Entry
stringlengths
6
10
Entry Name
stringlengths
5
11
Sequence
stringlengths
2
35.2k
EC number
stringlengths
7
118
Cofactor
stringlengths
38
1.77k
Gene Ontology (biological process)
stringlengths
18
11.3k
Gene Ontology (cellular component)
stringlengths
17
1.75k
Gene Ontology (molecular function)
stringlengths
24
2.09k
Pfam
stringlengths
8
232
Gene3D
stringlengths
10
250
Protein families
stringlengths
9
237
Post-translational modification
stringlengths
16
8.52k
Subcellular location [CC]
stringlengths
29
6.18k
Catalytic activity
stringlengths
64
35.7k
Kinetics
stringlengths
69
11.7k
Pathway
stringlengths
27
908
pH dependence
stringlengths
64
955
Temperature dependence
stringlengths
70
1.16k
Function [CC]
stringlengths
17
15.3k
Organism
stringlengths
8
196
B3H754
APD3_ARATH
MGSIRGDLQPLFVMPPPPLDEDCDDIFNSDESSWGLLSLSCFGIIMGLWFFASVCLIFGVYGSETVWLGPNSSILVKPSSIFVKSIKVKELDFSKPGLQLYGFNGQSTPSGYFVNWTESRVLSVSQNSYKGWPYYLNRGTHMNISYNILPKGSAVRLVITEGSQVIGMPFFYRSSLKDIAFRDTAWSWNLIQGSGMIQLDISKSKGYYLTVANLKRKDIEVELDIDVKAVLYDTKQTSYNCSFSNGECSFKMNERYPVENYAVVTSPALGQGVSIDDEWYIELSYQPRLIAYGSFTGVLLSFMLVAIHFCNKLKCCGGEG...
2.3.2.27
null
mitotic cell cycle [GO:0000278]; pollen development [GO:0009555]; protein ubiquitination [GO:0016567]
endosome [GO:0005768]; plant-type vacuole membrane [GO:0009705]
metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]
PF16041;PF16040;PF13920;
3.30.40.10;
null
null
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250|UniProtKB:Q0WS06}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:Q0WS06}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q6DBH0};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q6DBH0}.
null
null
FUNCTION: Involved in pollen mitosis II (PMII) regulation during male gametogenesis. {ECO:0000269|PubMed:22897245}.
Arabidopsis thaliana (Mouse-ear cress)
B3H7A9
PXG7_ARATH
MSHQTVALASKAKSPKPKRGKLDKEKMTALEKHVSFFDRNKDGTVYPWETYQGFRALGTGRLLAAFVAIFINMGLSKKTRPGKGFSPLFPIDVKNSHLCMHGSDTDVYDDDGRFVESKFEEIFNKHARTHKDALTAEEIQKMLKTNRDPFDITGWLSDYGEWKILHTLAQDKNGLLSEKSVRAIYDGSLFHQLEKKRSSSSSRGKKQKLP
1.11.2.3
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
null
extracellular region [GO:0005576]
18-hydroxyoleate peroxygenase activity [GO:0102070]; calcium ion binding [GO:0005509]; lipase activity [GO:0016298]; monooxygenase activity [GO:0004497]; plant seed peroxidase activity [GO:1990137]
PF05042;
1.10.238.10;
Caleosin family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11431566}.
CATALYTIC ACTIVITY: Reaction=RH + ROOH = ROH + ROH.; EC=1.11.2.3;
null
null
null
null
FUNCTION: Probable calcium-binding peroxygenase. May be involved in pollination.
Arabidopsis thaliana (Mouse-ear cress)
B3H7I1
SOP12_ARATH
MRNTISSKMGQVLIVLLLLCTVLCRTESALPSGQHSVLLTGRRLMGSGASGPVRSSQSSQAGGRFNDADPIAIDYGKY
null
null
cell-cell signaling involved in cell fate commitment [GO:0045168]; defense response to insect [GO:0002213]; indole glucosinolate biosynthetic process [GO:0009759]; jasmonic acid biosynthetic process [GO:0009695]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; plant-type cell wall organiz...
apoplast [GO:0048046]; plasma membrane [GO:0005886]
LRR domain binding [GO:0030275]; receptor serine/threonine kinase binding [GO:0033612]
null
null
Serine rich endogenous peptide (SCOOP) phytocytokine family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:34535661}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:34535661}. Note=The precursor of SCOOP12, PROSCOOP12, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP12 in the apoplasm. {ECO:0000269|PubMed:34535661}.
null
null
null
null
null
FUNCTION: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including root growth prevention, phospholipid signaling pathway activation (e.g....
