PACE1_HUMAN
ID PACE1_HUMAN Reviewed; 742 AA.
AC Q8IZE3; A8K8Z2; Q5THA6; Q5THA8; Q8IZN9; Q96C56; Q9UBK6;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Protein-associating with the carboxyl-terminal domain of ezrin;
DE AltName: Full=Ezrin-binding protein PACE-1;
DE AltName: Full=SCY1-like protein 3;
GN Name=SCYL3; Synonyms=PACE1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP EZR, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION,
RP MYRISTOYLATION AT GLY-2, MUTAGENESIS OF 2-GLU--SER-6, AND VARIANT ARG-621.
RC TISSUE=Kidney;
RX PubMed=12651155; DOI=10.1016/s0014-4827(02)00054-x;
RA Sullivan A., Uff C.R., Isacke C.M., Thorne R.F.;
RT "PACE-1, a novel protein that interacts with the C-terminal domain of
RT ezrin.";
RL Exp. Cell Res. 284:224-238(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Rhodes S., Huckle E.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-621.
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-621.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-597.
RC TISSUE=B-cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-707, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May play a role in regulating cell adhesion/migration
CC complexes in migrating cells. {ECO:0000269|PubMed:12651155}.
CC -!- SUBUNIT: Interacts with EZR/VIL2 C-terminal domain.
CC {ECO:0000269|PubMed:12651155}.
CC -!- INTERACTION:
CC Q8IZE3; P15311: EZR; NbExp=5; IntAct=EBI-1380680, EBI-1056902;
CC Q8IZE3; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-1380680, EBI-746969;
CC Q8IZE3; Q68G74: LHX8; NbExp=3; IntAct=EBI-1380680, EBI-8474075;
CC Q8IZE3; Q99757: TXN2; NbExp=4; IntAct=EBI-1380680, EBI-2932492;
CC Q8IZE3-2; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-11959369, EBI-746969;
CC Q8IZE3-2; P60520: GABARAPL2; NbExp=3; IntAct=EBI-11959369, EBI-720116;
CC Q8IZE3-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-11959369, EBI-1055254;
CC Q8IZE3-2; Q9Y4C2-2: TCAF1; NbExp=3; IntAct=EBI-11959369, EBI-11974855;
CC Q8IZE3-2; Q99757: TXN2; NbExp=3; IntAct=EBI-11959369, EBI-2932492;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12651155}. Golgi
CC apparatus {ECO:0000269|PubMed:12651155}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:12651155}. Note=Colocalized with EZR/VIL2, actin
CC and CD44 in lamellipodia.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IZE3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZE3-2; Sequence=VSP_013125;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12651155}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- PTM: May be myristoylated; myristoylation may target it to Golgi
CC compartment. {ECO:0000269|PubMed:12651155}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:12651155}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; AF540957; AAN23123.1; -; mRNA.
DR EMBL; AY144493; AAN41656.1; -; mRNA.
DR EMBL; AL117233; CAB55300.1; -; mRNA.
DR EMBL; AK292507; BAF85196.1; -; mRNA.
DR EMBL; AL031297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90867.1; -; Genomic_DNA.
DR EMBL; BC014662; AAH14662.1; -; mRNA.
DR CCDS; CCDS1286.1; -. [Q8IZE3-2]
DR CCDS; CCDS1287.1; -. [Q8IZE3-1]
DR RefSeq; NP_065156.5; NM_020423.6. [Q8IZE3-2]
DR RefSeq; NP_851607.2; NM_181093.3. [Q8IZE3-1]
DR RefSeq; XP_006711528.1; XM_006711465.1. [Q8IZE3-1]
DR RefSeq; XP_011508103.1; XM_011509801.1. [Q8IZE3-1]
DR RefSeq; XP_016857351.1; XM_017001862.1. [Q8IZE3-2]
DR RefSeq; XP_016857352.1; XM_017001863.1. [Q8IZE3-2]
DR AlphaFoldDB; Q8IZE3; -.
DR SMR; Q8IZE3; -.
DR BioGRID; 121404; 87.
DR IntAct; Q8IZE3; 32.
DR MINT; Q8IZE3; -.
DR STRING; 9606.ENSP00000356746; -.
DR GlyGen; Q8IZE3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IZE3; -.
DR PhosphoSitePlus; Q8IZE3; -.
DR BioMuta; SCYL3; -.
DR DMDM; 61214481; -.
DR EPD; Q8IZE3; -.
DR jPOST; Q8IZE3; -.
DR MassIVE; Q8IZE3; -.
DR MaxQB; Q8IZE3; -.
DR PaxDb; Q8IZE3; -.
DR PeptideAtlas; Q8IZE3; -.
DR PRIDE; Q8IZE3; -.
DR ProteomicsDB; 71333; -. [Q8IZE3-1]
DR ProteomicsDB; 71334; -. [Q8IZE3-2]
DR Antibodypedia; 936; 252 antibodies from 23 providers.
DR DNASU; 57147; -.
