DPYL4_HUMAN
ID DPYL4_HUMAN Reviewed; 572 AA.
AC O14531; B2RMQ1; D3DRG5; O00240; Q5T0Q7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Dihydropyrimidinase-related protein 4;
DE Short=DRP-4;
DE AltName: Full=Collapsin response mediator protein 3;
DE Short=CRMP-3;
DE AltName: Full=UNC33-like phosphoprotein 4;
DE Short=ULIP-4;
GN Name=DPYSL4; Synonyms=CRMP3, ULIP4;
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].
RC TISSUE=Brain;
RA Hamajima N., Kato Y., Kouwaki M., Wada Y., Sasaski M., Nonaka M.;
RT "Novel members of dihydropyrimidinase related protein family.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-553.
RC TISSUE=Retina;
RX PubMed=9652388; DOI=10.1046/j.1432-1327.1998.2540014.x;
RA Byk T., Ozon S., Sobel A.;
RT "The Ulip family phosphoproteins -- common and specific properties.";
RL Eur. J. Biochem. 254:14-24(1998).
RN [6]
RP PROTEIN SEQUENCE OF 401-415, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain;
RA Lubec G., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
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, DPYSL3 or
CC DPYSL5 (By similarity). Interacts with PLEXA1 (By similarity).
CC Interacts with FLNA (PubMed:25358863). {ECO:0000250,
CC ECO:0000250|UniProtKB:O35098, ECO:0000269|PubMed:25358863}.
CC -!- INTERACTION:
CC O14531; P28799-2: GRN; NbExp=3; IntAct=EBI-719542, EBI-25860013;
CC O14531; O60333-2: KIF1B; NbExp=3; IntAct=EBI-719542, EBI-10975473;
CC O14531; P17612: PRKACA; NbExp=3; IntAct=EBI-719542, EBI-476586;
CC O14531; Q93062: RBPMS; NbExp=3; IntAct=EBI-719542, EBI-740322;
CC O14531; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-719542, EBI-5235340;
CC O14531; P37173: TGFBR2; NbExp=3; IntAct=EBI-719542, EBI-296151;
CC O14531; Q15645: TRIP13; NbExp=3; IntAct=EBI-719542, EBI-358993;
CC O14531; O76024: WFS1; NbExp=3; IntAct=EBI-719542, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; AB006713; BAA21886.1; -; mRNA.
DR EMBL; AL512622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49132.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49134.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49135.1; -; Genomic_DNA.
DR EMBL; BC136329; AAI36330.1; -; mRNA.
DR EMBL; BC136330; AAI36331.1; -; mRNA.
DR EMBL; Y10976; CAA71872.1; -; mRNA.
DR CCDS; CCDS7665.1; -.
DR RefSeq; NP_006417.2; NM_006426.2.
DR PDB; 5NKS; X-ray; 1.80 A; A=1-572.
DR PDBsum; 5NKS; -.
DR AlphaFoldDB; O14531; -.
DR SMR; O14531; -.
DR BioGRID; 115821; 55.
DR IntAct; O14531; 25.
DR MINT; O14531; -.
DR STRING; 9606.ENSP00000339850; -.
DR MEROPS; M38.977; -.
DR GlyGen; O14531; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14531; -.
DR PhosphoSitePlus; O14531; -.
DR BioMuta; DPYSL4; -.
DR EPD; O14531; -.
DR jPOST; O14531; -.
DR MassIVE; O14531; -.
DR MaxQB; O14531; -.
DR PaxDb; O14531; -.
DR PeptideAtlas; O14531; -.
DR PRIDE; O14531; -.
DR ProteomicsDB; 48077; -.
DR TopDownProteomics; O14531; -.
DR Antibodypedia; 32549; 219 antibodies from 29 providers.
DR DNASU; 10570; -.
DR Ensembl; ENST00000338492.9; ENSP00000339850.3; ENSG00000151640.13.
DR GeneID; 10570; -.
DR KEGG; hsa:10570; -.
