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Database: UniProt
Entry: HCF_DROME
LinkDB: HCF_DROME
Original site: HCF_DROME 
ID   HCF_DROME               Reviewed;        1500 AA.
AC   Q9V4C8; A4V109; H9XVN5; Q8IGU2; Q95S26; Q95ZF3; Q9BKH1;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Host cell factor;
DE            Short=dHcf;
DE   Contains:
DE     RecName: Full=HCF N-terminal chain;
DE   Contains:
DE     RecName: Full=HCF C-terminal chain;
GN   Name=Hcf {ECO:0000312|EMBL:AAF59349.2}; ORFNames=CG1710;
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] {ECO:0000305, ECO:0000312|EMBL:CAC44472.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), SUBCELLULAR LOCATION, NUCLEAR
RP   LOCALIZATION SIGNAL, AND MUTAGENESIS OF 1470-LYS-ARG-1471 AND
RP   1492-LYS--ARG-1495.
RC   TISSUE=Embryo {ECO:0000269|PubMed:12609738};
RX   PubMed=12609738; DOI=10.1016/s0378-1119(03)00380-9;
RA   Izeta A., Malcomber S., O'Hare P.;
RT   "Primary structure and compartmentalization of Drosophila melanogaster host
RT   cell factor.";
RL   Gene 305:175-183(2003).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAK28427.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; D AND G), FUNCTION, DEVELOPMENTAL
RP   STAGE, AND PROTEOLYTIC CLEAVAGE.
RC   STRAIN=Berkeley; TISSUE=Embryo {ECO:0000269|PubMed:12494450};
RX   PubMed=12494450; DOI=10.1002/jcp.10193;
RA   Mahajan S.S., Johnson K.M., Wilson A.C.;
RT   "Molecular cloning of Drosophila HCF reveals proteolytic processing and
RT   self-association of the encoded protein.";
RL   J. Cell. Physiol. 194:117-126(2003).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAF59349.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAF59349.2}
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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] {ECO:0000305, ECO:0000312|EMBL:AAL28531.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAL28531.1};
RC   TISSUE=Embryo {ECO:0000269|PubMed:12537569}, and
RC   Ovary {ECO:0000269|PubMed:12537569};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6] {ECO:0000305, ECO:0000312|EMBL:AAT94497.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAT94497.1}; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE ATAC COMPLEX,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=18327268; DOI=10.1038/nsmb.1397;
RA   Suganuma T., Gutierrez J.L., Li B., Florens L., Swanson S.K.,
RA   Washburn M.P., Abmayr S.M., Workman J.L.;
RT   "ATAC is a double histone acetyltransferase complex that stimulates
RT   nucleosome sliding.";
RL   Nat. Struct. Mol. Biol. 15:364-372(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-958; SER-966;
RP   THR-1126 AND SER-1489, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
RN   [9]
RP   IDENTIFICATION IN THE SET1 COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=21694722; DOI=10.1038/emboj.2011.194;
RA   Ardehali M.B., Mei A., Zobeck K.L., Caron M., Lis J.T., Kusch T.;
RT   "Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase with
RT   role in transcription.";
RL   EMBO J. 30:2817-2828(2011).
RN   [10]
RP   IDENTIFICATION IN THE SET1 AND MLL3/4 COMPLEXES.
RX   PubMed=21875999; DOI=10.1128/mcb.06092-11;
RA   Mohan M., Herz H.M., Smith E.R., Zhang Y., Jackson J., Washburn M.P.,
RA   Florens L., Eissenberg J.C., Shilatifard A.;
RT   "The COMPASS family of H3K4 methylases in Drosophila.";
RL   Mol. Cell. Biol. 31:4310-4318(2011).
CC   -!- FUNCTION: May be involved in control of the cell cycle.
CC       {ECO:0000269|PubMed:12494450}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 20 degrees Celsius for complex formation
CC         activity of the N-terminus and 33.5 degrees Celsius for nuclear
CC         localization of the protein in vitro. {ECO:0000269|PubMed:12494450,
CC         ECO:0000269|PubMed:12609738};
CC   -!- SUBUNIT: Core component of several methyltransferase-containing
CC       complexes. Component of the SET1 complex, composed at least of the
CC       catalytic subunit Set1, wds/WDR5, Wdr82, Rbbp5, ash2, Cfp1/CXXC1, hcf
CC       and Dpy-30L1. Component of the MLL3/4 complex composed at least of the
CC       catalytic subunit trr, ash2, Rbbp5, Dpy-30L1, wds, hcf, ptip, Pa1, Utx,
CC       Lpt and Ncoa6. Component of the Ada2a-containing (ATAC) complex
CC       composed of at least Ada2a, Atac1, Hcf, Ada3, Gcn5, Mocs2B, Charac-14,
CC       Atac3, Atac2, NC2beta and wds (PubMed:18327268).
