ID A0A2U3WYF9_ODORO Unreviewed; 687 AA.
AC A0A2U3WYF9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Dihydropyrimidinase-related protein 3 isoform X1 {ECO:0000313|RefSeq:XP_004414687.1};
GN Name=DPYSL3 {ECO:0000313|RefSeq:XP_004414687.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004414687.1};
RN [1] {ECO:0000313|RefSeq:XP_004414687.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00025548}.
CC -!- SUBCELLULAR LOCATION: Cell projection, growth cone
CC {ECO:0000256|ARBA:ARBA00004624}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family.
CC {ECO:0000256|ARBA:ARBA00008829}.
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DR RefSeq; XP_004414687.1; XM_004414630.2.
DR AlphaFoldDB; A0A2U3WYF9; -.
DR STRING; 9708.A0A2U3WYF9; -.
DR GeneID; 101382773; -.
DR KEGG; oro:101382773; -.
DR CTD; 1809; -.
DR InParanoid; A0A2U3WYF9; -.
DR OrthoDB; 1772494at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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:SF57; DIHYDROPYRIMIDINASE-RELATED PROTEIN 3; 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.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Reference proteome {ECO:0000313|Proteomes:UP000245340}.
FT DOMAIN 181..570
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 74016 MW; FB70D7654736C44F CRC64;
MASGRRGWDS SHEDDLPVYL ARPGTTDQVP RQKYGGMFCN VEGAFESKTL DFDALSVGQR
GAKTPRSGQG SGRGSGSRPG VEGDSPRRGQ GREEGREPAP ASPASPAPAG VEIRSATGKE
VLQNLGPKDK SDRLLIKGGR IVNDDQSFYA DIYMEDGLIK QIGDNLIVPG GVKTIEANGK
MVIPGGIDVH THFQMPYKGM TTVDDFFQGT KAALAGGTTM IIDHVVPEPE ASLTEAYEKW
REWADGKSCC DYALHVDITH WNDSVKQEVQ NLIKDKGVNS FMVYMAYKDL YQVSNTELYE
IFTCLGELGA IAQVHAENGD IIAQEQTRML EMGITGPEGH VLSRPEELEA EAVFRAITIA
SQTNCPLYVT KVMSKSAADL ISQARKKGNV VFGEPITASL GTDGTHYWSK NWAKAAAFVT
SPPLSPDPTT PDYINSLLAS GDLQLSGSAH CTFSTAQKAI GKDNFTAIPE GTNGVEERMS
VIWDKAVATG KMDENQFVAV TSTNAAKIFN LYPRKGRISV GSDSDLVIWD PDAVKIVSAK
NHQSAAEYNI FEGLELRGAP LVVICQGKIM LEDGNLHVTQ GAGRFIPCSP FSDYVYKRIK
ARRKMADLHA VPRGLYDGPV FDLTTTPKGG TPAGSTRGSP TRPNPPVRNL HQSGFSLSGT
QVDEGVRSAS KRIVAPPGGR SNITSLS
//