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 24-JAN-2024, entry version 149. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSRNOP00000075549; -. DR iPTMnet; O35412; -. DR PhosphoSitePlus; O35412; -. DR PaxDb; 10116-ENSRNOP00000054996; -. DR GeneID; 246212; -. DR KEGG; rno:246212; -. DR UCSC; RGD:708497; rat. DR AGR; RGD:708497; -. DR CTD; 26037; -. DR RGD; 708497; Sipa1l1. DR eggNOG; KOG3686; Eukaryota. DR InParanoid; O35412; -. DR OrthoDB; 25782at2759; -. DR PhylomeDB; O35412; -. DR PRO; PR:O35412; -. DR Proteomes; UP000002494; Unplaced. 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:0030036; P:actin cytoskeleton organization; 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 CDD; cd00992; PDZ_signaling; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 3.30.1120.160; -; 1. DR Gene3D; 3.40.50.11210; Rap/Ran-GAP; 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; IPR021818; SIPA1L_C. DR PANTHER; PTHR15711; RAP GTPASE-ACTIVATING PROTEIN; 1. DR PANTHER; PTHR15711:SF10; SIGNAL-INDUCED PROLIFERATION-ASSOCIATED 1-LIKE PROTEIN 1; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF21022; Rap-GAP_dimer; 1. DR Pfam; PF02145; Rap_GAP; 1. DR Pfam; PF11881; SPAR_C; 1. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR SUPFAM; SSF111347; Rap/Ran-GAP; 2. 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 //