DR MANE-Select; ENST00000338492.9; ENSP00000339850.3; NM_006426.3; NP_006417.2.
DR UCSC; uc009ybb.4; human.
DR CTD; 10570; -.
DR DisGeNET; 10570; -.
DR GeneCards; DPYSL4; -.
DR HGNC; HGNC:3016; DPYSL4.
DR HPA; ENSG00000151640; Tissue enhanced (brain, heart muscle, retina).
DR MIM; 608407; gene.
DR neXtProt; NX_O14531; -.
DR OpenTargets; ENSG00000151640; -.
DR PharmGKB; PA27474; -.
DR VEuPathDB; HostDB:ENSG00000151640; -.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR InParanoid; O14531; -.
DR OMA; YEQWREK; -.
DR OrthoDB; 719800at2759; -.
DR PhylomeDB; O14531; -.
DR TreeFam; TF314706; -.
DR PathwayCommons; O14531; -.
DR Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
DR SignaLink; O14531; -.
DR BioGRID-ORCS; 10570; 12 hits in 1068 CRISPR screens.
DR GeneWiki; DPYSL4; -.
DR GenomeRNAi; 10570; -.
DR Pharos; O14531; Tbio.
DR PRO; PR:O14531; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O14531; protein.
DR Bgee; ENSG00000151640; Expressed in apex of heart and 127 other tissues.
DR ExpressionAtlas; O14531; baseline and differential.
DR Genevisible; O14531; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0070997; P:neuron death; IEA:InterPro.
DR GO; GO:0097485; P:neuron projection guidance; IEA:InterPro.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR030612; DRP4.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF55; PTHR11647:SF55; 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; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..572
FT /note="Dihydropyrimidinase-related protein 4"
FT /id="PRO_0000165921"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35098"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35098"
FT CONFLICT 122
FT /note="Q -> R (in Ref. 1; BAA21886)"
FT /evidence="ECO:0000305"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 132..141
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 148..158
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:5NKS"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 229..246
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 258..269
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 287..291
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:5NKS"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 361..369
FT /evidence="ECO:0007829|PDB:5NKS"
FT TURN 370..373
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 377..384
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 386..392
FT /evidence="ECO:0007829|PDB:5NKS"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 409..419
FT /evidence="ECO:0007829|PDB:5NKS"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:5NKS"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 438..448
FT /evidence="ECO:0007829|PDB:5NKS"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:5NKS"
FT HELIX 476..491
FT /evidence="ECO:0007829|PDB:5NKS"
SQ SEQUENCE 572 AA; 61878 MW; FCFF3212B4AEA5B4 CRC64;
MSFQGKKSIP RITSDRLLIR GGRIVNDDQS FYADVHVEDG LIKQIGENLI VPGGIKTIDA
HGLMVLPGGV DVHTRLQMPV LGMTPADDFC QGTKAALAGG TTMILDHVFP DTGVSLLAAY
EQWRERADSA ACCDYSLHVD ITRWHESIKE ELEALVKEKG VNSFLVFMAY KDRCQCSDSQ
MYEIFSIIRD LGALAQVHAE NGDIVEEEQK RLLELGITGP EGHVLSHPEE VEAEAVYRAV
TIAKQANCPL YVTKVMSKGA ADAIAQAKRR GVVVFGEPIT ASLGTDGSHY WSKNWAKAAA
FVTSPPVNPD PTTADHLTCL LSSGDLQVTG SAHCTFTTAQ KAVGKDNFAL IPEGTNGIEE
RMSMVWEKCV ASGKMDENEF VAVTSTNAAK IFNFYPRKGR VAVGSDADLV IWNPKATKII
SAKTHNLNVE YNIFEGVECR GAPAVVISQG RVALEDGKMF VTPGAGRFVP RKTFPDFVYK
RIKARNRLAE IHGVPRGLYD GPVHEVMVPA KPGSGAPARA SCPGKISVPP VRNLHQSGFS
LSGSQADDHI ARRTAQKIMA PPGGRSNITS LS
