUITINATION.
RX PubMed=21382555; DOI=10.1016/j.neuron.2011.02.004;
RA Lee K.J., Lee Y., Rozeboom A., Lee J.Y., Udagawa N., Hoe H.S., Pak D.T.;
RT "Requirement for Plk2 in orchestrated ras and rap signaling, homeostatic
RT structural plasticity, and memory.";
RL Neuron 69:957-973(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1288; SER-1449; SER-1451;
RP SER-1567; SER-1603 AND SER-1752, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: Stimulates the GTPase activity of RAP2A. Promotes
CC reorganization of the actin cytoskeleton and recruits DLG4 to F-actin.
CC Contributes to the regulation of dendritic spine morphogenesis.
CC {ECO:0000269|PubMed:11502259}.
CC -!- SUBUNIT: Interacts (via PDZ domain) with EPHA4 (via PDZ motif);
CC controls neuronal morphology through regulation of the RAP1 (RAP1A or
CC RAP1B) and RAP2 (RAP2A, RAP2B or RAP2C) GTPases (By similarity).
CC Interacts with DLG4, PDLIM5, PDLIM7 and LZTS3. Interacts with the actin
CC cytoskeleton. {ECO:0000250, ECO:0000269|PubMed:11502259,
CC ECO:0000269|PubMed:16522626, ECO:0000269|PubMed:19900557}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Postsynaptic density.
CC Synapse, synaptosome. Note=Associated with the actin cytoskeleton.
CC Detected at synapses and dendritic spines of cultured hippocampal
CC neurons.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level).
CC {ECO:0000269|PubMed:11502259, ECO:0000269|PubMed:16522626}.
CC -!- PTM: Ubiquitinated and degraded by the SCF(BTRC) following
CC phosphorylation by PLK2.
CC -!- PTM: Phosphorylated at Ser-1367 by CDK5, creating a docking site for
CC the POLO box domains of PLK2. Subsequently, PLK2 binds and
CC phosphorylates SIPA1L1, leading to ubiquitination and degradation by
CC the proteasome. {ECO:0000269|PubMed:18498738}.
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DR EMBL; AF026504; AAB81526.1; -; mRNA.
DR PIR; T14106; T14106.
DR RefSeq; NP_647546.1; NM_139330.1.
DR AlphaFoldDB; O35412; -.
DR SMR; O35412; -.
DR BioGRID; 251530; 7.
DR IntAct; O35412; 1.
DR MINT; O35412; -.
DR STRING; 10116.ENSRNOP00000054996; -.
DR iPTMnet; O35412; -.
DR PhosphoSitePlus; O35412; -.
DR PaxDb; O35412; -.
DR PRIDE; O35412; -.
DR GeneID; 246212; -.
DR KEGG; rno:246212; -.
DR UCSC; RGD:708497; rat.
DR CTD; 26037; -.
DR RGD; 708497; Sipa1l1.
DR eggNOG; KOG3686; Eukaryota.
DR InParanoid; O35412; -.
DR OrthoDB; 28453at2759; -.
DR PhylomeDB; O35412; -.
DR PRO; PR:O35412; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0046875; F:ephrin receptor binding; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
DR GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:RGD.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0099151; P:regulation of postsynaptic density assembly; IDA:SynGO.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IDA:UniProtKB.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.11210; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR InterPro; IPR030770; SIPA1L1.
DR InterPro; IPR021818; SIPA1L_C.
DR PANTHER; PTHR15711:SF10; PTHR15711:SF10; 2.
DR Pfam; PF02145; Rap_GAP; 1.
DR Pfam; PF11881; SPAR_C; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF111347; SSF111347; 2.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; GTPase activation; Methylation;
KW Phosphoprotein; Reference proteome; Synapse; Synaptosome; Ubl conjugation.
FT CHAIN 1..1822
FT /note="Signal-induced proliferation-associated 1-like
FT protein 1"
FT /id="PRO_0000056748"
FT DOMAIN 638..855
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT DOMAIN 992..1068
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1358..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1395..1493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1753..1813
FT /evidence="ECO:0000255"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1183..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1568..1595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1344
FT /note="Phosphoserine; by PLK2"
FT /evidence="ECO:0000269|PubMed:18723513"
FT MOD_RES 1348
FT /note="Phosphothreonine; by PLK2"
FT /evidence="ECO:0000269|PubMed:18723513"
FT MOD_RES 1367
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000269|PubMed:18498738"
FT MOD_RES 1384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1569
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1603
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43166"
FT MOD_RES 1619
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1729
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1747
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C0T5"
FT MOD_RES 1752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 743
FT /note="R->A: Decreases stimulation of the GTPase activity
FT of RAP2A."
FT /evidence="ECO:0000269|PubMed:11502259"
FT MUTAGEN 846..847
FT /note="RT->AS: Abolishes stimulation of the GTPase activity
FT of RAP2A."
FT /evidence="ECO:0000269|PubMed:11502259"
FT MUTAGEN 1344
FT /note="S->A: Abolishes ubiquitination and degradation by
FT the proteasome; when associated with A-1348."