CC       {ECO:0000269|PubMed:18327268, ECO:0000269|PubMed:21694722,
CC       ECO:0000269|PubMed:21875999}.
CC   -!- INTERACTION:
CC       Q9V4C8; Q5LJZ2: Set1; NbExp=3; IntAct=EBI-2912878, EBI-3405171;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12609738,
CC       ECO:0000269|PubMed:18327268, ECO:0000269|PubMed:21694722}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=A {ECO:0000269|PubMed:12494450}; Synonyms=B
CC       {ECO:0000303|PubMed:10731132};
CC         IsoId=Q9V4C8-1; Sequence=Displayed;
CC       Name=E;
CC         IsoId=Q9V4C8-6; Sequence=VSP_047937, VSP_047938;
CC       Name=F;
CC         IsoId=Q9V4C8-5; Sequence=VSP_047712;
CC       Name=D {ECO:0000269|PubMed:12494450}; Synonyms=8-11
CC       {ECO:0000303|PubMed:12494450};
CC         IsoId=Q9V4C8-3; Sequence=Not described;
CC       Name=G; Synonyms=11-13 {ECO:0000303|PubMed:12494450};
CC         IsoId=Q9V4C8-4; Sequence=Not described;
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development and in adults.
CC       {ECO:0000269|PubMed:12494450}.
CC   -!- PTM: Proteolytic cleavage occurs between amino acids 900 and 1100
CC       within the non-conserved central region, giving rise to two independent
CC       but tightly associated N- and C-terminal subunits.
CC       {ECO:0000269|PubMed:12494450}.
CC   -!- MISCELLANEOUS: Due to lack of HCF repeats, the cleavage process occurs
CC       via a different mechanism to that in the mammalian HCFC1.
CC       {ECO:0000305|PubMed:12494450}.
CC   -!- MISCELLANEOUS: [Isoform D]: Exons 9 and 10 deleted.
CC       {ECO:0000269|PubMed:12494450}.
CC   -!- MISCELLANEOUS: [Isoform G]: Exon 12 deleted. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL28531.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ320236; CAC44472.1; -; mRNA.
DR   EMBL; AF251006; AAK28427.1; -; mRNA.
DR   EMBL; AE014135; AAF59349.2; -; Genomic_DNA.
DR   EMBL; AE014135; AAN06529.1; -; Genomic_DNA.
DR   EMBL; AE014135; AAN06530.2; -; Genomic_DNA.
DR   EMBL; AE014135; AFH06780.1; -; Genomic_DNA.
DR   EMBL; AY060983; AAL28531.1; ALT_INIT; mRNA.
DR   EMBL; BT001602; AAN71357.1; -; mRNA.
DR   EMBL; BT015268; AAT94497.1; -; mRNA.
DR   RefSeq; NP_001245420.1; NM_001258491.3. [Q9V4C8-6]
DR   RefSeq; NP_524621.2; NM_079882.4. [Q9V4C8-1]
DR   RefSeq; NP_726566.1; NM_166756.3. [Q9V4C8-1]
DR   RefSeq; NP_726567.2; NM_166757.3. [Q9V4C8-5]
DR   RefSeq; NP_995595.1; NM_205873.3. [Q9V4C8-1]
DR   AlphaFoldDB; Q9V4C8; -.
DR   SMR; Q9V4C8; -.
DR   BioGRID; 68622; 36.
DR   ComplexPortal; CPX-2287; Histone-lysine N-methyltransferase TRX complex.
DR   ComplexPortal; CPX-2423; SWR1 chromatin remodelling complex.
DR   ComplexPortal; CPX-2742; ATAC histone acetyltransferase complex.
DR   ComplexPortal; CPX-2798; COMPASS complex.
DR   IntAct; Q9V4C8; 9.
DR   MINT; Q9V4C8; -.