Arabidopsis thaliana (Mouse-ear cress)
B3KU38
IQIP1_HUMAN
MRLEELKRLQNPLEQVNDGKYSFENHQLAMDAENNIEKYPLNLQPLESKVKIIQRAWREYLQRQEPLGKRSPSPPSVSSEKLSSSVSMNTFSDSSTPDYREDGMDLGSDAGSSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDERDQRGYRDDRSPAREPGDVSARTRSGGGGGRSATTAMPPPVPNGNLHQHDPQDLRHNGNVVVAGRPSCSRGPRRAIQKPQPAGGRRSGRGPAAGGLCLQPPDGGTCVPEEPPVPPMDWEALEKHLAGLQFREQEVRNQ...
null
null
negative regulation of cytoskeleton organization [GO:0051494]; positive regulation of hippo signaling [GO:0035332]
axon initial segment [GO:0043194]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
null
PF15157;PF10148;
null
null
null
SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250|UniProtKB:A0A088MLT8}. Cytoplasm {ECO:0000269|PubMed:17045569}. Note=Localizes to the axon initial segments (AIS) and nodes of Ranvier of neurons and is absent from dendrites. {ECO:0000250|UniProtKB:A0A088MLT8}.
null
null
null
null
null
FUNCTION: May play a role in action potential conduction in myelinated cells through the organization of molecular complexes at nodes of Ranvier and axon initial segments (PubMed:25950943). May also play a role in axon outgrowth and guidance (By similarity). {ECO:0000250|UniProtKB:A0A088MLT8, ECO:0000269|PubMed:2595094...
Homo sapiens (Human)
B3L2V1
PSD_PLAKH
MKKNGRDNNFYHLYKNKYLITGVTILSFILMFQYKYHEVLTLHDNSENAVQSSKLFWARLLFGRTRSRITGQILKMEIPNTYRLFIFNFLIKYMHINKEEIKYPIESYKSIGDFFSRYIREETRPIGDVSDYSIVSPCDSELIDYGELTSEYLENIKGVKFNVNTFLGSKFQKKHNDGSTKFFYAIFYLSPKKYHHFHAPFNFKYKIRRHISGELFPVFQGMFKFINNLFNINERVILSGEWKGGNVYYAAISAYNVGNIKIINDEELVTNNLRHQLSYMGGDINTKIFDSYKSVEVGDEIGEFRMGSSIVVIFENKKDF...
4.1.1.65
COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:25724650}; Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:25724650};
phosphatidylethanolamine biosynthetic process [GO:0006646]; protein autoprocessing [GO:0016540]
endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739]
phosphatidylserine decarboxylase activity [GO:0004609]
PF02666;
null
Phosphatidylserine decarboxylase family, PSD-B subfamily, Eukaryotic type I sub-subfamily
PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme...
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:22057268}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9GPP8, ECO:0000255|HAMAP-Rule:MF_03208}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Equally found in the membrane-bound as well as in the soluble fraction. {ECO:0000255|HAMAP-Ru...
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:22057268, ECO...
null
PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:22057268}.
null
null
FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:22057268}.
Plasmodium knowlesi (strain H)
B3LF48
EHD2_ARATH
METSSTISIGSCLKEHQKIYKEWFNIADSDGDGRVSGNDATKFFAMSKLSRQELKQVWAVADSKRQGFLGLSEFITAMKLVSLAQEGHEITSDLLKGSIDMKSVELPVLEGLENVVSKQKVSKTNVDVEDNVVTKPQVTAKTPWFKSKSIIKPQVNVVTIVDGLKRLYTEKLKPLEVTYRFNDFASPVLTSSDFDAKPMVMLLGQYSTGKTTFIKHLLGCDYPGAHIGPEPTTDRFVVAMSGPDERTIPGNTMAVQADMPFNGLTSFGGAFLSKFECSQMPHPVLDQITLVDTPGVLSGEKQRMQRSYDFTGVISWFASK...