DR Ensembl; ENST00000367770.5; ENSP00000356744.1; ENSG00000000457.14. [Q8IZE3-1]
DR Ensembl; ENST00000367771.11; ENSP00000356745.5; ENSG00000000457.14. [Q8IZE3-2]
DR Ensembl; ENST00000367772.8; ENSP00000356746.4; ENSG00000000457.14. [Q8IZE3-1]
DR GeneID; 57147; -.
DR KEGG; hsa:57147; -.
DR MANE-Select; ENST00000367771.11; ENSP00000356745.5; NM_020423.7; NP_065156.5. [Q8IZE3-2]
DR UCSC; uc001ggs.5; human. [Q8IZE3-1]
DR CTD; 57147; -.
DR DisGeNET; 57147; -.
DR GeneCards; SCYL3; -.
DR HGNC; HGNC:19285; SCYL3.
DR HPA; ENSG00000000457; Low tissue specificity.
DR MIM; 608192; gene.
DR neXtProt; NX_Q8IZE3; -.
DR OpenTargets; ENSG00000000457; -.
DR PharmGKB; PA142670945; -.
DR VEuPathDB; HostDB:ENSG00000000457; -.
DR eggNOG; KOG1243; Eukaryota.
DR GeneTree; ENSGT00930000151043; -.
DR InParanoid; Q8IZE3; -.
DR OMA; PQKNGGI; -.
DR OrthoDB; 1074965at2759; -.
DR PhylomeDB; Q8IZE3; -.
DR TreeFam; TF313435; -.
DR PathwayCommons; Q8IZE3; -.
DR SignaLink; Q8IZE3; -.
DR BioGRID-ORCS; 57147; 21 hits in 1113 CRISPR screens.
DR ChiTaRS; SCYL3; human.
DR GeneWiki; SCYL3; -.
DR GenomeRNAi; 57147; -.
DR Pharos; Q8IZE3; Tbio.
DR PRO; PR:Q8IZE3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8IZE3; protein.
DR Bgee; ENSG00000000457; Expressed in buccal mucosa cell and 191 other tissues.
DR ExpressionAtlas; Q8IZE3; baseline and differential.
DR Genevisible; Q8IZE3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; NAS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Golgi apparatus;
KW Lipoprotein; Myristate; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..742
FT /note="Protein-associating with the carboxyl-terminal
FT domain of ezrin"
FT /id="PRO_0000058167"
FT DOMAIN 2..245
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 199..238
FT /note="HEAT 1"
FT REPEAT 285..323
FT /note="HEAT 2"
FT REPEAT 333..370
FT /note="HEAT 3"
FT REPEAT 372..409
FT /note="HEAT 4"
FT REGION 506..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..742
FT /note="Interaction with EZR"
FT /evidence="ECO:0000269|PubMed:12651155"
FT REGION 568..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..742
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBQ7"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:12651155"
FT VAR_SEQ 438..491
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12651155,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_013125"
FT VARIANT 597
FT /note="G -> A (in dbSNP:rs12143301)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_051690"
FT VARIANT 621
FT /note="Q -> R (in dbSNP:rs4656197)"
FT /evidence="ECO:0000269|PubMed:12651155,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5"
FT /id="VAR_051691"
FT MUTAGEN 2..6
FT /note="GSENS->M: No Golgi targeting, accumulates in the
FT cytoplasm."
FT /evidence="ECO:0000269|PubMed:12651155"
FT CONFLICT 613
FT /note="M -> T (in Ref. 1; AAN23123/AAN41656)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 742 AA; 82857 MW; 2F7D03681A4F641B CRC64;
MGSENSALKS YTLREPPFTL PSGLAVYPAV LQDGKFASVF VYKRENEDKV NKAAKHLKTL
RHPCLLRFLS CTVEADGIHL VTERVQPLEV ALETLSSAEV CAGIYDILLA LIFLHDRGHL
THNNVCLSSV FVSEDGHWKL GGMETVCKVS QATPEFLRSI QSIRDPASIP PEEMSPEFTT
LPECHGHARD AFSFGTLVES LLTILNEQVS ADVLSSFQQT LHSTLLNPIP KCRPALCTLL
SHDFFRNDFL EVVNFLKSLT LKSEEEKTEF FKFLLDRVSC LSEELIASRL VPLLLNQLVF
AEPVAVKSFL PYLLGPKKDH AQGETPCLLS PALFQSRVIP VLLQLFEVHE EHVRMVLLSH
IEAYVEHFTQ EQLKKVILPQ VLLGLRDTSD SIVAITLHSL AVLVSLLGPE VVVGGERTKI
FKRTAPSFTK NTDLSLEDSP MCVVCSHHSQ ISPILENPFS SIFPKCFFSG STPINSKKHI
QRDYYNTLLQ TGDPFSQPIK FPINGLSDVK NTSEDSENFP SSSKKSEEWP DWSEPEEPEN
QTVNIQIWPR EPCDDVKSQC TTLDVEESSW DDCEPSSLDT KVNPGGGITA TKPVTSGEQK
PIPALLSLTE ESMPWKSSLP QKISLVQRGD DADQIEPPKV SSQERPLKVP SELGLGEEFT
IQVKKKPVKD PEMDWFADMI PEIKPSAAFL ILPELRTEMV PKKDDVSPVM QFSSKFAAAE
ITEGEAEGWE EEGELNWEDN NW
