DPYL3_HUMAN
ID DPYL3_HUMAN Reviewed; 570 AA.
AC Q14195; B3SXQ8; Q93012;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Dihydropyrimidinase-related protein 3;
DE Short=DRP-3;
DE AltName: Full=Collapsin response mediator protein 4;
DE Short=CRMP-4;
DE AltName: Full=Unc-33-like phosphoprotein 1;
DE Short=ULIP-1;
GN Name=DPYSL3; Synonyms=CRMP4, DRP3, ULIP, ULIP1;
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).
RC TISSUE=Brain;
RX PubMed=8973361; DOI=10.1016/s0378-1119(96)00445-3;
RA Hamajima N., Matsuda K., Sakata S., Tamaki N., Sasaki M., Nonaka M.;
RT "A novel gene family defined by human dihydropyrimidinase and three related
RT proteins with differential tissue distribution.";
RL Gene 180:157-163(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9115293; DOI=10.1074/jbc.272.18.12195;
RA Gaetano C., Matsuo T., Thiele C.J.;
RT "Identification and characterization of a retinoic acid-regulated human
RT homologue of the unc-33-like phosphoprotein gene (hUlip) from neuroblastoma
RT cells.";
RL J. Biol. Chem. 272:12195-12201(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LCRMP-4).
RA Pan S.-H., Hong T.-M., Chao Y.-C., Yang S.-C., Yang P.-C.;
RT "Long form collapsin response mediator protein-1 (LCRMP-1) is a novel
RT invasion enhancer: counter-regulation of cancer cell invasion by LCRMP-1
RT and CRMP-1.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP PROTEIN SEQUENCE OF 24-56; 82-122; 131-157; 239-254; 259-268; 346-368;
RP 375-397; 401-418; 424-440; 452-480; 488-511 AND 532-550, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 (ISOFORM LCRMP-4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION AT SER-522 BY DYRK2, AND PHOSPHORYLATION AT THR-509;
RP THR-514 AND SER-518 BY GSK3.
RX PubMed=16611631; DOI=10.1074/jbc.m513344200;
RA Cole A.R., Causeret F., Yadirgi G., Hastie C.J., McLauchlan H.,
RA McManus E.J., Hernandez F., Eickholt B.J., Nikolic M., Sutherland C.;
RT "Distinct priming kinases contribute to differential regulation of
RT collapsin response mediator proteins by glycogen synthase kinase-3 in
RT vivo.";
RL J. Biol. Chem. 281:16591-16598(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259; THR-509; THR-514 AND
RP SER-522, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 (ISOFORM
RP LCRMP-4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509 AND SER-522,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 (ISOFORM LCRMP-4), AND
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 [11]
RP INTERACTION WITH FLNA.
RX PubMed=25358863; DOI=10.1038/ncomms6325;
RA Nakamura F., Kumeta K., Hida T., Isono T., Nakayama Y.,
RA Kuramata-Matsuoka E., Yamashita N., Uchida Y., Ogura K., Gengyo-Ando K.,
RA Mitani S., Ogino T., Goshima Y.;
RT "Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to
RT mediate Sema3A signalling.";
RL Nat. Commun. 5:5325-5325(2014).
CC -!- FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent
CC remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal
CC growth cone collapse and cell migration (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL2, DPYSL4 or
CC DPYSL5 (By similarity). Interacts with synaptic vesicle protein 2 and
CC SH3A domain of intersectin (By similarity). Interacts with FLNA
CC (PubMed:25358863). {ECO:0000250|UniProtKB:Q62952,
CC ECO:0000269|PubMed:25358863}.
CC -!- INTERACTION:
CC Q14195; Q96AP0: ACD; NbExp=2; IntAct=EBI-1104726, EBI-717666;
CC Q14195; Q16555: DPYSL2; NbExp=4; IntAct=EBI-1104726, EBI-1104711;
CC Q14195-2; Q14194: CRMP1; NbExp=6; IntAct=EBI-10232496, EBI-473101;
CC Q14195-2; Q16555: DPYSL2; NbExp=10; IntAct=EBI-10232496, EBI-1104711;
CC Q14195-2; Q9BPU6: DPYSL5; NbExp=3; IntAct=EBI-10232496, EBI-724653;
CC Q14195-2; Q7L8S5: OTUD6A; NbExp=3; IntAct=EBI-10232496, EBI-11960139;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection, growth
CC cone {ECO:0000250}. Note=Colocalizes with synaptic vesicle protein 2 in
CC the central region of the growth cone. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14195-1; Sequence=Displayed;
CC Name=LCRMP-4;
CC IsoId=Q14195-2; Sequence=VSP_042546;
CC -!- TISSUE SPECIFICITY: Mainly expressed in heart and skeletal muscle. Also
CC strongly expressed in fetal brain and spinal cord.
