DPYL1_RAT
ID DPYL1_RAT Reviewed; 572 AA.
AC Q62950; P70546;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Dihydropyrimidinase-related protein 1;
DE Short=DRP-1;
DE AltName: Full=Collapsin response mediator protein 1;
DE Short=CRMP-1;
DE AltName: Full=Inactive dihydropyrimidinase {ECO:0000305};
GN Name=Crmp1; Synonyms=Dpysl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8815901; DOI=10.1523/jneurosci.16-19-06197.1996;
RA Wang L., Strittmatter S.M.;
RT "A family of rat CRMP genes is differentially expressed in the nervous
RT system.";
RL J. Neurosci. 16:6197-6207(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Quach T.T., Honnorat J., Aguera M., Belin M.-F., Kolattukudy P.E.,
RA Antoine J.-C.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBUNIT, AND INTERACTION WITH DPYSL2; DPYSL3 AND DPYSL4.
RX PubMed=9375656; DOI=10.1046/j.1471-4159.1997.69062261.x;
RA Wang L.H., Strittmatter S.M.;
RT "Brain CRMP forms heterotetramers similar to liver dihydropyrimidinase.";
RL J. Neurochem. 69:2261-2269(1997).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-521 AND SER-522, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP INTERACTION WITH FLNA, AND DEVELOPMENTAL STAGE.
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 (By similarity). Plays a role in axon
CC guidance (By similarity). During the axon guidance process, acts
CC downstream of SEMA3A to promote FLNA dissociation from F-actin which
CC results in the rearrangement of the actin cytoskeleton and the collapse
CC of the growth cone (By similarity). Involved in invasive growth and
CC cell migration. May participate in cytokinesis (By similarity).
CC {ECO:0000250|UniProtKB:P97427, ECO:0000250|UniProtKB:Q14194}.
CC -!- SUBUNIT: Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4
CC or DPYSL5 (By similarity). Interacts with PLXNA1 (By similarity).
CC Interacts with FLNA (via calponin-homology (CH) domain 1 and filamin
CC repeat 24); the interaction alters FLNA ternary structure and thus
CC promotes FLNA dissociation from F-actin (PubMed:25358863).
CC {ECO:0000250|UniProtKB:P97427, ECO:0000269|PubMed:25358863}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14194}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q14194}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q14194}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:P97427}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P97427}. Perikaryon
CC {ECO:0000250|UniProtKB:P97427}. Note=Associated with centrosomes and
CC the mitotic spindle during metaphase (By similarity). Colocalizes with
CC FLNA and tubulin in the central region of DRG neuron growth cone.
CC Following SEMA3A stimulation of DRG neurons, colocalizes with F-actin
CC (By similarity). {ECO:0000250|UniProtKB:P97427,
CC ECO:0000250|UniProtKB:Q14194}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the brain of 20 dpc embryos.
CC {ECO:0000269|PubMed:25358863}.
CC -!- PTM: Phosphorylation at Ser-522 enhances CRMP1-mediated alteration of
CC FLNA ternary structure and FLNA dissociation from F-actin.
CC {ECO:0000250|UniProtKB:Q14194}.
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; U52102; AAB03280.1; -; mRNA.
DR EMBL; U52095; AAB07042.1; -; mRNA.
DR RefSeq; NP_037064.1; NM_012932.2.
DR AlphaFoldDB; Q62950; -.
DR SMR; Q62950; -.
DR BioGRID; 247450; 5.
DR IntAct; Q62950; 5.
DR MINT; Q62950; -.
DR STRING; 10116.ENSRNOP00000063671; -.
DR MEROPS; M38.974; -.
DR iPTMnet; Q62950; -.
DR PhosphoSitePlus; Q62950; -.
DR World-2DPAGE; 0004:Q62950; -.
DR jPOST; Q62950; -.
DR PaxDb; Q62950; -.
DR PRIDE; Q62950; -.
DR Ensembl; ENSRNOT00000065334; ENSRNOP00000063671; ENSRNOG00000004781.
DR GeneID; 25415; -.
DR KEGG; rno:25415; -.
DR CTD; 1400; -.
DR RGD; 2407; Crmp1.
DR eggNOG; KOG2584; Eukaryota.
DR GeneTree; ENSGT01030000234527; -.
DR HOGENOM; CLU_015572_2_2_1; -.
DR InParanoid; Q62950; -.
DR OMA; IKYPMGK; -.
DR OrthoDB; 719800at2759; -.
DR PhylomeDB; Q62950; -.
DR Reactome; R-RNO-399956; CRMPs in Sema3A signaling.
DR PRO; PR:Q62950; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000004781; Expressed in frontal cortex and 13 other tissues.
DR Genevisible; Q62950; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0030426; C:growth cone; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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; ISO:RGD.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:InterPro.
DR GO; GO:1904530; P:negative regulation of actin filament binding; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR GO; GO:0048666; P:neuron development; IEP:RGD.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISO:RGD.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR030624; CRMP1.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF54; PTHR11647:SF54; 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 Cell projection; Cytoplasm; Cytoskeleton; Nitration; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..572
FT /note="Dihydropyrimidinase-related protein 1"
FT /id="PRO_0000165911"
FT REGION 509..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 246..247
FT /note="Required for interaction with FLNA"
FT /evidence="ECO:0000250|UniProtKB:Q14194"
FT COMPBIAS 525..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14194"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14194"
FT MOD_RES 316
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97427"
FT MOD_RES 504
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P97427"
FT MOD_RES 509
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P97427"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97427"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97427"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97427"
FT CONFLICT 3
FT /note="H -> Y (in Ref. 2; AAB07042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 62196 MW; ED63BD8C751CCFDF CRC64;
MSHQGKKSIP HITSDRLLIR GGRIINDDQS FYADVYLEDG LIKQIGENLI VPGGVKTIEA
NGRMVIPGGI DVNTYLQKPS QGMTSADDFF QGTRAALAGG TTMIIDHVVP EPGSSLLTSF
EKWHEAADTK SCCDYSLHVD ITSWYDGVRE ELEVLVQDKG VNSFQVYMAY KDLYQMSDSQ
LYEAFTFLKG LGAVILVHAE NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI
AIAGRINCPV YITKVMSKSA ADIIALARKK GPLVFGEPIA ASLGTDGTHY WSKNWAKAAA
FVTSPPLSPD PTTPDYLTSL LACGDLQVTG SGHCPYSTAQ KAVGKDNFTL IPEGVNGIEE
RMTVVWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDADVV IWDPDKMKTL
TAKSHKSTVE YNIFEGMECH GSPLVVISQG KIVFEDGNIS VSKGMGRFIP RKPFPEHLYQ
RVRIRSKVFG LHSVSRGMYD GPVYEVPATP KHAAPAPSAK SSPSKHQPPP IRNLHQSNFS
LSGAQIDDNN PRRTGHRIVA PPGGRSNITS LG
