DCAF1_MOUSE
ID DCAF1_MOUSE Reviewed; 1506 AA.
AC Q80TR8; Q3UXD5; Q6P1E2; Q8CDY3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=DDB1- and CUL4-associated factor 1 {ECO:0000250|UniProtKB:Q9Y4B6};
DE AltName: Full=Serine/threonine-protein kinase VPRBP;
DE EC=2.7.11.1;
GN Name=Dcaf1 {ECO:0000250|UniProtKB:Q9Y4B6}; Synonyms=Kiaa0800, Vprbp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [LARGE SCALE MRNA] OF 1-1488 (ISOFORM 1).
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 613-1506 (ISOFORM 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1269-1506 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Egg, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11223251; DOI=10.1016/s0378-1119(00)00583-7;
RA Zhang S., Feng Y., Narayan O., Zhao L.-J.;
RT "Cytoplasmic retention of HIV-1 regulatory protein Vpr by protein-protein
RT interaction with a novel human cytoplasmic protein VprBP.";
RL Gene 263:131-140(2001).
RN [5]
RP DISRUPTION PHENOTYPE, AND CONDITIONAL KNOCKOUT.
RX PubMed=18606781; DOI=10.1128/mcb.00232-08;
RA McCall C.M., Miliani de Marval P.L., Chastain P.D. II, Jackson S.C.,
RA He Y.J., Kotake Y., Cook J.G., Xiong Y.;
RT "Human immunodeficiency virus type 1 Vpr-binding protein VprBP, a WD40
RT protein associated with the DDB1-CUL4 E3 ubiquitin ligase, is essential for
RT DNA replication and embryonic development.";
RL Mol. Cell. Biol. 28:5621-5633(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CONDITIONAL KNOCKOUT.
RX PubMed=22157821; DOI=10.1038/emboj.2011.455;
RA Kassmeier M.D., Mondal K., Palmer V.L., Raval P., Kumar S., Perry G.A.,
RA Anderson D.K., Ciborowski P., Jackson S., Xiong Y., Swanson P.C.;
RT "VprBP binds full-length RAG1 and is required for B-cell development and
RT V(D)J recombination fidelity.";
RL EMBO J. 31:945-958(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-700, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Acts both as a substrate recognition component of E3
CC ubiquitin-protein ligase complexes and as an atypical serine/threonine-
CC protein kinase, playing key roles in various processes such as cell
CC cycle, telomerase regulation and histone modification. Probable
CC substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-
CC protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex,
CC which mediates ubiquitination and proteasome-dependent degradation of
CC proteins such as NF2. Involved in the turnover of methylated proteins:
CC recognizes and binds methylated proteins via its chromo domain, leading
CC to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP
CC complex. The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-
CC cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins,
CC leading to limit error-prone repair during V(D)J recombination. Also
CC part of the EDVP complex, an E3 ligase complex that mediates
CC ubiquitination of proteins such as TERT, leading to TERT degradation
CC and telomerase inhibition. Also acts as an atypical serine/threonine-
CC protein kinase that specifically mediates phosphorylation of 'Thr-120'
CC of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing
CC transcription. H2AT120ph is present in the regulatory region of many
CC tumor suppresor genes, down-regulates their transcription and is
CC present at high level in a number of tumors. Involved in JNK-mediated
CC apoptosis during cell competition process via its interaction with
CC LLGL1 and LLGL2. {ECO:0000250|UniProtKB:Q9Y4B6,
CC ECO:0000269|PubMed:22157821}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein
CC ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex. Interacts
CC with DDB1; the interaction is direct. Also forms a ternary complex with
CC DDA1 and DDB1. Interacts with NF2 (via FERM domain). Component of the
CC EDVP complex, a E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and
CC DCAF1. Interacts with DYRK2; the interaction is direct. Interacts with
CC RAG1; the interaction is direct. Interacts with LLGL1 and LLGL2.
CC Interacts with histone H3. Interacts with ESR1 and LATS1; probably
CC recruited by LATS1 to promote ESR1 ubiquitination and ubiquitin-
CC mediated proteasomal degradation. {ECO:0000250|UniProtKB:Q9Y4B6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Associated with chromatin in a DDB1-independent and cell cycle-
CC dependent manner: recruited to chromatin as DNA is being replicated and
CC is released from chromatin before mitosis. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q80TR8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TR8-2; Sequence=VSP_025502;
CC Name=3;
CC IsoId=Q80TR8-3; Sequence=VSP_025500, VSP_025501;
CC Name=4;
CC IsoId=Q80TR8-4; Sequence=VSP_025503, VSP_025504;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11223251}.
CC -!- DOMAIN: The protein kinase-like region mediates the threonine-protein
CC kinase activity. {ECO:0000250}.
CC -!- DOMAIN: The DWD boxes are required for interaction with DDB1.
CC {ECO:0000250}.
