DPYL4_MOUSE
ID DPYL4_MOUSE Reviewed; 572 AA.
AC O35098; O08886; Q3UL94;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
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 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 [MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RA Hamajima N., Kato Y., Kouwaki M., Wada Y., Sasaski M., Nonaka M.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=ICR; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
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 PROTEIN SEQUENCE OF 346-361, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH DPYSL2.
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 [6]
RP SUBUNIT.
RX PubMed=10956643; DOI=10.1074/jbc.m003277200;
RA Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A.,
RA Matsuda Y., Noda M.;
RT "Molecular characterization of CRMP5, a novel member of the collapsin
RT response mediator protein family.";
RL J. Biol. Chem. 275:37957-37965(2000).
RN [7]
RP INTERACTION WITH PLEXA1, AND SUBUNIT.
RX PubMed=14685275; DOI=10.1038/sj.emboj.7600021;
RA Deo R.C., Schmidt E.F., Elhabazi A., Togashi H., Burley S.K.,
RA Strittmatter S.M.;
RT "Structural bases for CRMP function in plexin-dependent semaphorin3A
RT signaling.";
RL EMBO J. 23:9-22(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537 AND SER-544, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, 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).
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 (PubMed:9375656, PubMed:10956643, PubMed:14685275). Interacts
CC with PLEXA1 (PubMed:14685275). Interacts with FLNA (By similarity).
CC {ECO:0000250|UniProtKB:O14531, ECO:0000269|PubMed:10956643,
CC ECO:0000269|PubMed:14685275, ECO:0000269|PubMed:9375656}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O35098-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35098-2; Sequence=VSP_024802;
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; AB006715; BAA21888.1; -; mRNA.
DR EMBL; Y09079; CAA70299.1; -; mRNA.
DR EMBL; AK145638; BAE26556.1; -; mRNA.
DR CCDS; CCDS21951.1; -. [O35098-1]
DR AlphaFoldDB; O35098; -.
DR SMR; O35098; -.
DR IntAct; O35098; 2.
DR MINT; O35098; -.
DR STRING; 10090.ENSMUSP00000026551; -.
DR MEROPS; M38.977; -.
DR iPTMnet; O35098; -.
DR PhosphoSitePlus; O35098; -.
DR SwissPalm; O35098; -.
DR REPRODUCTION-2DPAGE; O35098; -.
DR jPOST; O35098; -.
DR MaxQB; O35098; -.
DR PaxDb; O35098; -.
DR PeptideAtlas; O35098; -.
DR PRIDE; O35098; -.
DR ProteomicsDB; 275400; -. [O35098-1]
DR ProteomicsDB; 275401; -. [O35098-2]
DR UCSC; uc009kfk.2; mouse. [O35098-2]
DR MGI; MGI:1349764; Dpysl4.
DR eggNOG; KOG2584; Eukaryota.
DR InParanoid; O35098; -.
DR PhylomeDB; O35098; -.
DR Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
DR PRO; PR:O35098; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35098; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031005; F:filamin binding; ISO:MGI.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:BHF-UCL.
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 Alternative splicing; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..572
FT /note="Dihydropyrimidinase-related protein 4"
FT /id="PRO_0000165922"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..13
FT /note="MSFQGKKSIPRIT -> MAYKMSQSISVTLGKDIPSRLRCLPQRPLFSLCQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024802"
FT CONFLICT 125..126
FT /note="ER -> DG (in Ref. 2; CAA70299)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="G -> V (in Ref. 2; CAA70299)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="F -> I (in Ref. 2; CAA70299 and 3; BAE26556)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 61962 MW; 37671129FC02C7AF CRC64;
MSFQGKKSIP RITSDRLLIK GGKIVNDDQS FHADLYVEDG LIKQIGENLI VPGGIKTIDA
HGLMVLPGGV DVHTRLQMPV MGMTPADDFC QGTKAALAGG TTMILDHVFP DAGVSLLAAY
EQWRERADSA ACCDYSLHVD IPRWHESTKE ELEALVRDKG VNSFLVFMAY KDRCQCTDGQ
IYEIFSLIRD LGAVAQVHAE NGDIVEEEQK RLLEQGITGP EGHVLSHPEE VEAEAVYRAV
TIAKQANCPL YVTKVMSKGA ADMVAQAKRR GVVVFGEPIT ASLGTDGSHY WSKNWAKAAA
FVTSPPINPD PTTADHLTSL LSSGDLQVTG SAHCTFTTAQ KAVGKDNFTL IPEGVNGIEE
RMSVVWEKCV ASGKMDENEF VAVTSTNAAK IFNFYPRKGR VAVGSDADLV IWNPRATKVF
SAKSHNLNVE YNIFEGVECR GVPTVVISQG RVVLEDGNLL VTPGAGRFIP RKTFPDFVYK
RIKARNRLAE IHGVPRGLYD GPVHEVMLPA KPGSGTQARA SCSGKISVPP VRNLHQSGFS
LSGSQADDHI ARRTAQKIMA PPGGRSNITS LS
