FBX4_HUMAN
ID FBX4_HUMAN Reviewed; 387 AA.
AC Q9UKT5; Q68CU8; Q86VT8; Q9UK98;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=F-box only protein 4;
GN Name=FBXO4; Synonyms=FBX4;
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] (ISOFORM 1), FUNCTION, AND INTERACTION WITH SKP1
RP AND CUL1.
RX PubMed=10531035; DOI=10.1016/s0960-9822(00)80020-2;
RA Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M.,
RA Pagano M.;
RT "Identification of a family of human F-box proteins.";
RL Curr. Biol. 9:1177-1179(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10531037; DOI=10.1016/s0960-9822(00)80021-4;
RA Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W.;
RT "A family of mammalian F-box proteins.";
RL Curr. Biol. 9:1180-1182(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 144-387.
RC TISSUE=Fetal brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP INTERACTION WITH TERF1, AND FUNCTION IN UBIQUITINATION OF TERF1.
RX PubMed=16275645; DOI=10.1074/jbc.m509855200;
RA Lee T.H., Perrem K., Harper J.W., Lu K.P., Zhou X.Z.;
RT "The F-box protein FBX4 targets PIN2/TRF1 for ubiquitin-mediated
RT degradation and regulates telomere maintenance.";
RL J. Biol. Chem. 281:759-768(2006).
RN [6]
RP FUNCTION, SUBUNIT, INTERACTION WITH SKP1, PHOSPHORYLATION AT SER-12,
RP VARIANTS ARG-8; LEU-12; SER-13; GLN-23 AND THR-76, AND CHARACTERIZATION OF
RP VARIANTS LEU-12; SER-13 AND GLN-23.
RX PubMed=18598945; DOI=10.1016/j.ccr.2008.05.017;
RA Barbash O., Zamfirova P., Lin D.I., Chen X., Yang K., Nakagawa H., Lu F.,
RA Rustgi A.K., Diehl J.A.;
RT "Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase and
RT contribute to cyclin D1 overexpression in human cancer.";
RL Cancer Cell 14:68-78(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-48, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP 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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 162-387 IN COMPLEX WITH TERF1,
RP FUNCTION, MUTAGENESIS OF CYS-341 AND ALA-345, AND SUBUNIT.
RX PubMed=20159592; DOI=10.1016/j.devcel.2010.01.007;
RA Zeng Z., Wang W., Yang Y., Chen Y., Yang X., Diehl J.A., Liu X., Lei M.;
RT "Structural basis of selective ubiquitination of TRF1 by SCFFbx4.";
RL Dev. Cell 18:214-225(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 55-387 IN COMPLEX WITH SKP1,
RP FUNCTION, AND SUBUNIT.
RX PubMed=20181953; DOI=10.1074/jbc.m110.111518;
RA Li Y., Hao B.;
RT "Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4)
RT ubiquitin ligase.";
RL J. Biol. Chem. 285:13896-13906(2010).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex that mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Promotes ubiquitination of CCND1 and its subsequent
CC proteasomal degradation. Recognizes TERF1 and promotes its
CC ubiquitination together with UBE2D1. {ECO:0000269|PubMed:10531035,
CC ECO:0000269|PubMed:16275645, ECO:0000269|PubMed:18598945,
CC ECO:0000269|PubMed:20159592, ECO:0000269|PubMed:20181953}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. Directly interacts with SKP1 and CUL1. Part of the
CC SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBXO4)
CC formed of CUL1, SKP1, RBX1 and FBXO4. Interacts with TERF1. This
CC interaction is prevented in the presence of GNL3L. Identified in a
CC complex with CRYAB and CCND1. {ECO:0000269|PubMed:10531035,
CC ECO:0000269|PubMed:16275645, ECO:0000269|PubMed:18598945,
CC ECO:0000269|PubMed:20159592, ECO:0000269|PubMed:20181953}.
CC -!- INTERACTION:
CC Q9UKT5; Q13616: CUL1; NbExp=3; IntAct=EBI-960409, EBI-359390;
CC Q9UKT5; P63208: SKP1; NbExp=16; IntAct=EBI-960409, EBI-307486;
CC Q9UKT5; Q13148: TARDBP; NbExp=3; IntAct=EBI-960409, EBI-372899;
CC Q9UKT5; Q59H18: TNNI3K; NbExp=3; IntAct=EBI-960409, EBI-704142;
CC Q9UKT5; O76024: WFS1; NbExp=3; IntAct=EBI-960409, EBI-720609;
CC Q9UKT5; P62258: YWHAE; NbExp=5; IntAct=EBI-960409, EBI-356498;
CC Q9UKT5; P62260: Ywhae; Xeno; NbExp=2; IntAct=EBI-960409, EBI-356462;
CC Q9UKT5-1; P54274: TERF1; NbExp=2; IntAct=EBI-960421, EBI-710997;
CC Q9UKT5-1; P54274-2: TERF1; NbExp=3; IntAct=EBI-960421, EBI-711018;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UKT5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UKT5-2; Sequence=VSP_012977, VSP_012978;
CC -!- PTM: Phosphorylation at Ser-12 varies during the cell cycle. It is low
CC in resting cells and high in the S phase and the G2/M phase of the cell
CC cycle. Phosphorylation is decreased during late G1 phase (By
CC similarity). Phosphorylation at Ser-12 promotes homodimerization and is
CC necessary for optimal ubiquitin ligase activity towards CCND1.
