SCYL2_HUMAN
ID SCYL2_HUMAN Reviewed; 929 AA.
AC Q6P3W7; A8KAB5; Q96EF4; Q96ST4; Q9H7V5; Q9NVH3; Q9P2I7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=SCY1-like protein 2 {ECO:0000305};
DE AltName: Full=Coated vesicle-associated kinase of 104 kDa {ECO:0000303|PubMed:15809293};
GN Name=SCYL2 {ECO:0000312|HGNC:HGNC:19286};
GN Synonyms=CVAK104 {ECO:0000303|PubMed:15809293},
GN KIAA1360 {ECO:0000312|EMBL:BAA92598.1};
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 [LARGE SCALE MRNA], AND VARIANT LEU-357.
RC TISSUE=Teratocarcinoma, and Trachea;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Carcinoma, and Leiomyosarcoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-929.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [5]
RP FUNCTION, INTERACTION WITH CLATHRIN AND AP2 COMPLEX, AUTOPHOSPHORYLATION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=15809293; DOI=10.1074/jbc.m502462200;
RA Conner S.D., Schmid S.L.;
RT "CVAK104 is a novel poly-L-lysine-stimulated kinase that targets the beta2-
RT subunit of AP2.";
RL J. Biol. Chem. 280:21539-21544(2005).
RN [6]
RP FUNCTION, INTERACTION WITH CLATHRIN AND AP2 COMPLEX, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16914521; DOI=10.1091/mbc.e06-05-0390;
RA Duewel M., Ungewickell E.J.;
RT "Clathrin-dependent association of CVAK104 with endosomes and the trans-
RT Golgi network.";
RL Mol. Biol. Cell 17:4513-4525(2006).
RN [7]
RP INTERACTION WITH AP2B1.
RX PubMed=16903783; DOI=10.1371/journal.pbio.0040262;
RA Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y.,
RA Mills I.G., Benmerah A., McMahon H.T.;
RT "Role of the AP2 beta-appendage hub in recruiting partners for clathrin-
RT coated vesicle assembly.";
RL PLoS Biol. 4:E262-E262(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677 AND THR-708, AND
RP IDENTIFICATION BY 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 [11]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-357; SER-720 AND HIS-863.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [12]
RP INVOLVEMENT IN AMC4, AND VARIANT AMC4 36-ARG--GLY-929 DEL.
RX PubMed=31960134; DOI=10.1007/s00439-020-02117-7;
RA Seidahmed M.Z., Al-Kindi A., Alsaif H.S., Miqdad A., Alabbad N., Alfifi A.,
RA Abdelbasit O.B., Alhussein K., Alsamadi A., Ibrahim N., Al-Futaisi A.,
RA Al-Maawali A., Alkuraya F.S.;
RT "Recessive mutations in SCYL2 cause a novel syndromic form of
RT arthrogryposis in humans.";
RL Hum. Genet. 139:513-519(2020).
CC -!- FUNCTION: Component of the AP2-containing clathrin coat that may
CC regulate clathrin-dependent trafficking at plasma membrane, TGN and
CC endosomal system (Probable). A possible serine/threonine-protein kinase
CC toward the beta2-subunit of the plasma membrane adapter complex AP2 and
CC other proteins in presence of poly-L-lysine has not been confirmed
CC (PubMed:15809293, PubMed:16914521). By regulating the expression of
CC excitatory receptors at synapses, plays an essential role in neuronal
CC function and signaling and in brain development (By similarity).
CC {ECO:0000250|UniProtKB:Q8CFE4, ECO:0000269|PubMed:15809293,
CC ECO:0000269|PubMed:16914521, ECO:0000305|PubMed:15809293,
CC ECO:0000305|PubMed:16914521}.
CC -!- SUBUNIT: Interacts with clathrin and AP2B1; the interaction mediates
CC the association with the AP-2 complex. {ECO:0000269|PubMed:15809293,
CC ECO:0000269|PubMed:16903783, ECO:0000269|PubMed:16914521}.
CC -!- INTERACTION:
CC Q6P3W7; O14640: DVL1; NbExp=4; IntAct=EBI-1046810, EBI-723489;
CC Q6P3W7; Q13467: FZD5; NbExp=4; IntAct=EBI-1046810, EBI-3913027;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000269|PubMed:15809293, ECO:0000269|PubMed:16914521}. Golgi
CC apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:16914521}.
CC Endosome membrane {ECO:0000269|PubMed:16914521}. Note=Colocalizes to
CC the trans-Golgi network (TGN) and to endosomal membranes with clathrin,
CC transferrin and plasma membrane adapter AP1 and AP3 complexes.