3.6.5.2
null
endocytosis [GO:0006897]; endosomal transport [GO:0016197]; protein homooligomerization [GO:0051260]; regulation of actin cytoskeleton organization [GO:0032956]
cytoplasm [GO:0005737]; endosome membrane [GO:0010008]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]
calcium ion binding [GO:0005509]; G protein activity [GO:0003925]; GTP binding [GO:0005525]
PF18150;PF00350;PF12763;PF16880;
1.10.268.20;1.10.238.10;3.40.50.300;
TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family, EHD subfamily
null
SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q641Z6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q641Z6}. Cell membrane {ECO:0000269|PubMed:18547399, ECO:0000269|PubMed:19936242}; Peripheral membrane protein {ECO:0000269|PubMed:18547399, ECO:0000269|PubMed:19936242}; Cytoplasmic side {ECO:0000...
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU00758};
null
null
null
null
FUNCTION: Involved in endocytosis negative regulation, probably by influencing actin organization. Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes. Exhibits an inhibitory effect on endocytosis when over-expressed. {ECO:0000269|PubMed:18547399, ECO:0000269|PubMed:19936242}.
Arabidopsis thaliana (Mouse-ear cress)
B3LGE9
ARO1_YEAS1
MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGEKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQ...
1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]
3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476...
PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202;
3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300;
Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr...
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st...
null
null
FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast)
B3LV44
HH_DROAN
MDNSDCRVPWASAPSSMTCLSLDPTKCHSSSSSSKCQPDCDTPPAAEKIQRHIAYTQRCPGKITTLLAVLLLVLPLSFTPAHSCGPGRGLGRRRERNLYPLVLKQTIPNLSEYTSGASGPLEGPIRRDSPKFKDLVPNYNRDILFRDDEGTGADRLMSKRCKEKLNVLAYSVMNEWPGVRLLVAESWDEDYQHGKESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSISSHVHGCFTPESTALLEGGVRKPLGELSIGDRVLSMTSNGQPVYSEVILFMDRNLKQMQNFVRLHTAGGA...
3.1.-.-
null
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; cell-cell signaling involved in cell fate commitment [GO:0045168]; intein-mediated protein splicing [GO:0016539]; protein autoprocessing [GO:0016540]; regulation of gene expression [GO:0010468]; segment polarity determination [GO:000...
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
PF01085;PF01079;
3.30.1380.10;2.170.16.10;
Hedgehog family
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results ...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR ...
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI...
null
null
null
null
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that res...
Drosophila ananassae (Fruit fly)
B3M185
RAS1_DROAN
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLASWNVNNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRRGRKMNKPNRRFKCKML
3.6.5.2
null
border follicle cell migration [GO:0007298]; cellular response to starvation [GO:0009267]; chorion-containing eggshell pattern formation [GO:0030381]; defense response to virus [GO:0051607]; determination of adult lifespan [GO:0008340]; dorsal closure, spreading of leading edge cells [GO:0007395]; epidermal growth fact...
membrane [GO:0016020]; plasma membrane [GO:0005886]
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; protein serine/threonine kinase activator activity [GO:0043539]
PF00071;
3.40.50.300;
Small GTPase superfamily, Ras family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08646}; Lipid-anchor {ECO:0000250|UniProtKB:P08646}; Cytoplasmic side {ECO:0000250|UniProtKB:P08646}.
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112};
null
null
null
null
FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormo...
Drosophila ananassae (Fruit fly)
B3M301
SPAST_DROAN
MVRTKNQSSSSSASSSTKSPIKSGSAGSGSAAGGNSASGSRQSTHRSSSASNVASAAAAAVASSNRTRTSPGSSPDGDDDTTTTDDLTPTSCSPRSGHHHHGHPYGGSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNSKDQQQQHQSQPLSYPLELSEGGNPEQQLPSQTQRYRAIQPLEMASNRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREEDLRM...
5.6.1.1
null
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regul...
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
PF00004;PF17862;PF09336;
1.10.8.60;3.40.50.300;1.20.58.80;
AAA ATPase family, Spastin subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-...
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
null
null
null
null
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Inv...
Drosophila ananassae (Fruit fly)
B3M3M6
UBP36_DROAN
MPVSVAVCETTNVVNAALRESLGVGIGSGGASSDDKSAGEDTNSLQNHIVANAKRILMTKIEYEEVPNYQEAVLENLKSKYIVIKPTNPTNGCNLNGNTANTFGNKNNAGKIVGANGHDNNGRKLSDHPNQNHNHANPNGHHANPNELPKPKRVLYPRENIRIGWKQSERKWQVGSGMINAGNTCYLNSTLQALFHIPALANWLVSEQAHMENCNVSESGSFCIICAMAKTLQATQTTQSAVRPFLIYTKLKQICKHMIVGRQEDAHEFLRFLVEAMERAYLMRFRNYKELDQLVKETTPLGQIFGGYLRSEVRCLSCNH...