CC {ECO:0000250, ECO:0000269|PubMed:18598945}.
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DR EMBL; AF176703; AAF03703.1; -; mRNA.
DR EMBL; BC048098; AAH48098.1; -; mRNA.
DR EMBL; CR749719; CAH18486.1; -; mRNA.
DR EMBL; AF129534; AAF04468.1; -; mRNA.
DR CCDS; CCDS3938.1; -. [Q9UKT5-1]
DR CCDS; CCDS3939.1; -. [Q9UKT5-2]
DR RefSeq; NP_036308.1; NM_012176.2. [Q9UKT5-1]
DR RefSeq; NP_277019.1; NM_033484.2. [Q9UKT5-2]
DR PDB; 3L2O; X-ray; 2.80 A; B=55-387.
DR PDB; 3L82; X-ray; 2.40 A; B=162-387.
DR PDBsum; 3L2O; -.
DR PDBsum; 3L82; -.
DR AlphaFoldDB; Q9UKT5; -.
DR SMR; Q9UKT5; -.
DR BioGRID; 117656; 32.
DR IntAct; Q9UKT5; 15.
DR MINT; Q9UKT5; -.
DR STRING; 9606.ENSP00000281623; -.
DR iPTMnet; Q9UKT5; -.
DR PhosphoSitePlus; Q9UKT5; -.
DR BioMuta; FBXO4; -.
DR DMDM; 60416426; -.
DR EPD; Q9UKT5; -.
DR jPOST; Q9UKT5; -.
DR MassIVE; Q9UKT5; -.
DR MaxQB; Q9UKT5; -.
DR PaxDb; Q9UKT5; -.
DR PeptideAtlas; Q9UKT5; -.
DR PRIDE; Q9UKT5; -.
DR ProteomicsDB; 84849; -. [Q9UKT5-1]
DR ProteomicsDB; 84850; -. [Q9UKT5-2]
DR Antibodypedia; 23214; 289 antibodies from 30 providers.
DR DNASU; 26272; -.
DR Ensembl; ENST00000281623.8; ENSP00000281623.3; ENSG00000151876.13. [Q9UKT5-1]
DR Ensembl; ENST00000296812.6; ENSP00000296812.2; ENSG00000151876.13. [Q9UKT5-2]
DR GeneID; 26272; -.
DR KEGG; hsa:26272; -.
DR MANE-Select; ENST00000281623.8; ENSP00000281623.3; NM_012176.3; NP_036308.1.
DR UCSC; uc003jmp.4; human. [Q9UKT5-1]
DR CTD; 26272; -.
DR DisGeNET; 26272; -.
DR GeneCards; FBXO4; -.
DR HGNC; HGNC:13583; FBXO4.
DR HPA; ENSG00000151876; Low tissue specificity.
DR MIM; 609090; gene.
DR neXtProt; NX_Q9UKT5; -.
DR OpenTargets; ENSG00000151876; -.
DR PharmGKB; PA28044; -.
DR VEuPathDB; HostDB:ENSG00000151876; -.
DR eggNOG; ENOG502QUXD; Eukaryota.
DR GeneTree; ENSGT00390000014416; -.
DR HOGENOM; CLU_064324_0_0_1; -.
DR InParanoid; Q9UKT5; -.
DR OMA; RQIHGIG; -.
DR PhylomeDB; Q9UKT5; -.
DR TreeFam; TF331105; -.
DR PathwayCommons; Q9UKT5; -.
DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9UKT5; -.
DR SIGNOR; Q9UKT5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 26272; 7 hits in 1115 CRISPR screens.
DR ChiTaRS; FBXO4; human.
DR EvolutionaryTrace; Q9UKT5; -.
DR GeneWiki; FBXO4; -.
DR GenomeRNAi; 26272; -.
DR Pharos; Q9UKT5; Tbio.
DR PRO; PR:Q9UKT5; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UKT5; protein.
DR Bgee; ENSG00000151876; Expressed in calcaneal tendon and 141 other tissues.
DR ExpressionAtlas; Q9UKT5; baseline and differential.
DR Genevisible; Q9UKT5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0019725; P:cellular homeostasis; IEA:Ensembl.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0035726; P:common myeloid progenitor cell proliferation; IEA:Ensembl.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:1902916; P:positive regulation of protein polyubiquitination; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IDA:BHF-UCL.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR DisProt; DP01884; -.