CC {ECO:0000269|PubMed:16914521}.
CC -!- PTM: Could autophosphorylate in presence of poly-L-lysine.
CC {ECO:0000269|PubMed:15809293}.
CC -!- DISEASE: Arthrogryposis multiplex congenita 4, neurogenic, with
CC agenesis of the corpus callosum (AMC4) [MIM:618766]: A form of
CC arthrogryposis multiplex congenita, a developmental condition
CC characterized by multiple joint contractures resulting from reduced or
CC absent fetal movements. AMC4 is an autosomal recessive, severe form
CC with onset in utero. Patients manifest little or no fetal movements,
CC significant contractures affecting the upper and lower limbs,
CC dysmorphic facial features, optic atrophy, limb fractures, profound
CC global developmental delay, seizures, and peripheral neuropathy. Many
CC patients die in early childhood. {ECO:0000269|PubMed:31960134}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91778.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14869.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB55194.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK001597; BAA91778.1; ALT_INIT; mRNA.
DR EMBL; AK024274; BAB14869.1; ALT_INIT; mRNA.
DR EMBL; AK027551; BAB55194.1; ALT_INIT; mRNA.
DR EMBL; AK292980; BAF85669.1; -; mRNA.
DR EMBL; CH471054; EAW97633.1; -; Genomic_DNA.
DR EMBL; BC012387; AAH12387.3; -; mRNA.
DR EMBL; BC063798; AAH63798.1; -; mRNA.
DR EMBL; AB037781; BAA92598.1; -; mRNA.
DR CCDS; CCDS9076.1; -.
DR RefSeq; NP_001304713.1; NM_001317784.1.
DR RefSeq; NP_001317182.1; NM_001330253.1.
DR RefSeq; NP_001317183.1; NM_001330254.1.
DR RefSeq; NP_001317185.1; NM_001330256.1.
DR RefSeq; NP_060458.3; NM_017988.5.
DR AlphaFoldDB; Q6P3W7; -.
DR SMR; Q6P3W7; -.
DR BioGRID; 120810; 139.
DR CORUM; Q6P3W7; -.
DR IntAct; Q6P3W7; 41.
DR MINT; Q6P3W7; -.
DR STRING; 9606.ENSP00000354061; -.
DR GlyGen; Q6P3W7; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; Q6P3W7; -.
DR MetOSite; Q6P3W7; -.
DR PhosphoSitePlus; Q6P3W7; -.
DR BioMuta; SCYL2; -.
DR DMDM; 74762350; -.
DR EPD; Q6P3W7; -.
DR jPOST; Q6P3W7; -.
DR MassIVE; Q6P3W7; -.
DR MaxQB; Q6P3W7; -.
DR PaxDb; Q6P3W7; -.
DR PeptideAtlas; Q6P3W7; -.
DR PRIDE; Q6P3W7; -.
DR ProteomicsDB; 66937; -.
DR Antibodypedia; 17837; 175 antibodies from 25 providers.
DR DNASU; 55681; -.
DR Ensembl; ENST00000360820.7; ENSP00000354061.2; ENSG00000136021.19.
DR GeneID; 55681; -.
DR KEGG; hsa:55681; -.
DR MANE-Select; ENST00000360820.7; ENSP00000354061.2; NM_017988.6; NP_060458.3.
DR UCSC; uc001thn.4; human.
DR CTD; 55681; -.
DR DisGeNET; 55681; -.
DR GeneCards; SCYL2; -.
DR HGNC; HGNC:19286; SCYL2.
DR HPA; ENSG00000136021; Low tissue specificity.
DR MalaCards; SCYL2; -.
DR MIM; 616365; gene.
DR MIM; 618766; phenotype.
DR neXtProt; NX_Q6P3W7; -.
DR OpenTargets; ENSG00000136021; -.
DR PharmGKB; PA134887807; -.
DR VEuPathDB; HostDB:ENSG00000136021; -.
DR eggNOG; KOG2137; Eukaryota.
DR GeneTree; ENSGT00880000138031; -.
DR InParanoid; Q6P3W7; -.
DR OrthoDB; 196028at2759; -.
DR PhylomeDB; Q6P3W7; -.
DR TreeFam; TF314178; -.
DR PathwayCommons; Q6P3W7; -.
DR SignaLink; Q6P3W7; -.
DR BioGRID-ORCS; 55681; 19 hits in 1112 CRISPR screens.
DR ChiTaRS; SCYL2; human.
DR GeneWiki; SCYL2; -.