DR   STRING; 7227.FBpp0311451; -.
DR   GlyGen; Q9V4C8; 8 sites, 1 O-linked glycan (8 sites).
DR   iPTMnet; Q9V4C8; -.
DR   PaxDb; 7227-FBpp0088193; -.
DR   EnsemblMetazoa; FBtr0089125; FBpp0088194; FBgn0039904. [Q9V4C8-1]
DR   EnsemblMetazoa; FBtr0089126; FBpp0088195; FBgn0039904. [Q9V4C8-1]
DR   EnsemblMetazoa; FBtr0307379; FBpp0298368; FBgn0039904. [Q9V4C8-6]
DR   EnsemblMetazoa; FBtr0334479; FBpp0306551; FBgn0039904. [Q9V4C8-5]
DR   EnsemblMetazoa; FBtr0345284; FBpp0311451; FBgn0039904. [Q9V4C8-1]
DR   GeneID; 43788; -.
DR   KEGG; dme:Dmel_CG1710; -.
DR   AGR; FB:FBgn0039904; -.
DR   CTD; 43788; -.
DR   FlyBase; FBgn0039904; Hcf.
DR   VEuPathDB; VectorBase:FBgn0039904; -.
DR   eggNOG; KOG4152; Eukaryota.
DR   GeneTree; ENSGT00940000166952; -.
DR   InParanoid; Q9V4C8; -.
DR   OMA; GPCGTIH; -.
DR   OrthoDB; 5477547at2759; -.
DR   PhylomeDB; Q9V4C8; -.
DR   Reactome; R-DME-5689603; UCH proteinases.
DR   Reactome; R-DME-9772755; Formation of WDR5-containing histone-modifying complexes.
DR   SignaLink; Q9V4C8; -.
DR   BioGRID-ORCS; 43788; 1 hit in 3 CRISPR screens.
DR   GenomeRNAi; 43788; -.
DR   PRO; PR:Q9V4C8; -.
DR   Proteomes; UP000000803; Chromosome 4.
DR   Bgee; FBgn0039904; Expressed in central nervous system and 19 other cell types or tissues.
DR   Genevisible; Q9V4C8; DM.
DR   GO; GO:0140672; C:ATAC complex; IDA:FlyBase.
DR   GO; GO:0035097; C:histone methyltransferase complex; IBA:GO_Central.
DR   GO; GO:0044665; C:MLL1/2 complex; ISS:FlyBase.
DR   GO; GO:0044666; C:MLL3/4 complex; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IDA:FlyBase.
DR   GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR   GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:FlyBase.
DR   GO; GO:0045927; P:positive regulation of growth; IGI:FlyBase.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 6.10.250.2590; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR043536; HCF1/2.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   PANTHER; PTHR46003; HOST CELL FACTOR; 1.
DR   PANTHER; PTHR46003:SF1; HOST CELL FACTOR; 1.
DR   Pfam; PF01344; Kelch_1; 1.
DR   Pfam; PF13415; Kelch_3; 2.
DR   Pfam; PF13854; Kelch_5; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF117281; Kelch motif; 1.
DR   PROSITE; PS50853; FN3; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Autocatalytic cleavage; Cell cycle; Kelch repeat;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..?
FT                   /note="HCF N-terminal chain"
FT                   /id="PRO_0000016647"
FT   CHAIN           ?..1500
FT                   /note="HCF C-terminal chain"
FT                   /id="PRO_0000016648"
FT   REPEAT          85..133
FT                   /note="Kelch 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          135..181
FT                   /note="Kelch 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          189..237
FT                   /note="Kelch 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          259..307
FT                   /note="Kelch 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          308..373
FT                   /note="Kelch 5"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1244..1341
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1346..1457
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          517..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1024..1061
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1161..1185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1458..1500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1470..1495
FT                   /note="Bipartite nuclear localization signal"
FT   COMPBIAS        1033..1057
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1161..1177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1459..1489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         477
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         958
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         966
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1126
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1489
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   VAR_SEQ         392..443
FT                   /note="Missing (in isoform F)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047712"
FT   VAR_SEQ         392
FT                   /note="V -> VRV (in isoform E)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047937"
FT   VAR_SEQ         794..811
FT                   /note="Missing (in isoform E)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_047938"
FT   MUTAGEN         1470..1471
FT                   /note="Missing: Causes accumulation exclusively in the
FT                   cytoplasm."