3.4.19.12
null
germ-line stem cell population maintenance [GO:0030718]; heterochromatin formation [GO:0031507]; negative regulation of antimicrobial peptide production [GO:0002785]; negative regulation of innate immune response [GO:0045824]; negative regulation of macroautophagy [GO:0016242]; negative regulation of peptidoglycan reco...
cytosol [GO:0005829]; nucleolus [GO:0005730]
cysteine-type deubiquitinase activity [GO:0004843]; K63-linked deubiquitinase activity [GO:0061578]
PF00443;
3.90.70.10;
Peptidase C19 family
null
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
null
null
null
null
FUNCTION: Required for maintaining multiple types of adult stem cells, including male and female germline, epithelial follicle cell and intestinal stem cells. May function as a transcriptional repressor by continually deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, thereby prev...
Drosophila ananassae (Fruit fly)
B3M6I4
PLK4_DROAN
MLSNRAFGETIEEYEVQHLLGKGGFASVYKARCLHTHQDVAIKMIDKKLIQGTGLTNRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIGRPFTEAEAASILRQVVAGLLYLHSHNIMHRDISLSNLLLSKEMHVKIADFGLATQLKRPDERHVTMCGTPNYISPEVVSRTSHGLPADVWSVGCMLYTLLVGRPPFETDAVQTTLNKVVLSEYIMPTHLSFEAQDLINKLLKKVPHERIALEHVLRHPFLTKRLENSSNGVYSTPGALNVFSQSLESGDSGIITFASSDSRNSQRLRSVENTA...
2.7.11.21
null
centriole replication [GO:0007099]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of protein catabolic process [GO:0045732]; regulation of centriole replication [GO:0046599]; regulation of protein stability [GO:0031647]; sperm ax...
centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922]
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;PF18190;PF18409;
2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
PTM: Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as sas-6. When overexpressed, it is...
Drosophila ananassae (Fruit fly)
B3MEY6
LIS1_DROAN
MKMVLSQRQREELNQAIADYLGSNGYADSLEAFRKEADLSTEAEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKYSMSGHRASITRVIFHPIFGLVVSASEDATIKIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQTYECVKTMHGHDHNVSSVAFVPAGDYVLSASRDRTVKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDHTIRVWLTNSRDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKT...
null
null
border follicle cell migration [GO:0007298]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]; establishment of mitotic spindle...
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; CIA complex [GO:0097361]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; spindle pole centrosome [GO:00316...
dynein complex binding [GO:0070840]
PF08513;PF00400;
1.20.960.30;2.130.10.10;
WD repeat LIS1/nudF family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
null
null
null
null
null
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
Drosophila ananassae (Fruit fly)
B3MH43
PTK7_DROAN
MAALRISVWILVQALMMALVSSNSSHFLQLPQSQSVVENESVDFECQASTDPSSELHYEWLHNGHRIAYDKRVYQIGSHLHIEAVQRAEDVGDYVCIATSLASGAREASPPAKLSVIYIDSASVQLLGSNRNELLLKCHVEAVSGSDDPLQIEWYRNSAKLSSWQNVQLDQHRLIIRQPSAADDGLYRCTASNAAGRVMSKQGYVYRSSLKCLPRLPRRKNQKLPESWSKEVFLCRGKRGGSGGVEALPSAPEDLRIVQGPASHAIIKEGDPAALTCLYELPAELQNQRIQLRWRKDGKLLRHVELGNSLPLPGISSDSG...
null
null
cell adhesion [GO:0007155]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell axon guidance [GO:0072499...
axon [GO:0030424]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; W...
PF07679;PF13927;PF07714;
2.60.40.10;1.10.510.10;
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}.
null
null
null
null
null
FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in t...
Drosophila ananassae (Fruit fly)
B3MPN6
IRS1_DROAN
MASISDDGMVLSGYHKKLKTMKKKFFVLYEETSINQARLEYYDTEKKFLQRAEPKRVIYLKDCFNINRRLDTKHRFVIVLSSREGGFGIVLESENDLRKWLDKLLLLQRNIANVNGQVYSAYEHVWQVIIQKKGMSEKVGITGTYHCCLSAKSLTFVCIGPEKTANGDDRISSIEILLTTIRRCGHASPQCIFYMELGRQSVLGSGELWMETDNAAIATNMHNTILSAMSAKTDSNTNLINVYQARPDISHEPMRKRSSSANEASKPINVIQNRQNSLELRNCSSPHNYGFPRERCDSLPTRNGTLSESSNQSYFGSNLG...
null
null
cellular response to starvation [GO:0009267]; determination of adult lifespan [GO:0008340]; germ-line stem-cell niche homeostasis [GO:0060250]; glucose homeostasis [GO:0042593]; growth of a germarium-derived egg chamber [GO:0007295]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor s...
