CUL1_DROME
ID CUL1_DROME Reviewed; 774 AA.
AC Q24311; A4UZ78; Q0E9G0; Q9V312;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cullin homolog 1;
DE AltName: Full=Lin-19 homolog protein;
GN Name=Cul1; Synonyms=cul-1, lin19; ORFNames=CG1877;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Oregon-R; TISSUE=Larval brain;
RA Filippov V.A., Filippova M.A., Sehnal F.;
RT "Homolog of C.elegans lin-19 gene.";
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Dealy M.J., Heriche J.K., Nguyen K.V.T., Lo J., Gstaiger M., Krek W.,
RA Ang D., Bier E., Elson D., Arbeit J., Kipreos E.T., O'Farrell P.H.,
RA Johnson R.S.;
RT "Cul-1 limits cyclin E level in mouse and cyclin E function in
RT Drosophila.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH ROC1A AND SLMB.
RX PubMed=11500045; DOI=10.1006/bbrc.2001.5394;
RA Bocca S.N., Muzzopappa M., Silberstein S., Wappner P.;
RT "Occurrence of a putative SCF ubiquitin ligase complex in Drosophila.";
RL Biochem. Biophys. Res. Commun. 286:357-364(2001).
RN [7]
RP NEDDYLATION, AND DENEDDYLATION BY THE CSN COMPLEX.
RX PubMed=12183637; DOI=10.1126/science.1075901;
RA Cope G.A., Suh G.S.B., Aravind L., Schwarz S.E., Zipursky S.L.,
RA Koonin E.V., Deshaies R.J.;
RT "Role of predicted metalloprotease motif of Jab1/Csn5 in cleavage of Nedd8
RT from Cul1.";
RL Science 298:608-611(2002).
RN [8]
RP NEDDYLATION.
RX PubMed=18493598; DOI=10.1371/journal.pone.0002239;
RA Rencus-Lazar S., Amir Y., Wu J., Chien C.T., Chamovitz D.A., Segal D.;
RT "The proto-oncogene Int6 is essential for neddylation of Cul1 and Cul3 in
RT Drosophila.";
RL PLoS ONE 3:E2239-E2239(2008).
RN [9]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH SKPA AND NTC, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20392747; DOI=10.1242/dev.050088;
RA Bader M., Arama E., Steller H.;
RT "A novel F-box protein is required for caspase activation during cellular
RT remodeling in Drosophila.";
RL Development 137:1679-1688(2010).
RN [10]
RP INTERACTION WITH FSN.
RX PubMed=20123973; DOI=10.1128/mcb.01100-09;
RA Kugler J.M., Woo J.S., Oh B.H., Lasko P.;
RT "Regulation of Drosophila vasa in vivo through paralogous cullin-RING E3
RT ligase specificity receptors.";
RL Mol. Cell. Biol. 30:1769-1782(2010).
RN [11]
RP FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND IDENTIFICATION IN
RP SCF COMPLEX.
RX PubMed=24068890; DOI=10.1371/journal.pbio.1001657;
RA Wong J.J., Li S., Lim E.K., Wang Y., Wang C., Zhang H., Kirilly D., Wu C.,
RA Liou Y.C., Wang H., Yu F.;
RT "A Cullin1-based SCF E3 ubiquitin ligase targets the InR/PI3K/TOR pathway
RT to regulate neuronal pruning.";
RL PLoS Biol. 11:E1001657-E1001657(2013).
RN [12]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=24413555; DOI=10.1002/embr.201337966;
RA Li S., Wang C., Sandanaraj E., Aw S.S., Koe C.T., Wong J.J., Yu F.,
RA Ang B.T., Tang C., Wang H.;
RT "The SCFSlimb E3 ligase complex regulates asymmetric division to inhibit
RT neuroblast overgrowth.";
RL EMBO Rep. 15:165-174(2014).
RN [13]
RP FUNCTION, AND INTERACTION WITH CAD99C AND SANS.
RX PubMed=27331610; DOI=10.7554/elife.15258;
RA Li T., Giagtzoglou N., Eberl D.F., Jaiswal S.N., Cai T., Godt D.,
RA Groves A.K., Bellen H.J.;
RT "The E3 ligase Ubr3 regulates Usher syndrome and MYH9 disorder proteins in
RT the auditory organs of Drosophila and mammals.";
RL Elife 5:E15258-E15258(2016).
RN [14]
RP INTERACTION WITH DLISH.
RX PubMed=27692068; DOI=10.7554/elife.16624;
RA Zhang Y., Wang X., Matakatsu H., Fehon R., Blair S.S.;
RT "The novel SH3 domain protein Dlish/CG10933 mediates fat signaling in
RT Drosophila by binding and regulating Dachs.";
RL Elife 5:E16624-E16624(2016).
RN [15]
RP ERRATUM OF PUBMED:27692068.
RX PubMed=27824307; DOI=10.7554/elife.22672;
RA Zhang Y., Wang X., Matakatsu H., Fehon R., Blair S.S.;
RL Elife 5:E22672-E22672(2016).
