FBX38_HUMAN
ID FBX38_HUMAN Reviewed; 1188 AA.
AC Q6PIJ6; Q6PK72; Q7Z2U0; Q86VN3; Q9BXY6; Q9H837; Q9HC40;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=F-box only protein 38 {ECO:0000305};
GN Name=FBXO38 {ECO:0000312|HGNC:HGNC:28844}; ORFNames=SP329;
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] (ISOFORMS 2 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 421-1188 (ISOFORM 1), AND VARIANT PRO-592.
RC TISSUE=Muscle, PNS, Testis, and Uterus;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 299-1188 (ISOFORM 2), AND VARIANT PRO-592.
RA Mao Y., Xie Y., Zhou Z., Zhao W., Zhao S., Wang W., Huang Y., Wang S.,
RA Tang R., Chen X., Wu C.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-692 (ISOFORMS 1/2).
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 MRNA] OF 639-1188 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-740, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [9]
RP FUNCTION, PATHWAY, INTERACTION WITH PDCD1, AND INDUCTION.
RX PubMed=30487606; DOI=10.1038/s41586-018-0756-0;
RA Meng X., Liu X., Guo X., Jiang S., Chen T., Hu Z., Liu H., Bai Y., Xue M.,
RA Hu R., Sun S.C., Liu X., Zhou P., Huang X., Wei L., Yang W., Xu C.;
RT "FBXO38 mediates PD-1 ubiquitination and regulates anti-tumour immunity of
RT T cells.";
RL Nature 564:130-135(2018).
RN [10]
RP VARIANT HMN2D ARG-206, AND CHARACTERIZATION OF VARIANT HMN2D ARG-206.
RX PubMed=24207122; DOI=10.1016/j.ajhg.2013.10.006;
RA Sumner C.J., d'Ydewalle C., Wooley J., Fawcett K.A., Hernandez D.,
RA Gardiner A.R., Kalmar B., Baloh R.H., Gonzalez M., Zuchner S.,
RA Stanescu H.C., Kleta R., Mankodi A., Cornblath D.R., Boylan K.B.,
RA Reilly M.M., Greensmith L., Singleton A.B., Harms M.B., Rossor A.M.,
RA Houlden H.;
RT "A dominant mutation in FBXO38 causes distal spinal muscular atrophy with
RT calf predominance.";
RL Am. J. Hum. Genet. 93:976-983(2013).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of PDCD1/PD-1,
CC thereby regulating T-cells-mediated immunity (PubMed:30487606).
CC Required for anti-tumor activity of T-cells by promoting the
CC degradation of PDCD1/PD-1; the PDCD1-mediated inhibitory pathway being
CC exploited by tumors to attenuate anti-tumor immunity and facilitate
CC tumor survival (PubMed:30487606). May indirectly stimulate the activity
CC of transcription factor KLF7, a regulator of neuronal differentiation,
CC without promoting KLF7 ubiquitination (By similarity).
CC {ECO:0000250|UniProtKB:Q8BMI0, ECO:0000269|PubMed:30487606}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:30487606}.
CC -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase
CC complex SCF(FBXO38) composed of CUL1, SKP1, RBX1 and FBXO38 (Probable).
CC Interacts with KLF7 (By similarity). Interacts with PDCD1/PD-1
CC (PubMed:30487606). {ECO:0000250|UniProtKB:Q8BMI0,
CC ECO:0000269|PubMed:30487606, ECO:0000305|PubMed:30487606}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8BMI0}. Nucleus {ECO:0000250|UniProtKB:Q8BMI0}.
CC Note=Accumulates predominantly in the cytosol. Exported from the
CC nucleus in a XPO1/CRM1-dependent manner.
CC {ECO:0000250|UniProtKB:Q8BMI0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6PIJ6-1; Sequence=Displayed;
CC Name=2; Synonyms=a;
CC IsoId=Q6PIJ6-2; Sequence=VSP_011449;
CC Name=3;
CC IsoId=Q6PIJ6-3; Sequence=VSP_011448, VSP_011449;
CC -!- INDUCTION: Up-regulated by IL2 (PubMed:30487606). Down-regulated in
CC tumor-infiltrating T-cells (PubMed:30487606).
CC {ECO:0000269|PubMed:30487606}.
CC -!- DISEASE: Neuronopathy, distal hereditary motor, 2D (HMN2D)
CC [MIM:615575]: A disorder characterized by onset of slowly progressive
CC distal lower limb weakness and atrophy between the second and fourth
CC decades of life. Weakness usually begins in the calf muscles and later
CC involves more proximal muscles. The severity is variable, and some
CC patients have difficulty walking or running. Most also have upper limb
CC involvement, particularly of the triceps and intrinsic hand muscles.
CC Some patients may lose independent ambulation later in the disease
CC course. Sensory impairment is typically not present, and cognition and
CC bulbar function are normal. {ECO:0000269|PubMed:24207122}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG17983.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH56147.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK34945.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14783.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC005849; AAH05849.1; -; mRNA.