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; phosphatidylinositol 3-kinase binding [GO:0043548]
PF02174;
2.30.29.30;
null
null
null
null
null
null
null
null
FUNCTION: Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit. May mediate the control of various cellular processes by insulin-like peptides. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains. Involved in control of cell prol...
Drosophila ananassae (Fruit fly)
B3MRI9
SWS_DROAN
MDVLELLRASATGSYTALFSDAWCQYVSKQITNSMYLYCALGVLSMVFLAWFMYFKRLARIRLRDEASRSMSAVNSSSGGDLRGLRFRKRDKMLFYGRRMLRKMKNVSGQMYSSGKGYKRRAVMRFARRILQLRRDNMPLEMRTVEPPAEYLEETIDGSDRVPPDALYMLQSIRIFGHFEKPVFLRLCKHTQLLELMAGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVTSLLSFIDVLSGNPSYYKTVTAKAIEKSVVIRLPMEAFEEVFQDNPDVMIRVIQVIMIRLQRVLFTALRNYLGLNAE...
3.1.1.5
null
ensheathment of neurons [GO:0007272]; glial cell apoptotic process [GO:0034349]; lipid catabolic process [GO:0016042]; membrane lipid metabolic process [GO:0006643]; membrane organization [GO:0061024]; neuron apoptotic process [GO:0051402]; phosphatidylcholine metabolic process [GO:0046470]; photoreceptor cell maintena...
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; protein kinase A catalytic subunit binding [GO:0034236]
PF00027;PF01734;
3.40.1090.10;2.60.120.10;
NTE family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}.
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969};
null
null
null
null
FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in...
Drosophila ananassae (Fruit fly)
B3N5J3
FICD_DROER
MGTEAEPPSPPSPPAQQQEQANPPVWNAQNQKPARLYRLVLFFIAGSLTAWMFHAFSSSNLAWKLRQLHHLPTAHYLQTRDEFALYSVEELNAFKEFYDKSVSDSVGASFTEAEQTSINEALVSLRMAQDMYLTGKDDKAARLFEHALALAPRHPEVLLRYGEFLEHNQRNIVLADQYYFQALTISPSNSEALANRQRTADVVQNLDQRRLESLDSKRDALSAIHESNAALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKIEITIKDILELHRRVMGHVDPIE...
2.7.7.108; 3.1.4.-
null
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
plasma membrane [GO:0005886]
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
PF02661;
1.10.3290.10;1.25.40.10;
Fic family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV...
null
null
null
null
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-250 determines which of the two op...
Drosophila erecta (Fruit fly)
B3N946
IRS1_DROER
MASISDDGMALSGYLKKLKTMKKKFFVLYEETSNSSARLEYYDTEKKFLQRAEPKRVIYLKNCFNINRRLDTKQRFVIVLSSRDGGFGIVLESENDLRKWLDKLLVLQRNIANTNGTAYSPYDQVWQVVIQKKGISEKVGITGTYHCCLTSKSLTFVCIGPDKTPNGEERVASIEILLTTIRRCGHASPQCIFYVELGRQSVLGSGDLWMETDNAAVATNMHNTILSAMSAKTESNTNLINVYQNRPDLSHEPMRKRSSSANEASKPINVNVIQNSQNSLDLRSCSSPHNYGFGRERCDSLPTRNGTLSESSNQTYFGSN...
null
null
cellular response to starvation [GO:0009267]; determination of adult lifespan [GO:0008340]; germ-line stem-cell niche homeostasis [GO:0060250]; glucose homeostasis [GO:0042593]; growth of a germarium-derived egg chamber [GO:0007295]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor s...
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; phosphatidylinositol 3-kinase binding [GO:0043548]
PF02174;
2.30.29.30;
null
null
null
null
null
null
null
null
FUNCTION: Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit. May mediate the control of various cellular processes by insulin-like peptides. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains. Involved in control of cell prol...