CC -!- PTM: Phosphorylation on Ser-522 by DYRK2 promotes subsequent
CC phosphorylation on Thr-509, Thr-514 and Ser-518 by GSK3.
CC {ECO:0000269|PubMed:16611631}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family. {ECO:0000305}.
CC -!- CAUTION: Lacks most of the conserved residues that are essential for
CC binding the metal cofactor and hence for dihydropyrimidinase activity.
CC Its enzyme activity is therefore unsure. {ECO:0000305}.
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DR EMBL; D78014; BAA11192.1; -; mRNA.
DR EMBL; Y07818; CAA69153.1; -; mRNA.
DR EMBL; EU007906; ABV80252.1; -; mRNA.
DR EMBL; AC011373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS43381.1; -. [Q14195-1]
DR CCDS; CCDS56387.1; -. [Q14195-2]
DR PIR; JC5318; JC5318.
DR RefSeq; NP_001184223.1; NM_001197294.1. [Q14195-2]
DR RefSeq; NP_001378.1; NM_001387.2. [Q14195-1]
DR PDB; 4BKN; X-ray; 2.10 A; A/B=1-570.
DR PDB; 4CNS; X-ray; 2.40 A; A/B/C/D=13-490.
DR PDB; 4CNT; X-ray; 2.65 A; A/B/C/D=1-570.
DR PDB; 4CNU; X-ray; 2.80 A; A/B=1-570.
DR PDBsum; 4BKN; -.
DR PDBsum; 4CNS; -.
DR PDBsum; 4CNT; -.
DR PDBsum; 4CNU; -.
DR AlphaFoldDB; Q14195; -.
DR SMR; Q14195; -.
DR BioGRID; 108143; 76.
DR IntAct; Q14195; 30.
DR MINT; Q14195; -.
DR STRING; 9606.ENSP00000343690; -.
DR MEROPS; M38.976; -.
DR GlyGen; Q14195; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14195; -.
DR MetOSite; Q14195; -.
DR PhosphoSitePlus; Q14195; -.
DR SwissPalm; Q14195; -.
DR BioMuta; DPYSL3; -.
DR DMDM; 3122050; -.
DR REPRODUCTION-2DPAGE; Q14195; -.
DR UCD-2DPAGE; Q14195; -.
DR EPD; Q14195; -.
DR jPOST; Q14195; -.
DR MassIVE; Q14195; -.
DR MaxQB; Q14195; -.
DR PaxDb; Q14195; -.
DR PeptideAtlas; Q14195; -.
DR PRIDE; Q14195; -.
DR ProteomicsDB; 59917; -. [Q14195-1]
DR ProteomicsDB; 59918; -. [Q14195-2]
DR Antibodypedia; 1526; 306 antibodies from 29 providers.
DR DNASU; 1809; -.
DR Ensembl; ENST00000343218.10; ENSP00000343690.5; ENSG00000113657.13. [Q14195-2]
DR Ensembl; ENST00000398514.7; ENSP00000381526.3; ENSG00000113657.13. [Q14195-1]
DR GeneID; 1809; -.
DR KEGG; hsa:1809; -.
DR MANE-Select; ENST00000343218.10; ENSP00000343690.5; NM_001197294.2; NP_001184223.1. [Q14195-2]
DR UCSC; uc003lon.2; human. [Q14195-1]
DR CTD; 1809; -.
DR DisGeNET; 1809; -.
DR GeneCards; DPYSL3; -.
DR HGNC; HGNC:3015; DPYSL3.
DR HPA; ENSG00000113657; Low tissue specificity.
DR MIM; 601168; gene.
DR neXtProt; NX_Q14195; -.
DR OpenTargets; ENSG00000113657; -.
DR PharmGKB; PA27473; -.
DR VEuPathDB; HostDB:ENSG00000113657; -.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; Q14195; -.
DR OMA; RNFVCSP; -.
DR PhylomeDB; Q14195; -.
DR TreeFam; TF314706; -.
DR PathwayCommons; Q14195; -.