DR EMBL; BC005873; AAH05873.1; -; mRNA.
DR EMBL; BC033454; AAH33454.1; -; mRNA.
DR EMBL; BC050424; AAH50424.1; -; mRNA.
DR EMBL; BC056147; AAH56147.1; ALT_INIT; mRNA.
DR EMBL; AF251055; AAK34945.1; ALT_INIT; mRNA.
DR EMBL; AK024024; BAB14783.1; ALT_FRAME; mRNA.
DR EMBL; AF177339; AAG17983.1; ALT_FRAME; mRNA.
DR CCDS; CCDS4290.1; -. [Q6PIJ6-1]
DR CCDS; CCDS43384.1; -. [Q6PIJ6-2]
DR CCDS; CCDS64285.1; -. [Q6PIJ6-3]
DR RefSeq; NP_001258652.1; NM_001271723.1. [Q6PIJ6-3]
DR RefSeq; NP_110420.3; NM_030793.4. [Q6PIJ6-2]
DR RefSeq; XP_005268570.1; XM_005268513.1.
DR AlphaFoldDB; Q6PIJ6; -.
DR BioGRID; 123513; 141.
DR IntAct; Q6PIJ6; 18.
DR MINT; Q6PIJ6; -.
DR STRING; 9606.ENSP00000377895; -.
DR iPTMnet; Q6PIJ6; -.
DR PhosphoSitePlus; Q6PIJ6; -.
DR BioMuta; FBXO38; -.
DR DMDM; 116241362; -.
DR EPD; Q6PIJ6; -.
DR jPOST; Q6PIJ6; -.
DR MassIVE; Q6PIJ6; -.
DR MaxQB; Q6PIJ6; -.
DR PaxDb; Q6PIJ6; -.
DR PeptideAtlas; Q6PIJ6; -.
DR PRIDE; Q6PIJ6; -.
DR ProteomicsDB; 67162; -. [Q6PIJ6-1]
DR ProteomicsDB; 67163; -. [Q6PIJ6-2]
DR ProteomicsDB; 67164; -. [Q6PIJ6-3]
DR Antibodypedia; 27733; 73 antibodies from 15 providers.
DR DNASU; 81545; -.
DR Ensembl; ENST00000296701.10; ENSP00000296701.6; ENSG00000145868.17. [Q6PIJ6-3]
DR Ensembl; ENST00000340253.10; ENSP00000342023.6; ENSG00000145868.17. [Q6PIJ6-1]
DR Ensembl; ENST00000394370.7; ENSP00000377895.3; ENSG00000145868.17. [Q6PIJ6-2]
DR Ensembl; ENST00000513826.1; ENSP00000426410.1; ENSG00000145868.17. [Q6PIJ6-3]
DR GeneID; 81545; -.
DR KEGG; hsa:81545; -.
DR MANE-Select; ENST00000340253.10; ENSP00000342023.6; NM_205836.3; NP_995308.1.
DR UCSC; uc003lpg.3; human. [Q6PIJ6-1]
DR CTD; 81545; -.
DR DisGeNET; 81545; -.
DR GeneCards; FBXO38; -.
DR HGNC; HGNC:28844; FBXO38.
DR HPA; ENSG00000145868; Low tissue specificity.
DR MalaCards; FBXO38; -.
DR MIM; 608533; gene.
DR MIM; 615575; phenotype.
DR neXtProt; NX_Q6PIJ6; -.
DR OpenTargets; ENSG00000145868; -.
DR Orphanet; 139525; Distal hereditary motor neuropathy type 2.
DR PharmGKB; PA134929999; -.
DR VEuPathDB; HostDB:ENSG00000145868; -.
DR eggNOG; ENOG502QSUC; Eukaryota.
DR GeneTree; ENSGT00390000013163; -.
DR HOGENOM; CLU_010774_0_0_1; -.
DR InParanoid; Q6PIJ6; -.
DR OMA; CKEEYPR; -.
DR OrthoDB; 63661at2759; -.
DR PhylomeDB; Q6PIJ6; -.
DR TreeFam; TF331125; -.
DR PathwayCommons; Q6PIJ6; -.
DR SignaLink; Q6PIJ6; -.
DR SIGNOR; Q6PIJ6; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 81545; 9 hits in 1121 CRISPR screens.
DR ChiTaRS; FBXO38; human.
DR GenomeRNAi; 81545; -.
DR Pharos; Q6PIJ6; Tbio.
DR PRO; PR:Q6PIJ6; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q6PIJ6; protein.
DR Bgee; ENSG00000145868; Expressed in calcaneal tendon and 192 other tissues.
DR Genevisible; Q6PIJ6; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; TAS:UniProtKB.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0002842; P:positive regulation of T cell mediated immune response to tumor cell; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR042354; FBX38.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR14753; PTHR14753; 1.