Drosophila erecta (Fruit fly)
B3NC86
UBP36_DROER
MPVSMAVCETANVVNAALRESLGGNSSAAGSSADQAKSGEESNGSLQNHIVANAKRILMAKIEYEEVPNYHESVLESLKSKYIVIKPGNPGAINGFGGKNNTGKVVGANGHDNNGARKQAEHPNNQSHHNNHNNHPHPTSNPNELPKPKRVLYPRENIRIGWKQSERKWQVGTGMINVGNTCYLNSTLQALLHIPALANWLVSEQAHLENCNVAESGGGCIVCAMAKTLLATQSNQSAVRPFLIYSKLKQICKHMVVGRQEDAHEFLRFLVEAMERAYLMRFRNYKELDQLVKETTPLGQIFGGYLRSEVRCLSCNHVSI...
3.4.19.12
null
germ-line stem cell population maintenance [GO:0030718]; heterochromatin formation [GO:0031507]; negative regulation of antimicrobial peptide production [GO:0002785]; negative regulation of innate immune response [GO:0045824]; negative regulation of macroautophagy [GO:0016242]; negative regulation of peptidoglycan reco...
cytosol [GO:0005829]; nucleolus [GO:0005730]
cysteine-type deubiquitinase activity [GO:0004843]; K63-linked deubiquitinase activity [GO:0061578]
PF00443;
3.90.70.10;
Peptidase C19 family
null
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
null
null
null
null
FUNCTION: Required for maintaining multiple types of adult stem cells, including male and female germline, epithelial follicle cell and intestinal stem cells. May function as a transcriptional repressor by continually deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, thereby prev...
Drosophila erecta (Fruit fly)
B3NE99
PLK4_DROER
MLSNRAFGETIEDYEVQHLLGKGGFAIVYKARCLHTHQDVAIKMIDKKLIQGTGLTNRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIARPFTETEAASILKQVVAGLLYLHSHNIMHRDISLSNLLLSKEMHVKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRSSHGLPADVWSVGCMLYTLLVGRPPFETDAVQSTLNKVVMSEYIMPAHLSYEAQDLINKLLKKLPHERITLEAVLCHPFMLKCSNGGHSTPGALNMFSQSMESGDSGIITFASSDSRNSQQIRSVENSGPQQV...
2.7.11.21
null
centriole replication [GO:0007099]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of protein catabolic process [GO:0045732]; regulation of centriole replication [GO:0046599]; regulation of protein stability [GO:0031647]; sperm ax...
centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922]
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;PF18190;PF18409;
2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
PTM: Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as sas-6. When overexpressed, it is...
Drosophila erecta (Fruit fly)
B3NPW0
LIS1_DROER
MKMVLSQRQREELNQAIADYLGSNGYADSLETFRKEADLSTEVEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKFSLTGHRASITRVIFHPIFGLMVSASEDATIRIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQSYECIKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDQTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKT...
null
null
border follicle cell migration [GO:0007298]; brain morphogenesis [GO:0048854]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]...
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cytoplasmic microtubule [GO:0005881]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; nuclear envelope [GO:...
dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010]
PF08513;PF00400;
1.20.960.30;2.130.10.10;
WD repeat LIS1/nudF family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
null
null
null
null
null
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
Drosophila erecta (Fruit fly)
B3NS99
PTK7_DROER
MTARMISIYGLVLASMMASVWASSSRFQRLPQSQSVVENESVKFECESTDSYSELHYDWLHNGHRIAYDKRVHQIGSNLHIEAARRTEDVGSYVCIATNLASGAREASPPAKLSVIYLESASVQLLGSNRNELLLKCHVEGASGDSEPLEIEWYRNSEKLSTWKNVQLDQHRLIIRQPGSDDDGLYRCTASNAAGRVMSKQGYAYQSSVKCLPRLARRKNQKMMESWDKQTFLCRGKRGGAAGLEALPAAPEDLRIVQGPVGQSIIKEGEPTALTCLYELPDELKNQRIQLRWRKDGKLLRQVELGGSAPITGHSFDSGK...
null
null
cell adhesion [GO:0007155]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell axon guidance [GO:0072499...
axon [GO:0030424]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; W...
PF07679;PF13927;PF07714;
2.60.40.10;1.10.510.10;
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}.
null
null
null
null
null
FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in t...