FT                   /evidence="ECO:0000269|PubMed:12609738"
FT   MUTAGEN         1492..1495
FT                   /note="Missing: Causes accumulation exclusively in the
FT                   cytoplasm."
FT                   /evidence="ECO:0000269|PubMed:12609738"
FT   CONFLICT        694
FT                   /note="K -> T (in Ref. 2; AAK28427)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        956
FT                   /note="R -> K (in Ref. 2; AAK28427)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1500 AA;  160185 MW;  1275EC71E7D8A44F CRC64;
     MEGSDFVDPA FSSGERISAS DLNSEHIIQA ENHSFANRIS MDMDVPDGHQ LDSNLTGFRW
     KRVLNPTGPQ PRPRHGHRAI NIKELMVVFG GGNEGIVDEL HVYNTVTNQW YVPVLKGDVP
     NGCAAYGFVV EGTRMFVFGG MIEYGKYSNE LYELQATKWE WRKMYPESPD SGLSPCPRLG
     HSFTMVGEKI FLFGGLANES DDPKNNIPKY LNDLYILDTR GVHSHNGKWI VPKTYGDSPP
     PRESHTGISF ATKSNGNLNL LIYGGMSGCR LGDLWLLETD SMTWSKPKTS GEAPLPRSLH
     SSTMIGNKMY VFGGWVPLVI NDSKSTTERE WKCTNTLAVL DLETMTWENV TLDTVEENVP
     RARAGHCAVG IQSRLYVWSG RDGYRKAWNN QVCCKDLWYL EVSKPLYAVK VALVRASTHA
     LELSWTATTF AAAYVLQIQK IEQPLNTSSK LLSNNIVQQG TPTSAETSGI NISANRSGSA
     LGLGVEATST VLKLEKESLQ LSGCQPETNV QPSVNDLLQS MSQPSSPASR ADKDPLSSGG
     GTTFNLSTSV ASVHPQISVI SSTAAVTGND TASPSGAINS ILQKFRPVVT AVRTSTTTAV
     SIATSTSDPL SVRVPSTMSA NVVLSSSSST LRIVPSVTAS HSLRIASSQA SGNNCRSSSA
     INILKTALPN VAVQSQPTSS TTTSIGGKQY FIQKPLTLAP NVQLQFVKTS GGMTVQTLPK
     VNFTASKGTP PHGISIANPH LASGITQIQG STVPGSQIQK PIVSGNVLKL VSPHTMAGGK
     LIMKNSNILQ MGKVTPNVMG GKPAFVITNK QGTPLGNQQI IIVTTGGNVR SVPTSTVMTS
     AGGSASGTNI VSIVNSTSTT PSPLQALSGQ KTLISNQSGV KMLRNISSVQ ASSSMAFGQK
     QSGTPIHQKT ALYIGGKAVT VMSTNTSMAA SGNKVMVLPG TSSNNSPATT TALSARKSFV
     FNAGGSPRTV TLATKSINAK SIPQSQPVTE TNNHSVATIK DTDPMDDIIE QLDGAGDLLK
     LSESEGQHGS EENENNGENA TSSSASALFT GGDTAGPSRA QNPIVMEHPV DIIEDVSGVS
     STTDVNETAI VSGDTIESLK MSEKENDDVK SMGEKSILSD DCHQPTTSET EAATILTTIK
     SAEALVLETA EIRKDHTGCT IGSLKENQDE NKKFKQRQES SPSQNIHQFQ NVDGSQLEAL
     ASAALLQAAT SDTTALALKE LIERPESETN TRSSNIAEIQ QNNVQSTLAV VVPNTSQNEN
     QKWHTVGVFK DLSHTVTSYI DSNCISDSFF DGIDVDNLPD FSKFPRTNLE PGTAYRFRLS
     AINSCGRGEW GEISSFKTCL PGFPGAPSAI KISKDVKEGA HLTWEPPPAQ KTKEIIEYSV
     YLAVKPTAKD KALSTPQLAF VRVYVGAANQ CTVPNASLSN AHVDCSNKPA IIFRIAARNQ
     KGYGPATQVR WLQDPAAAKQ HTPTVTPNLK RGPEKSTIGS SNIANTFCSP HKRGRNGLHD
//
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