CC -!- FUNCTION: Core component of multiple SCF (SKP1-CUL1-F-box protein) E3
CC ubiquitin-protein ligase complexes which mediate the ubiquitination of
CC proteins involved in cell cycle progression, signal transduction and
CC transcription. In the SCF complex, serves as a rigid scaffold that
CC organizes the SKP1-F-box protein and RBX1 subunits. May contribute to
CC catalysis through positioning of the substrate and the ubiquitin-
CC conjugating enzyme. During early metamorphosis, part of the SCF-slmb
CC complex that negatively regulates the InR/PI3K/TOR pathway to activate
CC the pruning of unnecessary larval ddaC dendrites and mushroom body
CC axons (PubMed:24068890). The SCF-slmb complex also regulates
CC asymmetrical division of neuroblasts and inhibits ectopic neuroblast
CC formation partly through SAK and Akt1 (PubMed:24413555). Also part of
CC an SCF complex required for caspase activation during sperm
CC differentiation (PubMed:20392747). Necessary for auditory transduction:
CC plays a role in Johnston's organ organization by acting in the
CC regulation of zip and ck function in scolopidial apical attachment
CC (PubMed:27331610). May function by acting in a Ubr3-mediated pathway
CC that negatively regulates the ubiquitination of zip, consequently
CC affecting its interaction with ck (PubMed:27331610).
CC {ECO:0000269|PubMed:20392747, ECO:0000269|PubMed:24068890,
CC ECO:0000269|PubMed:24413555, ECO:0000269|PubMed:27331610}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of SCF E3 ubiquitin-protein ligase complexes
CC consisting of Skpa, Cul1, Roc1a and an F-box protein. In larval
CC neuroblast self renewal and asymmetric division, as well as ddaC
CC dendrite and mushroom body axon pruning, the complex contains the F-box
CC protein slmb (SCF-slmb) (PubMed:24068890, PubMed:24413555). In caspase
CC activation during sperm differentiation, the complex contains the F-box
CC protein ntc (PubMed:20392747). Interacts directly with Roc1a
CC (PubMed:11500045). Interacts with Fsn (PubMed:20123973). Interacts with
CC Dlish (PubMed:27692068). Interacts with Cad99C (via the cytoplasmic
CC domain) (PubMed:27331610). Interacts with Sans (PubMed:27331610).
CC {ECO:0000269|PubMed:11500045, ECO:0000269|PubMed:20123973,
CC ECO:0000269|PubMed:20392747, ECO:0000269|PubMed:24068890,
CC ECO:0000269|PubMed:24413555, ECO:0000269|PubMed:27331610,
CC ECO:0000269|PubMed:27692068}.
CC -!- INTERACTION:
CC Q24311; P91666: Rca1; NbExp=2; IntAct=EBI-136038, EBI-7085629;
CC Q24311; O77430: SkpA; NbExp=2; IntAct=EBI-136038, EBI-180180;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20392747}. Note=In
CC the spermatid, colocalizes with ntc at the actin-based
CC individualization complex and the cystic bulge.
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:20392747}.
CC -!- PTM: Neddylated (PubMed:12183637, PubMed:18493598). Deneddylated via
CC its interaction with the COP9 signalosome (CSN) complex
CC (PubMed:12183637). {ECO:0000269|PubMed:12183637,
CC ECO:0000269|PubMed:18493598}.
CC -!- DISRUPTION PHENOTYPE: Severe dendrite pruning defects in ddaC neurons
CC at 16 hours after puparium formation (APF) and axon pruning defects in
CC mushroom body gamma neurons at 24 hours APF. RNAi-mediated knockdown
CC results in a significant increase in Akt1 protein levels and activity
CC in ddaC somas (PubMed:24068890). In the larval brain there is a large
CC increase in the number of neuroblasts, 40% of which show a spindle
CC misorientation at metaphase (PubMed:24413555). RNAi-mediated knockdown
CC results in apical detachment of scolopidial cells in Johnston's organ
CC (PubMed:27331610). {ECO:0000269|PubMed:24068890,
CC ECO:0000269|PubMed:24413555, ECO:0000269|PubMed:27331610}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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; L41642; AAA85085.1; -; mRNA.
DR EMBL; AF136343; AAD33676.1; -; mRNA.
DR EMBL; AE013599; AAF59174.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68871.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68872.1; -; Genomic_DNA.
DR EMBL; BT010290; AAQ23608.1; -; mRNA.
DR RefSeq; NP_523655.1; NM_078931.4.
DR RefSeq; NP_724621.1; NM_165569.2.
DR RefSeq; NP_724622.1; NM_165570.3.
DR RefSeq; NP_724623.1; NM_165571.2.
DR AlphaFoldDB; Q24311; -.
DR SMR; Q24311; -.
DR BioGRID; 61606; 40.
DR DIP; DIP-19461N; -.