Drosophila erecta (Fruit fly)
B3NY03
SWS_DROER
MDVLEMLRASASGSYNTIFSEAWCQYVSKQITATMYMYCALGMMGVLFLAWFMYFKRMARLRLRDEIARSISAVTNSSGDLRGLRFRKRDKMLFYGRRMLRKMKNVSGQMYSSGKGYKRRAVMRFARRILQLRRDNMPLEMRTVEPPAEYLEETIEGSDRVPPDALYMLQSIRIFGHFEKPVFLRLCKHTQLLELMAGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVTSLLSFIDVLSGNPSYYKTVTAKAIEKSVVIRLPMQAFEEVFQDNPDVMIRVIQVIMIRLQRVLFTALRNYLGLNAEL...
3.1.1.5
null
ensheathment of neurons [GO:0007272]; glial cell apoptotic process [GO:0034349]; lipid catabolic process [GO:0016042]; membrane lipid metabolic process [GO:0006643]; membrane organization [GO:0061024]; neuron apoptotic process [GO:0051402]; phosphatidylcholine metabolic process [GO:0046470]; photoreceptor cell maintena...
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; protein kinase A catalytic subunit binding [GO:0034236]
PF00027;PF01734;
3.40.1090.10;2.60.120.10;
NTE family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}.
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969};
null
null
null
null
FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in...
Drosophila erecta (Fruit fly)
B3NZR4
RAS1_DROER
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLASWNVNNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRRGRKMNKPNRRFKCKML
3.6.5.2
null
border follicle cell migration [GO:0007298]; cellular response to starvation [GO:0009267]; chorion-containing eggshell pattern formation [GO:0030381]; defense response to virus [GO:0051607]; determination of adult lifespan [GO:0008340]; dorsal closure, spreading of leading edge cells [GO:0007395]; epidermal growth fact...
membrane [GO:0016020]; plasma membrane [GO:0005886]
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; protein serine/threonine kinase activator activity [GO:0043539]
PF00071;
3.40.50.300;
Small GTPase superfamily, Ras family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08646}; Lipid-anchor {ECO:0000250|UniProtKB:P08646}; Cytoplasmic side {ECO:0000250|UniProtKB:P08646}.
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112};
null
null
null
null
FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormo...
Drosophila erecta (Fruit fly)
B3P7F8
HH_DROER
MDNTSSVPWASAASVTCLSLDAKCHSSSAKSAASSISASPETQAMRHIAHTQRCLSRLTSLVALLLIVLPMTFSPAHSCGPGRGLGRHRARNLYPLVLKQTIPNLSEYTNSASGPLEGVIRRDSPKFKDLVPNYNRDILFRDEEGTGADRLMSKRCREKLNLLAYSVMNEWPGIRLLVTESWDEDYHHGQESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSISSHVHGCFTPESTALLENGVRKPLGELSIGDRVLSMTANGQAVYSEVILFMDRNLEQMQNFVQLHTDGEAVLTVT...
3.1.-.-
null
Bolwig's organ morphogenesis [GO:0001746]; cell-cell signaling involved in cell fate commitment [GO:0045168]; cytoneme assembly [GO:0035231]; epithelial cell migration, open tracheal system [GO:0007427]; genital disc anterior/posterior pattern formation [GO:0035224]; glial cell migration [GO:0008347]; gonadal mesoderm ...
cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
PF01085;PF01079;
3.30.1380.10;2.170.16.10;
Hedgehog family
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results ...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR ...
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI...
null
null
null
null
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that res...
Drosophila erecta (Fruit fly)
B3P8A3
SPAST_DROER
MVRTKNQSSSSSASSSSTKSPIKSSSGAGSSGGGVGGRQSTHRSSSASNVAAVVAGGSSAAGGGSSSNRRSPGSSPDGDDDTTTTDDLTPTTCSPRSGHHHTYGGYSSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNSSKEQQQSLNHPSELSREGDGQEQQLSNQPQRFRPIQPLEMAANRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREQDLQMQRL...
5.6.1.1
null
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regul...
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
PF00004;PF17862;PF09336;
1.10.8.60;3.40.50.300;1.20.58.80;
AAA ATPase family, Spastin subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-...
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
null
null
null
null
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Inv...