CC -!- DOMAIN: The chromo domain with a restricted pocket directly recognizes
CC monomethylated substrates. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Early embryonic lethality. Conditional knockout
CC in mouse embryonic fibroblasts results in severely defective
CC progression through S phase and subsequent apoptosis (PubMed:18606781).
CC Conditional knockout in B lineage-specific cells arrests B-cell
CC development at the pro-B-to-pre-B cell transition: mice display modest
CC reduction of D-J(H) rearrangement, while V(H)-DJ(H) and V(kappa)-
CC J(kappa) rearrangements are severely impaired. D-J(H) coding joints
CC show longer junctional nucleotide insertions and a higher mutation
CC frequency in D and J segments than normal (PubMed:22157821).
CC {ECO:0000269|PubMed:18606781, ECO:0000269|PubMed:22157821}.
CC -!- SIMILARITY: Belongs to the VPRBP/DCAF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65654.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC065119; AAH65119.1; -; mRNA.
DR EMBL; AK122372; BAC65654.3; ALT_INIT; Transcribed_RNA.
DR EMBL; AK029372; BAC26425.1; -; mRNA.
DR EMBL; AK135721; BAE22628.1; -; mRNA.
DR CCDS; CCDS23485.1; -. [Q80TR8-4]
DR CCDS; CCDS90657.1; -. [Q80TR8-1]
DR RefSeq; NP_001015507.1; NM_001015507.2. [Q80TR8-4]
DR RefSeq; XP_006511818.1; XM_006511755.3.
DR AlphaFoldDB; Q80TR8; -.
DR SMR; Q80TR8; -.
DR BioGRID; 236458; 12.
DR IntAct; Q80TR8; 2.
DR STRING; 10090.ENSMUSP00000123865; -.
DR iPTMnet; Q80TR8; -.
DR PhosphoSitePlus; Q80TR8; -.
DR EPD; Q80TR8; -.
DR jPOST; Q80TR8; -.
DR MaxQB; Q80TR8; -.
DR PaxDb; Q80TR8; -.
DR PeptideAtlas; Q80TR8; -.
DR PRIDE; Q80TR8; -.
DR ProteomicsDB; 279282; -. [Q80TR8-1]
DR ProteomicsDB; 279283; -. [Q80TR8-2]
DR ProteomicsDB; 279284; -. [Q80TR8-3]
DR ProteomicsDB; 279285; -. [Q80TR8-4]
DR Antibodypedia; 31017; 140 antibodies from 22 providers.
DR Ensembl; ENSMUST00000055009; ENSMUSP00000060025; ENSMUSG00000040325. [Q80TR8-1]
DR Ensembl; ENSMUST00000159645; ENSMUSP00000123865; ENSMUSG00000040325. [Q80TR8-4]
DR Ensembl; ENSMUST00000161758; ENSMUSP00000125730; ENSMUSG00000040325. [Q80TR8-2]
DR GeneID; 321006; -.
DR KEGG; mmu:321006; -.
DR UCSC; uc009rkp.2; mouse. [Q80TR8-4]
DR CTD; 9730; -.
DR MGI; MGI:2445220; Dcaf1.
DR VEuPathDB; HostDB:ENSMUSG00000040325; -.
DR eggNOG; KOG1832; Eukaryota.
DR GeneTree; ENSGT00390000005874; -.
DR HOGENOM; CLU_001785_1_0_1; -.
DR InParanoid; Q80TR8; -.
DR OMA; ECSQDQA; -.
DR OrthoDB; 105679at2759; -.
DR PhylomeDB; Q80TR8; -.
DR TreeFam; TF314434; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 321006; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Vprbp; mouse.
DR PRO; PR:Q80TR8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q80TR8; protein.
DR Bgee; ENSMUSG00000040325; Expressed in undifferentiated genital tubercle and 266 other tissues.
DR ExpressionAtlas; Q80TR8; baseline and differential.
DR Genevisible; Q80TR8; MM.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:1990244; F:histone kinase activity (H2A-T120 specific); ISS:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0030183; P:B cell differentiation; IMP:UniProtKB.
DR GO; GO:0035212; P:cell competition in a multicellular organism; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:1990245; P:histone H2A-T120 phosphorylation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0033151; P:V(D)J recombination; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR033270; VPRBP/DCAF1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13129; PTHR13129; 1.
