ID DPYL5_HUMAN Reviewed; 564 AA. AC Q9BPU6; Q8TCL6; Q9NQC4; Q9NRY9; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 191. DE RecName: Full=Dihydropyrimidinase-related protein 5; DE Short=DRP-5; DE AltName: Full=CRMP3-associated molecule; DE Short=CRAM; DE AltName: Full=Collapsin response mediator protein 5; DE Short=CRMP-5; DE AltName: Full=UNC33-like phosphoprotein 6; DE Short=ULIP-6; GN Name=DPYSL5; Synonyms=CRMP5, ULIP6; 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=Spinal cord; RA Aguera M., Antoine J.-C., Belin M.-F., Charrier E., Honnorat J., RA Rogemond V.; RT "Ulip6, a new human Unc-33-like phosphoprotein."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Spinal cord; RX PubMed=11034345; DOI=10.1016/s0014-5793(00)01952-9; RA Horiuchi M., El Far O., Betz H.; RT "Ulip6, a novel unc-33 and dihydropyrimidinase related protein highly RT expressed in developing rat brain."; RL FEBS Lett. 480:283-286(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11220734; RX DOI=10.1002/1531-8249(20010201)49:2<146::aid-ana34>3.3.co;2-5; RA Yu Z., Kryzer T.J., Griesmann G.E., Kim K., Benarroch E.E., Lennon V.A.; RT "CRMP-5 neuronal autoantibody: marker of lung cancer and thymoma-related RT autoimmunity."; RL Ann. Neurol. 49:146-154(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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 [6] RP PROTEIN SEQUENCE OF 17-40; 204-231; 239-261; 373-383; 394-431; 490-504 AND RP 527-546, AND IDENTIFICATION 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-564. RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). 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 VARIANTS RTSC4 LYS-41 AND ARG-47, INVOLVEMENT IN RTSC4, FUNCTION, RP INTERACTION WITH MAP2 AND TUBB3, AND CHARACTERIZATION OF VARIANTS RTSC4 RP LYS-41 AND ARG-47. RX PubMed=33894126; DOI=10.1016/j.ajhg.2021.04.004; RA Jeanne M., Demory H., Moutal A., Vuillaume M.L., Blesson S., Thepault R.A., RA Marouillat S., Halewa J., Maas S.M., Motazacker M.M., Mancini G.M.S., RA van Slegtenhorst M.A., Andreou A., Cox H., Vogt J., Laufman J., RA Kostandyan N., Babikyan D., Hancarova M., Bendova S., Sedlacek Z., RA Aldinger K.A., Sherr E.H., Argilli E., England E.M., Audebert-Bellanger S., RA Bonneau D., Colin E., Denomme-Pichon A.S., Gilbert-Dussardier B., RA Isidor B., Kuery S., Odent S., Redon R., Khanna R., Dobyns W.B., RA Bezieau S., Honnorat J., Lohkamp B., Toutain A., Laumonnier F.; RT "Missense variants in DPYSL5 cause a neurodevelopmental disorder with RT corpus callosum agenesis and cerebellar abnormalities."; RL Am. J. Hum. Genet. 108:951-961(2021). CC -!- FUNCTION: Involved in the negative regulation of dendrite outgrowth. CC {ECO:0000269|PubMed:33894126}. CC -!- SUBUNIT: Homotetramer, and heterotetramer with other DPYS-like CC proteins. Interacts with DPYSL2, DPYSL3 and DPYSL4 (By similarity). CC Interacts with MAP2 and TUBB3 (PubMed:33894126). CC {ECO:0000250|UniProtKB:Q9EQF6, ECO:0000269|PubMed:33894126}. CC -!- INTERACTION: CC Q9BPU6; P55212: CASP6; NbExp=3; IntAct=EBI-724653, EBI-718729; CC Q9BPU6; Q6P656: CFAP161; NbExp=3; IntAct=EBI-724653, EBI-11901329; CC Q9BPU6; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-724653, EBI-745535; CC Q9BPU6; Q16555: DPYSL2; NbExp=14; IntAct=EBI-724653, EBI-1104711; CC Q9BPU6; Q14195-2: DPYSL3; NbExp=3; IntAct=EBI-724653, EBI-10232496; CC Q9BPU6; P22607: FGFR3; NbExp=3; IntAct=EBI-724653, EBI-348399; CC Q9BPU6; Q14957: GRIN2C; NbExp=3; IntAct=EBI-724653, EBI-8285963; CC Q9BPU6; P06396: GSN; NbExp=3; IntAct=EBI-724653, EBI-351506; CC Q9BPU6; O00291: HIP1; NbExp=3; IntAct=EBI-724653, EBI-473886; CC Q9BPU6; P04792: HSPB1; NbExp=3; IntAct=EBI-724653, EBI-352682; CC Q9BPU6; P42858: HTT; NbExp=9; IntAct=EBI-724653, EBI-466029; CC Q9BPU6; O60333-2: KIF1B; NbExp=3; IntAct=EBI-724653, EBI-10975473; CC Q9BPU6; O14901: KLF11; NbExp=3; IntAct=EBI-724653, EBI-948266; CC Q9BPU6; P13473-2: LAMP2; NbExp=3; IntAct=EBI-724653, EBI-21591415; CC Q9BPU6; P28331-2: NDUFS1; NbExp=3; IntAct=EBI-724653, EBI-6190702; CC Q9BPU6; O43933: PEX1; NbExp=3; IntAct=EBI-724653, EBI-988601; CC Q9BPU6; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-724653, EBI-5280197; CC Q9BPU6; P62826: RAN; NbExp=3; IntAct=EBI-724653, EBI-286642; CC Q9BPU6; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-724653, EBI-396669; CC