DR GenomeRNAi; 55681; -.
DR Pharos; Q6P3W7; Tbio.
DR PRO; PR:Q6P3W7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6P3W7; protein.
DR Bgee; ENSG00000136021; Expressed in mucosa of sigmoid colon and 181 other tissues.
DR ExpressionAtlas; Q6P3W7; baseline and differential.
DR Genevisible; Q6P3W7; HS.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IDA:BHF-UCL.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IDA:BHF-UCL.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IDA:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0021860; P:pyramidal neuron development; ISS:UniProtKB.
DR GO; GO:2000286; P:receptor internalization involved in canonical Wnt signaling pathway; IDA:BHF-UCL.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasmic vesicle; Disease variant; Endosome;
KW Golgi apparatus; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..929
FT /note="SCY1-like protein 2"
FT /id="PRO_0000252446"
FT DOMAIN 32..327
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 443..479
FT /note="HEAT"
FT REGION 684..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..929
FT /note="Necessary for interaction with AP2 complex and
FT clathrin, interaction with clathrin is necessary for its
FT targeting to the TGN and endosomal membranes"
FT REGION 906..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 661..701
FT /evidence="ECO:0000255"
FT COMPBIAS 693..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 677
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 708
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 36..929
FT /note="Missing (in AMC4)"
FT /evidence="ECO:0000269|PubMed:31960134"
FT /id="VAR_083876"
FT VARIANT 357
FT /note="P -> L (in dbSNP:rs33968174)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_041368"
FT VARIANT 720
FT /note="T -> S (in dbSNP:rs763873645)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041369"
FT VARIANT 863
FT /note="Q -> H (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041370"
FT CONFLICT 139..145
FT /note="PISPDIK -> LMSGDIG (in Ref. 4; BAA92598)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="L -> S (in Ref. 1; BAB14869)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="Q -> QASNM (in Ref. 4; BAA92598)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="K -> R (in Ref. 1; BAB14869)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="F -> L (in Ref. 3; AAH12387)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="Q -> R (in Ref. 1; BAB14869)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="T -> I (in Ref. 3; AAH12387)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="T -> A (in Ref. 1; BAA91778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 929 AA; 103709 MW; 980B481BF7044628 CRC64;
MESMLNKLKS TVTKVTADVT SAVMGNPVTR EFDVGRHIAS GGNGLAWKIF NGTKKSTKQE
VAVFVFDKKL IDKYQKFEKD QIIDSLKRGV QQLTRLRHPR LLTVQHPLEE SRDCLAFCTE
PVFASLANVL GNWENLPSPI SPDIKDYKLY DVETKYGLLQ VSEGLSFLHS SVKMVHGNIT
PENIILNKSG AWKIMGFDFC VSSTNPSEQE PKFPCKEWDP NLPSLCLPNP EYLAPEYILS
VSCETASDMY SLGTVMYAVF NKGKPIFEVN KQDIYKSFSR QLDQLSRLGS SSLTNIPEEV
REHVKLLLNV TPTVRPDADQ MTKIPFFDDV GAVTLQYFDT LFQRDNLQKS QFFKGLPKVL
PKLPKRVIVQ RILPCLTSEF VNPDMVPFVL PNVLLIAEEC TKEEYVKLIL PELGPVFKQQ
EPIQILLIFL QKMDLLLTKT PPDEIKNSVL PMVYRALEAP SIQIQELCLN IIPTFANLID
YPSMKNALIP RIKNACLQTS SLAVRVNSLV CLGKILEYLD KWFVLDDILP FLQQIPSKEP
AVLMGILGIY KCTFTHKKLG ITKEQLAGKV LPHLIPLSIE NNLNLNQFNS FISVIKEMLN
RLESEHKTKL EQLHIMQEQQ KSLDIGNQMN VSEEMKVTNI GNQQIDKVFN NIGADLLTGS
ESENKEDGLQ NKHKRASLTL EEKQKLAKEQ EQAQKLKSQQ PLKPQVHTPV ATVKQTKDLT
DTLMDNMSSL TSLSVSTPKS SASSTFTSVP SMGIGMMFST PTDNTKRNLT NGLNANMGFQ
TSGFNMPVNT NQNFYSSPST VGVTKMTLGT PPTLPNFNAL SVPPAGAKQT QQRPTDMSAL
NNLFGPQKPK VSMNQLSQQK PNQWLNQFVP PQGSPTMGSS VMGTQMNVIG QSAFGMQGNP
FFNPQNFAQP PTTMTNSSSA SNDLKDLFG