DR SMART; SM00667; LisH; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Chromatin regulator;
KW Cytoplasm; Host-virus interaction; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..1506
FT /note="DDB1- and CUL4-associated factor 1"
FT /id="PRO_0000287474"
FT DOMAIN 561..592
FT /note="Chromo"
FT DOMAIN 845..877
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REPEAT 1090..1129
FT /note="WD 1"
FT REPEAT 1132..1173
FT /note="WD 2"
FT REPEAT 1175..1212
FT /note="WD 3"
FT REPEAT 1214..1246
FT /note="WD 4"
FT REPEAT 1247..1289
FT /note="WD 5"
FT REGION 141..499
FT /note="Protein kinase-like"
FT /evidence="ECO:0000250"
FT REGION 241..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1289
FT /note="WD repeat-like region"
FT REGION 1392..1506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1417..1506
FT /note="Interaction with NF2"
FT /evidence="ECO:0000250"
FT MOTIF 1241..1248
FT /note="DWD box 1"
FT MOTIF 1277..1284
FT /note="DWD box 2"
FT COMPBIAS 258..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..941
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1394..1496
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B6"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B6"
FT MOD_RES 700
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B6"
FT MOD_RES 887
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B6"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B6"
FT MOD_RES 897
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B6"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B6"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B6"
FT MOD_RES 1327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4B6"
FT VAR_SEQ 952..977
FT /note="LIGRISFIRERPSPCNGRKIRVLRQK -> PPRKGIAFLKGKTNMSLGISQY
FT IFFV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025500"
FT VAR_SEQ 978..1506
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025501"
FT VAR_SEQ 1344
FT /note="I -> IVMFYFS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025502"
FT VAR_SEQ 1404..1419
FT /note="EEEEQEEEDDDEDDDD -> QTARTTLIWKMTSSYL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025503"
FT VAR_SEQ 1420..1506
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025504"
FT CONFLICT 1488
FT /note="T -> S (in Ref. 1; BAC65654)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1506 AA; 168931 MW; 8E817B418BAC5FEA CRC64;
MTTVVVHVDS KAELTTLLEQ WEKDHGSGQD MVPILTRMSE LIEKETEEYR KGDPDPFDDR
HPGRADPECM LGHLLRILFK NDDFMNALVN AYVMTSREPP LNTAACRLLL DIMPGLETAV
VFQEKEGIVE NLFKWAREAD QPLRTYSTGL LGGAMENQDI AANYRDENSQ LVAIVLRRLR
ELQLQEVALR QDSKRPSPRK LSSEPLLPLD EEAVDMDYGD MAVDVVDGEQ ESSRDMEISF
RLDSSHKTSS RVNSATKPEE GGLKKNKSAK HGDRENFRKA KQKLGFSSSD PDRVFVELSN
SSWSEMSPWV IGTNYTLYPM TPAIEQRLIL QYLTPLGEYQ ELLPIFMQLG SRELMMFYID
LKQTNDVLLT FEALKHLASL LLHNKFATEF VAHGGVQKLL EIPRPSMAAT GVSMCLYYLS
YNQDAMERVC MHPHNVLSDV VNYTLWLMEC SHASGCCHAT MFFSICFSFR AVLELFDRYD
GLRRLVNLIS TLEILNLEDQ GALLSDDEIF ASRQTGKHTC MALRKYFEAH LAIKLEQVKQ
SLQRTEGGIL VHPQPPYKAC SYTHEQIVEM MEFLIEYGPA QLYWEPAEVF LKLSCVQLLL
QLISIACNWK TYYARNDTVR FALDVLAILT VVPKIQLQLA ESVDVLDEAG SAVSTVGISI
ILGVAEGEFF IHDAEIQKSA LQIIINCVCG PDNRISSIGK FISGTPRRKL SQTPKSSEHT
LAKMWNVVQS NNGIKVLLSL LSIKMPITDA DQIRALACKA LVGLSRSSTV RQIISKLPLF
SSCQIQQLMK EPVLQDKRSD HVKFCKYAAE LIERVSGKPL LIGTDVSLAR LQKADVVAQS
RISFPEKELL LLIRNHLISK GLGETATVLT READLPMTAA SHSSAFTPVT AAASPVSLPR
TPRIANGIAS RLGSHATVGA SAPSAPPAHP PPRPPQGSLP LPGPSYAGNS PLIGRISFIR
ERPSPCNGRK IRVLRQKSDH GAYSQSPAIK KQLDRHLPSP PTLDSIITEY LREQHARCKN
PVATCPPFSL FTPHQCPEPK QRRQAPINFT SRLNRRASFP KYGGVDGGCF DRHLIFSRFR
PISVFREANE DESGFTCCAF SARERFLMLG TCTGQLKLYN VFSGQEEASY NCHNSAITHL
EPSRDGSLLL TSATWSQPLS ALWGMKSVFD MKHSFTEDHY VEFSKHSQDR VIGTKGDIAH
IYDIQTGNKL LTLFNPDLAN NYKRNCATFN PTDDLVLNDG VLWDVRSAQA IHKFDKFNMN
ISGVFHPNGL EVIINTEIWD LRTFHLLHTV PALDQCRVVF NHTGTVMYGA MLQADDEDDL
LEERMKSPFG SSFRTFNATD YKPIATIDVK RNIFDLCTDT KDCYLAVIEN QGSMDALNMD
TVCRLYEVGR QRLAEDEDEE EDQEEEEQEE EDDDEDDDDT DDLDELDTDQ LLEAELEEDD
NNENAGEDGD NDFSPSDEEL ANLLEEGEEG EDEDSDADEE VELILGDTDS SDNSDLEDDI
ILSLNE