Q9BPU6; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-724653, EBI-741480; CC Q9BPU6; O76024: WFS1; NbExp=3; IntAct=EBI-724653, EBI-720609; CC Q9BPU6; Q9Y649; NbExp=3; IntAct=EBI-724653, EBI-25900580; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- DISEASE: Ritscher-Schinzel syndrome 4 (RTSC4) [MIM:619435]: An CC autosomal dominant form of Ritscher-Schinzel syndrome, a developmental CC malformation syndrome characterized by cerebellar brain anomalies CC associated with global developmental delay and impaired intellectual CC development, congenital heart defects, and craniofacial abnormalities. CC {ECO:0000269|PubMed:33894126}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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}. 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; AF264015; AAK16830.1; -; mRNA. DR EMBL; AJ251275; CAB95124.1; -; mRNA. DR EMBL; AF157634; AAF80348.1; -; mRNA. DR EMBL; BT006871; AAP35517.1; -; mRNA. DR EMBL; BC002874; AAH02874.1; -; mRNA. DR EMBL; AL713706; CAD28503.1; -; mRNA. DR CCDS; CCDS1730.1; -. DR RefSeq; NP_001240652.1; NM_001253723.1. DR RefSeq; NP_001240653.1; NM_001253724.1. DR RefSeq; NP_064519.2; NM_020134.3. DR PDB; 4B90; X-ray; 2.20 A; A/B=1-564. DR PDB; 4B91; X-ray; 1.70 A; A/B=1-483. DR PDB; 4B92; X-ray; 2.90 A; A/B=1-483. DR PDBsum; 4B90; -. DR PDBsum; 4B91; -. DR PDBsum; 4B92; -. DR AlphaFoldDB; Q9BPU6; -. DR SMR; Q9BPU6; -. DR BioGRID; 121226; 59. DR IntAct; Q9BPU6; 46. DR STRING; 9606.ENSP00000288699; -. DR MEROPS; M38.978; -. DR GlyGen; Q9BPU6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BPU6; -. DR PhosphoSitePlus; Q9BPU6; -. DR SwissPalm; Q9BPU6; -. DR BioMuta; DPYSL5; -. DR DMDM; 20137929; -. DR EPD; Q9BPU6; -. DR jPOST; Q9BPU6; -. DR MassIVE; Q9BPU6; -. DR MaxQB; Q9BPU6; -. DR PaxDb; 9606-ENSP00000288699; -. DR PeptideAtlas; Q9BPU6; -. DR ProteomicsDB; 78573; -. DR Pumba; Q9BPU6; -. DR Antibodypedia; 28026; 322 antibodies from 28 providers. DR DNASU; 56896; -. DR Ensembl; ENST00000288699.11; ENSP00000288699.6; ENSG00000157851.17. DR Ensembl; ENST00000401478.5; ENSP00000385549.1; ENSG00000157851.17. DR Ensembl; ENST00000614712.4; ENSP00000481305.1; ENSG00000157851.17. DR GeneID; 56896; -. DR KEGG; hsa:56896; -. DR MANE-Select; ENST00000288699.11; ENSP00000288699.6; NM_020134.4; NP_064519.2. DR UCSC; uc002rhu.4; human. DR AGR; HGNC:20637; -. DR CTD; 56896; -. DR DisGeNET; 56896; -. DR GeneCards; DPYSL5; -. DR HGNC; HGNC:20637; DPYSL5. DR HPA; ENSG00000157851; Tissue enriched (brain). DR MalaCards; DPYSL5; -. DR MIM; 608383; gene. DR MIM; 619435; phenotype. DR neXtProt; NX_Q9BPU6; -. DR OpenTargets; ENSG00000157851; -. DR Orphanet; 7; 3C syndrome. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR PharmGKB; PA134927413; -. DR VEuPathDB; HostDB:ENSG00000157851; -. DR eggNOG; KOG2584; Eukaryota. DR GeneTree; ENSGT01030000234527; -. DR HOGENOM; CLU_015572_2_2_1; -. DR InParanoid; Q9BPU6; -. DR OMA; CEHTPSI; -. DR OrthoDB; 1772494at2759; -. DR PhylomeDB; Q9BPU6; -. DR TreeFam; TF314706; -. DR PathwayCommons; Q9BPU6; -. DR Reactome; R-HSA-399956; CRMPs in Sema3A signaling. DR SignaLink; Q9BPU6; -. DR SIGNOR; Q9BPU6; -. DR BioGRID-ORCS; 56896; 12 hits in 1151 CRISPR screens. DR ChiTaRS; DPYSL5; human. DR GeneWiki; DPYSL5; -. DR GenomeRNAi; 56896; -. DR Pharos; Q9BPU6; Tbio. DR PRO; PR:Q9BPU6; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9BPU6; Protein. DR Bgee; ENSG00000157851; Expressed in cortical plate and 102 other cell types or tissues. DR ExpressionAtlas; Q9BPU6; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl. DR GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IBA:GO_Central. DR GO; GO:0007411; P:axon guidance; TAS:ProtInc. DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IMP:UniProtKB. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd01314; D-HYD; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR011778; Hydantoinase/dihydroPyrase. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR02033; D-hydantoinase; 1. DR PANTHER; PTHR11647:SF58; DIHYDROPYRIMIDINASE-RELATED PROTEIN 5; 1. DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR UCD-2DPAGE; Q9BPU6; -. DR Genevisible; Q9BPU6; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Disease variant; KW Methylation; Phosphoprotein; Reference proteome. FT CHAIN 1..564 FT /note="Dihydropyrimidinase-related protein 5" FT /id="PRO_0000165924" FT MOD_RES 509 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9EQF6" FT MOD_RES 514 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9EQF6" FT MOD_RES 532 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9EQF6" FT MOD_RES 538 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9EQF6" FT MOD_RES 559 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9EQF6" FT VARIANT 41 FT /note="E -> K (in RTSC4; reduced inhibition of dendrite FT development in transfected primary neurons; decreased FT interaction with MAP2; decreased interaction with TUBB3)" FT /evidence="ECO:0000269|PubMed:33894126" FT /id="VAR_086051" FT VARIANT 47 FT /note="G -> R (in RTSC4; reduced inhibition of dendrite FT development in transfected primary neurons; decreased FT interaction with MAP2; decreased interaction with TUBB3)" FT /evidence="ECO:0000269|PubMed:33894126" FT /id="VAR_086052" FT CONFLICT 380 FT /note="N -> S (in Ref. 2; CAB95124)" FT /evidence="ECO:0000305" FT CONFLICT 382 FT /note="A -> S (in Ref. 3; AAF80348)" FT /evidence="ECO:0000305" FT CONFLICT 399 FT /note="D -> H (in Ref. 3; AAF80348)" FT /evidence="ECO:0000305" FT STRAND 9..14 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 16..18 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 23..25 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 27..31 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 34..41 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 49..52 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 62..67 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 82..91 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 94..101 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 109..120 FT /evidence="ECO:0007829|PDB:4B91" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 125..133 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 139..151 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 156..161 FT /evidence="ECO:0007829|PDB:4B91" FT TURN 164..166 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 171..183 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 187..191 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 195..207 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 215..218 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 223..239 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 251..262 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 267..272 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 273..277 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 280..284 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 288..292 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 306..315 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 321..323 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 331..334 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 341..343 FT /evidence="ECO:0007829|PDB:4B91" FT TURN 351..353 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 354..362 FT /evidence="ECO:0007829|PDB:4B91" FT TURN 363..366 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 370..377 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 379..384 FT /evidence="ECO:0007829|PDB:4B91" FT TURN 388..390 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 402..406 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 415..417 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 420..423 FT /evidence="ECO:0007829|PDB:4B91" FT TURN 426..429 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 435..441 FT /evidence="ECO:0007829|PDB:4B91" FT STRAND 444..448 FT /evidence="ECO:0007829|PDB:4B91" FT HELIX 469..478 FT /evidence="ECO:0007829|PDB:4B91" SQ SEQUENCE 564 AA; 61421 MW; FF9DD1D44C599928 CRC64; MLANSASVRI LIKGGKVVND DCTHEADVYI ENGIIQQVGR ELMIPGGAKV IDATGKLVIP GGIDTSTHFH QTFMNATCVD DFYHGTKAAL VGGTTMIIGH VLPDKETSLV DAYEKCRGLA DPKVCCDYAL HVGITWWAPK VKAEMETLVR EKGVNSFQMF MTYKDLYMLR DSELYQVLHA CKDIGAIARV HAENGELVAE GAKEALDLGI TGPEGIEISR PEELEAEATH RVITIANRTH CPIYLVNVSS ISAGDVIAAA KMQGKVVLAE TTTAHATLTG LHYYHQDWSH AAAYVTVPPL RLDTNTSTYL MSLLANDTLN IVASDHRPFT TKQKAMGKED FTKIPHGVSG VQDRMSVIWE RGVVGGKMDE NRFVAVTSSN AAKLLNLYPR KGRIIPGADA DVVVWDPEAT KTISASTQVQ GGDFNLYENM RCHGVPLVTI SRGRVVYENG VFMCAEGTGK FCPLRSFPDT VYKKLVQREK TLKVRGVDRT PYLGDVAVVV HPGKKEMGTP LADTPTRPVT RHGGMRDLHE SSFSLSGSQI DDHVPKRASA RILAPPGGRS SGIW //