DR Pfam; PF00646; F-box; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Cytoplasm; Disease variant;
KW Immunity; Neurodegeneration; Neuropathy; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..1188
FT /note="F-box only protein 38"
FT /id="PRO_0000119933"
FT DOMAIN 30..75
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REGION 59..119
FT /note="Interaction with KLF7"
FT /evidence="ECO:0000250|UniProtKB:Q8BMI0"
FT REGION 487..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 194..201
FT /note="Nuclear export signal 1"
FT /evidence="ECO:0000250|UniProtKB:Q8BMI0"
FT MOTIF 307..316
FT /note="Nuclear export signal 2"
FT /evidence="ECO:0000250|UniProtKB:Q8BMI0"
FT MOTIF 451..460
FT /note="Nuclear export signal 3"
FT /evidence="ECO:0000250|UniProtKB:Q8BMI0"
FT MOTIF 896..899
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q8BMI0"
FT COMPBIAS 487..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 591
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMI0"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMI0"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMI0"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMI0"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 640..809
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011448"
FT VAR_SEQ 810..884
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_011449"
FT VARIANT 206
FT /note="C -> R (in HMN2D; unable to promote activation of
FT KLF7 target genes including CDKN1A and L1CAM in both
FT cultured cells and patient-derived cells;
FT dbSNP:rs398122838)"
FT /evidence="ECO:0000269|PubMed:24207122"
FT /id="VAR_070923"
FT VARIANT 592
FT /note="S -> P (in dbSNP:rs10043775)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_028099"
FT VARIANT 894
FT /note="A -> T (in dbSNP:rs11949133)"
FT /id="VAR_049049"
FT CONFLICT 137
FT /note="A -> S (in Ref. 1; AAH33454)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="L -> S (in Ref. 3; BAB14783)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="I -> N (in Ref. 3; BAB14783)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="T -> A (in Ref. 1; AAH33454)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="D -> E (in Ref. 1; AAH33454)"
FT /evidence="ECO:0000305"
FT CONFLICT 775..776
FT /note="RC -> DA (in Ref. 4; AAG17983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1188 AA; 133944 MW; 863A0F7333E95A0C CRC64;
MGPRKKSVKT CIMNNEIPEE MTADETKDYM NQLSHEVLCH IFRYLPLQDI MCMECLSRKL
KEAVTLYLRV VRVVDLCAGR WWEYMPSGFT DASFLTLLKK MPDVEQLYGL HPRYLERRRV
RGHEAFSIPG VLEALQACPN LVGVETSHLE LVESIWTYMP HVHILGKFRN RNGAFPIPPE
NKLKIPIGAK IQTLHLVGVN VPEIPCIPML RHLYMKWVRL TKPQPFKDFL CISLRTFVMR
NCAGPTNSLK YVPLVTGLAS ARNLEHLEMV RVPFLGGLIQ HVVEDSWRSG GFRNLHTIVL
GACKNALEVD LGYLIITAAR RLHEVRIQPS LTKDGVFSAL KMAELEFPQF ETLHLGYVDE
FLLQSRMANA DLVKYGLADV VENPGIITDI GMKAVNEVFS CIKYLAIYNC PHLHNPYNWI
SDHSRWTRLV DINLVRCHAL KLDSFGQFIE LLPSLEFISL DQMFREPPKG CARVGLSAGT
GIGVSSALVS NQNSNNDDNN AQNNNANIHD NNHHHPDDSD EENDFRQDLQ PGEQQFAADA
LNEMEDIVQE DGEVVAESGN NTPAHSQAII PVDVDEEQAG PSGLQRVVKP TSITVHDSES
DDEEDSLELQ EVWIPKNGTR RYSEREEKTG ESVQSRELSV SGKGKTPLRK RYNSHQMGQS
KQFPLEESSC EKGCQVTSEQ IKADMKAARD IPEKKKNKDV YPSCSSTTAS TVGNSSSHNT
ASQSPDFVRT VNSGGSSEPS PTEVDVSRQC ACSPGGSEDS EAMEEGDAES SVCPRCCCHR
PQESQRRTSR CSDEERPSTS RACVVNGPDG TRSAFSFRTL PQGGSSGPAH DERTNGSGSG
ATGEDRRGSS QPESCDVQSN EDYPRRPLTR ARSRLSHVLL VSESEVAKTK PRHAMKRKRT
ADKSTSTSDP VIEDDHVQVL VLKSKNLVGV TMTNCGITDL VLKDCPKMMF IHATRCRVLK
HLKVENAPIV NRFDYAQCKK LNMDQVLDQI LRMPPERNRI IYLRPMQQVD TLTLEQKLFS
GPYPYHICII HEFSNPPNVR NKVRIRSWMD TIANINQELI KYEFFPEATR SEEDLKKYPK
YPWGREIYTL EGVVDGAPYS MISDFPWLRS LRAAEPNSFA RYDFEDDEES TIYAPRRKGQ
LSADICMETI GEEISEMRQM KKGVFQRVVA IFIHYCDVNG EPVEDDYI