FT /evidence="ECO:0000269|PubMed:18723513"
FT MUTAGEN 1348
FT /note="T->A: Abolishes ubiquitination and degradation by
FT the proteasome; when associated with A-1344."
FT /evidence="ECO:0000269|PubMed:18723513"
FT MUTAGEN 1367
FT /note="S->A: Abolishes phosphorylation by CDK5 and
FT subsequent phosphorylation by PLK2, leading to prevent
FT ubiquitination and degradation by the proteasome."
FT /evidence="ECO:0000269|PubMed:18498738"
SQ SEQUENCE 1822 AA; 201925 MW; 479821CE8820B4FD CRC64;
MTSLKRSQTE RPVTADRASV VSTDGTPKVH TDDFYMRRFR SQNGSLGSSV MAAVGPPRSE
GPHHITSTPG VPKMGVRARI ADWPPRKENV KESSRSSQEI ETSSCLESLS SKGSPVSQGS
SVSLNSNDSA MLKSIQNTLK NKTGPAESMD SRFLMPEAYP SSPRKALRRI RQRSNSDITI
SELDVDSFDE CISPTYKSGP SLHREYGSTS SIDKQGTSGE SFFGLLKGYK DDRADRGPTP
TKLSDFLITG GGKGSGFSLD VIDGPISQRE NLRLFKEREK PLKRRSKSET GDSSIFRKLR
NAKGEELGKS SDLEDNRSED SVRPWTCPKC FAHYDVQSIL FDLNEAIMNR HNVIKRRNTT
TGASAAAVAS LVSGPLSHST SFSSPMGSTE DFNSKGSLGM DQGDDKSNEL VMSCPYFRNE
IGGEGERKIS LSKSNSGSFS GCESTSFESA LSSHCTNAGV AVLEVPKESL MLHLDRVRRY
TVEHVDLGAY YYRKCFYQKE HWNYFGADEN LGPVAVSIRR EKPEDMKENG SPYNYRIIFR
TSELMTLRGS VLEDAIPSTA KHSTARGLPL KEVLEHVIPE LNVQCLRLAF NTPKVTEQLM
KLDEQGLNYQ QKVGIMYCKA GQSTEEEMYN TPKVTEQFMK LDEQGLNYQQ KVGIMYCKAG
QSTEEEMYNN ESAGPAFEEF LQLLGERVRL KGFEKYRAQL DTKTDSTGTH SLYTTYKDYE
IMFHVSTMLP YTPNNKQQLL RKRHIGNDIV TIVFQEPGAQ PFSPKNIRSH FQHVFVIVRA
HNPCTESVCY SVAVTRSRDV PSFGPPIPKG VTFPKSNVFR DFLLAKVINA ENAAHKSEKF
RAMATRTRQE YLKDLAEKNV TNTPIDPSGK FPFISLASKK KEKSKPYPGA ELSSMGAIVW
AVRAKDYNKA MEFDCLLGIS NEFIVLIEQE TKSVVFNCSC RDVIGWTSSD SSLKIFYERG
ECISVESFMS SEDIKEIVKR LQFVSKGCES VEMTLRRNGL GQLGFHVNYE GIVADVEPYG
YAWQAGLKQG SRLVEICKVA VATLSHEQMI DLLRTSVTVK VVIIPPHDDC TPRRSCSETY
RMPVMEYKMN EGVSYEYKFP FRSNNKWQRN AGKGAHSPQV PLQLQSPMIS RVNAGKGDGK
MPLPERAANI PRSISSDGRP LERRLSPGSD IYVTVSSMAL ARSQCRNSPS NLSSSSETGS
GGGTYRQKSM PEGFGVSRRS PASIDRQNTQ SDIGGSGKST PSWQRSEDSL ADQMEPTCHL
PAVSKVLPAF RESPSGRLMR QDPVVHLSPN KQGHSDSHYS SHSSSNTLSS NASSAHSDEK
WYDGDRTESD LNSYNYLQGT SADSGIDTAS YGLSHGSTAS LGASTSSPRS GPGKEKVAPL
WHSSSEVLSL ADRTLETEGH GMDRKTESSL SLDIHSKSQG GSSPLTRENS TFSINDATSH
TSTMSSRHSA SPVVFSSARS SPKEELHPTT SSQLAPSFSS SSSSSSGPRT FYPRQGATSK
YLIGWKKPEG TINSVGFMDT RKRHQSDGNE IAHTRLRAST RDLRASPKPT SKSTIEEDLK
KLIDLESPTP ESQKNFKFHG LSSPQSPFPS TPTSRRALHR TLSDESIYSS QREHFFTSRA
SLLDQALPND VFFSSTYPSL PKSLPLRRPS YTLGMKSLHG EFFASDSSLT DIQETRRQPI
PDPGLMPLPD TASDLDWSNL VDAAKAYEVQ RASFFAASDE NHRPLSAASN SDQLEEQALV
QMKSYSSSKD SSPTLASKVD QLEGMLKMLR EDLKKEKEDK AHLQAEVEHL REDNLRLQEE
SQNASDKLKK FTEWVFNTID MS