DR Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
DR SignaLink; Q14195; -.
DR SIGNOR; Q14195; -.
DR BioGRID-ORCS; 1809; 7 hits in 1068 CRISPR screens.
DR ChiTaRS; DPYSL3; human.
DR GeneWiki; DPYSL3; -.
DR GenomeRNAi; 1809; -.
DR Pharos; Q14195; Tbio.
DR PRO; PR:Q14195; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q14195; protein.
DR Bgee; ENSG00000113657; Expressed in cortical plate and 198 other tissues.
DR ExpressionAtlas; Q14195; baseline and differential.
DR Genevisible; Q14195; HS.
DR GO; GO:0044297; C:cell body; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
DR GO; GO:0031005; F:filamin binding; IPI:WormBase.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; ISS:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; ISS:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0048678; P:response to axon injury; ISS:UniProtKB.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR030628; DRP3.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF57; PTHR11647:SF57; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1..570
FT /note="Dihydropyrimidinase-related protein 3"
FT /id="PRO_0000165917"
FT REGION 506..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 431
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62188"
FT MOD_RES 499
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q62188"
FT MOD_RES 509
FT /note="Phosphothreonine; by GSK3"
FT /evidence="ECO:0000269|PubMed:16611631,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 514
FT /note="Phosphothreonine; by GSK3"
FT /evidence="ECO:0000269|PubMed:16611631,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 518
FT /note="Phosphoserine; by GSK3"
FT /evidence="ECO:0000269|PubMed:16611631"
FT MOD_RES 522
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000269|PubMed:16611631,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62188"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62188"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62188"
FT MOD_RES 543
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q62188"
FT VAR_SEQ 1..13
FT /note="MSYQGKKNIPRIT -> MASGRRGWDSSHEDDLPVYLARPGTTDQVPRQKYG
FT GMFCNVEGAFESKTLDFDALSVGQRGAKTPRSGQGSDRGSGSRPGIEGDTPRRGQGREE
FT SREPAPASPAPAGVEIRSATGKEVLQNLGPKDK (in isoform LCRMP-4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_042546"
FT VARIANT 442
FT /note="A -> S (in dbSNP:rs2304044)"
FT /id="VAR_020485"
FT CONFLICT 49
FT /note="L -> V (in Ref. 2; CAA69153)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="T -> A (in Ref. 2; CAA69153)"
FT /evidence="ECO:0000305"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 132..141
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:4BKN"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 178..191
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 229..245
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 258..270
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:4BKN"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 361..369
FT /evidence="ECO:0007829|PDB:4BKN"
FT TURN 370..373
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 386..391
FT /evidence="ECO:0007829|PDB:4BKN"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 409..419
FT /evidence="ECO:0007829|PDB:4BKN"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:4BKN"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 438..448
FT /evidence="ECO:0007829|PDB:4BKN"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:4BKN"
FT HELIX 476..487
FT /evidence="ECO:0007829|PDB:4BKN"
FT MOD_RES Q14195-2:102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
SQ SEQUENCE 570 AA; 61963 MW; 9D6AFE86CBB33AD5 CRC64;
MSYQGKKNIP RITSDRLLIK GGRIVNDDQS FYADIYMEDG LIKQIGDNLI VPGGVKTIEA
NGKMVIPGGI DVHTHFQMPY KGMTTVDDFF QGTKAALAGG TTMIIDHVVP EPESSLTEAY
EKWREWADGK SCCDYALHVD ITHWNDSVKQ EVQNLIKDKG VNSFMVYMAY KDLYQVSNTE
LYEIFTCLGE LGAIAQVHAE NGDIIAQEQT RMLEMGITGP EGHVLSRPEE LEAEAVFRAI
TIASQTNCPL YVTKVMSKSA ADLISQARKK GNVVFGEPIT ASLGIDGTHY WSKNWAKAAA
FVTSPPLSPD PTTPDYINSL LASGDLQLSG SAHCTFSTAQ KAIGKDNFTA IPEGTNGVEE
RMSVIWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR ISVGSDSDLV IWDPDAVKIV
SAKNHQSAAE YNIFEGMELR GAPLVVICQG KIMLEDGNLH VTQGAGRFIP CSPFSDYVYK
RIKARRKMAD LHAVPRGMYD GPVFDLTTTP KGGTPAGSAR GSPTRPNPPV RNLHQSGFSL
SGTQVDEGVR SASKRIVAPP GGRSNITSLS