DR Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID00630; -.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR039588; FBXO4.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR16008; PTHR16008; 1.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..387
FT /note="F-box only protein 4"
FT /id="PRO_0000119879"
FT DOMAIN 56..102
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18598945,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 300..307
FT /note="RHEWQDEF -> SKYSYVHF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10531037"
FT /id="VSP_012977"
FT VAR_SEQ 308..387
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10531037"
FT /id="VSP_012978"
FT VARIANT 8
FT /note="S -> R (in esophagus cancer samples;
FT dbSNP:rs2231917)"
FT /evidence="ECO:0000269|PubMed:18598945"
FT /id="VAR_063500"
FT VARIANT 12
FT /note="S -> L (in esophagus cancer sample; impairs
FT homodimerization and reduces ubiquitin ligase activity)"
FT /evidence="ECO:0000269|PubMed:18598945"
FT /id="VAR_063501"
FT VARIANT 13
FT /note="P -> S (in esophagus cancer sample)"
FT /evidence="ECO:0000269|PubMed:18598945"
FT /id="VAR_063502"
FT VARIANT 23
FT /note="L -> Q (in esophagus cancer samples)"
FT /evidence="ECO:0000269|PubMed:18598945"
FT /id="VAR_063503"
FT VARIANT 76
FT /note="P -> T (in esophagus cancer samples; impairs
FT interaction with SKP1)"
FT /evidence="ECO:0000269|PubMed:18598945"
FT /id="VAR_063504"
FT MUTAGEN 12
FT /note="S->A: Reduces homodimerization. Reduces
FT ubiquitination of CCND1."
FT MUTAGEN 12
FT /note="S->E: No effect on homodimerization."
FT MUTAGEN 13
FT /note="P->A: Reduces homodimerization."
FT MUTAGEN 23
FT /note="L->A: Abolishes homodimerization."
FT MUTAGEN 341
FT /note="C->W: Abolishes interaction with TERF1."
FT /evidence="ECO:0000269|PubMed:20159592"
FT MUTAGEN 345
FT /note="A->R: Abolishes interaction with TERF1."
FT /evidence="ECO:0000269|PubMed:20159592"
FT CONFLICT 41
FT /note="E -> D (in Ref. 1; AAF04468)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="D -> N (in Ref. 1; AAF04468)"
FT /evidence="ECO:0000305"
FT CONFLICT 120..122
FT /note="DLE -> YLQ (in Ref. 1; AAF04468)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="T -> S (in Ref. 1; AAF04468)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="R -> L (in Ref. 1; AAF04468)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="Q -> P (in Ref. 1; AAF04468)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="M -> L (in Ref. 1; AAF04468)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="G -> R (in Ref. 1; AAF04468)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="E -> Q (in Ref. 1; AAF04468)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="M -> L (in Ref. 1; AAF04468)"
FT /evidence="ECO:0000305"
FT CONFLICT 268..269
FT /note="QQ -> RP (in Ref. 1; AAF04468)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="V -> L (in Ref. 1; AAF04468)"
FT /evidence="ECO:0000305"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:3L2O"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:3L2O"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:3L2O"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:3L2O"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:3L2O"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:3L2O"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3L2O"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:3L2O"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:3L2O"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:3L82"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:3L82"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3L82"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:3L82"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:3L82"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3L2O"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3L82"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3L2O"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:3L82"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:3L82"
FT HELIX 279..285
FT /evidence="ECO:0007829|PDB:3L82"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:3L82"
FT HELIX 303..313
FT /evidence="ECO:0007829|PDB:3L82"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:3L2O"
FT STRAND 325..333
FT /evidence="ECO:0007829|PDB:3L82"
FT HELIX 341..347
FT /evidence="ECO:0007829|PDB:3L82"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:3L82"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:3L82"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:3L82"
FT HELIX 370..377
FT /evidence="ECO:0007829|PDB:3L82"
FT TURN 378..383
FT /evidence="ECO:0007829|PDB:3L82"
SQ SEQUENCE 387 AA; 44136 MW; BD5E8DD14B9733E9 CRC64;
MAGSEPRSGT NSPPPPFSDW GRLEAAILSG WKTFWQSVSK ERVARTTSRE EVDEAASTLT
RLPIDVQLYI LSFLSPHDLC QLGSTNHYWN ETVRDPILWR YFLLRDLPSW SSVDWKSLPD
LEILKKPISE VTDGAFFDYM AVYRMCCPYT RRASKSSRPM YGAVTSFLHS LIIQNEPRFA
MFGPGLEELN TSLVLSLMSS EELCPTAGLP QRQIDGIGSG VNFQLNNQHK FNILILYSTT
RKERDRAREE HTSAVNKMFS RHNEGDDQQG SRYSVIPQIQ KVCEVVDGFI YVANAEAHKR
HEWQDEFSHI MAMTDPAFGS SGRPLLVLSC ISQGDVKRMP CFYLAHELHL NLLNHPWLVQ
DTEAETLTGF LNGIEWILEE VESKRAR