DR IntAct; Q24311; 8.
DR MINT; Q24311; -.
DR STRING; 7227.FBpp0087921; -.
DR PaxDb; Q24311; -.
DR PRIDE; Q24311; -.
DR DNASU; 35742; -.
DR EnsemblMetazoa; FBtr0088845; FBpp0087921; FBgn0015509.
DR EnsemblMetazoa; FBtr0088846; FBpp0087922; FBgn0015509.
DR EnsemblMetazoa; FBtr0088847; FBpp0087923; FBgn0015509.
DR EnsemblMetazoa; FBtr0088848; FBpp0087924; FBgn0015509.
DR GeneID; 35742; -.
DR KEGG; dme:Dmel_CG1877; -.
DR UCSC; CG1877-RA; d. melanogaster.
DR CTD; 8454; -.
DR FlyBase; FBgn0015509; Cul1.
DR VEuPathDB; VectorBase:FBgn0015509; -.
DR eggNOG; KOG2166; Eukaryota.
DR GeneTree; ENSGT00940000154774; -.
DR HOGENOM; CLU_004747_6_1_1; -.
DR InParanoid; Q24311; -.
DR OMA; GVYTAVH; -.
DR OrthoDB; 1040292at2759; -.
DR PhylomeDB; Q24311; -.
DR Reactome; R-DME-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-DME-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
DR Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
DR Reactome; R-DME-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-DME-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-DME-68949; Orc1 removal from chromatin.
DR Reactome; R-DME-69231; Cyclin D associated events in G1.
DR Reactome; R-DME-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-DME-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-DME-8951664; Neddylation.
DR Reactome; R-DME-9020702; Interleukin-1 signaling.
DR Reactome; R-DME-917937; Iron uptake and transport.
DR Reactome; R-DME-9708530; Regulation of BACH1 activity.
DR Reactome; R-DME-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q24311; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 35742; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 35742; -.
DR PRO; PR:Q24311; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0015509; Expressed in egg chamber and 38 other tissues.
DR ExpressionAtlas; Q24311; baseline and differential.
DR Genevisible; Q24311; DM.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:FlyBase.
DR GO; GO:0060090; F:molecular adaptor activity; IPI:FlyBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
DR GO; GO:0002785; P:negative regulation of antimicrobial peptide production; IMP:FlyBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:FlyBase.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IGI:FlyBase.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IGI:FlyBase.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IDA:FlyBase.
DR GO; GO:1904801; P:positive regulation of neuron remodeling; IMP:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:FlyBase.
DR GO; GO:1905088; P:positive regulation of synaptonemal complex assembly; IMP:FlyBase.
DR GO; GO:0030163; P:protein catabolic process; IMP:FlyBase.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:FlyBase.
DR GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; PTHR11932; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..774
FT /note="Cullin homolog 1"
FT /id="PRO_0000119786"
FT CROSSLNK 718
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000250|UniProtKB:Q13616"
FT CONFLICT 266
FT /note="Missing (in Ref. 1; AAA85085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 774 AA; 89511 MW; 1AF0D035DE85363C CRC64;
MNRSGNSQTT QKLVNLDDIW SELVEGIMQV FEHEKSLTRS QYMRFYTHVY DYCTSVSAAP
SGRSSGKTGG AQLVGKKLYD RLEQFLKSYL SELLTKFKAI SGEEVLLSRY TKQWKSYQFS
STVLDGICNY LNRNWVKREC EEGQKGIYKI YRLALVAWKG HLFQVLNEPV TKAVLKSIEE
ERQGKLINRS LVRDVIECYV ELSFNEEDTD AEQQKLSVYK QNFENKFIAD TSAFYEKESD
AFLSTNTVTE YLKHVENRLE EETQRVRGFN SKNGLSYLHE TTADVLKSTC EEVLIEKHLK
IFHTEFQNLL NADRNDDLKR MYSLVALSSK NLTDLKSILE NHILHQGTEA IAKCCTTDAA
NDPKTYVQTI LDVHKKYNAL VLTAFNNDNG FVAALDKACG KFINSNVVTI ANSASKSPEL
LAKYCDLLLK KSSKNPEDKE LEDNLNQVMV VFKYIEDKDV FQKYYSKMLA KRLVNHTSAS
DDAEAMMISK LKQTCGYEYT VKLQRMFQDI GVSKDLNSYF KQYLAEKNLT MEIDFGIEVL
SSGSWPFQLS NNFLLPSELE RSVRQFNEFY AARHSGRKLN WLYQMCKGEL IMNVNRNNSS
TYTLQASTFQ MSVLLQFNDQ LSFTVQQLQD NTQTQQENLI QVLQILLKAK VLTSSDNENS
LTPESTVELF LDYKNKKRRI NINQPLKTEL KVEQETVHKH IEEDRKLLIQ AAIVRIMKMR
KRLNHTNLIS EVLNQLSTRF KPKVPVIKKC IDILIEKEYL ERMEGHKDTY SYLA