Drosophila erecta (Fruit fly)
B3PC73
AGUA_CELJU
MSTFARLFLCLVFFASLQPAMAQTEDGYDMWLRYQPIADQTLLKTYQKQIRHLHVAGDSPTINAAAAELQRGLSGLLNKPIVARDEKLKDYSLVIGTPDNSPLIASLNLGERLQALGAEGYLLEQTRINKRHVVIVAANSDVGVLYGSFHLLRLIQTQHALEKLSLSSAPRLQHRVVNHWDNLNRVVERGYAGLSLWDWGSLPNYLAPRYTDYARINASLGINGTVINNVNADPRVLSDQFLQKIAALADAFRPYGIKMYLSINFNSPRAFGDVDTADPLDPRVQQWWKTRAQKIYSYIPDFGGFLVKADSEGQPGPQGY...
3.2.1.131
null
glucuronoxylan catabolic process [GO:2000886]
cell outer membrane [GO:0009279]; extracellular region [GO:0005576]
alpha-glucuronidase activity [GO:0046559]; xylan alpha-1,2-glucuronosidase activity [GO:0033939]
PF07477;PF07488;PF03648;
3.90.1330.10;3.30.379.10;3.20.20.80;
Glycosyl hydrolase 67 family
null
SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:12169619}.
CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->2)-alpha-D-(4-O-methyl)glucuronosyl links in the main chain of hardwood xylans.; EC=3.2.1.131; Evidence={ECO:0000269|PubMed:12169619};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.28 mM for aldotriouronic acid (at 37 degrees Celsius) {ECO:0000269|PubMed:11937059, ECO:0000269|PubMed:12654910}; KM=0.36 mM for aldotetraouronic acid (at 37 degrees Celsius) {ECO:0000269|PubMed:11937059, ECO:0000269|PubMed:12654910}; KM=0.42 mM for aldopentaouro...
null
null
null
FUNCTION: Alpha-glucuronidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. It catalyzes the cleavage of the alpha-1,2-glycosidic bond at the non-reducing end of 4-O-meth...
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
B3STU4
VCL_CARIL
MVTKAKIPLFLFLSALFLALVCSSLALETEDLSNELNPHHDPESHRWEFQQCQERCQHEERGQRQAQQCQRRCEEQLREREREREREEIVDPREPRKQYEQCRETCEKQDPRQQPQCERRCERQFQEQQERERRERRRGRDDDDKENPRDPREQYRQCEEHCRRQGQGQRQQQQCQSRCEERFEEEQRRQEERERRRGRDNDDEENPRDPREQYRQCQEHCRRQGQGQRQQQQCQSRCEERLEEEQRKQEERERRRGRDEDDQNPRDPEQRYEQCQQQCERQRRGQEQQLCRRRCEQQRQQEERERQRGRDRQDPQQQYH...
null
null
protein homotrimerization [GO:0070207]; seed development [GO:0048316]; seed maturation [GO:0010431]
null
copper ion binding [GO:0005507]; nutrient reservoir activity [GO:0045735]
PF00190;PF04702;
6.10.250.890;2.60.120.10;
7S seed storage protein family
null
null
null
null
null
null
null
FUNCTION: Seed storage protein. {ECO:0000305|PubMed:25084379, ECO:0000305|PubMed:27128197}.
Carya illinoinensis (Pecan)
B3SV56
NR1D1_SHEEP
MTTLDSNNNTGGVITYIGSSGSSPNRTSPESLYSDSSNGSFQSLTQGCPTYFPPSPTGSLTQDPARSFGSIPPSLGDDGSPSSSSSSSSSSSSSFYNGSPPGGLQVALEDGNRVSPSKSTSNITKLNGMVLLCKVCGDVASGFHYGVHACEGCKGFFRRSIQQNIQYKRCLKNENCSIVRINRNRCQQCRFKKCLSVGMSRDAVRFGRIPKREKQRMLAEMQSAMNLANNQLSSQCPLETPPTQHPTPGPMGPSPPPAPAPSPLVGFSQFPQQLTPPRSPSPEPTVEDVISQVARAHREIFTYAHDKLGTSPGNFNANHA...
null
null
cell differentiation [GO:0030154]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cholesterol homeostasis [GO:0042632]; circadian regulation of gene expression [GO:0032922]; circadian temperature homeostasis [GO:0060086]; glycogen biosynthetic process [GO:00059...
cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; nucleus [GO:0005634]
E-box binding [GO:0070888]; nuclear receptor activity [GO:0004879]; transcription corepressor binding [GO:0001222]; zinc ion binding [GO:0008270]
PF00104;PF00105;
3.30.50.10;1.10.565.10;
Nuclear hormone receptor family, NR1 subfamily
PTM: Ubiquitinated, leading to its proteasomal degradation (By similarity). Ubiquitinated by the SCF(FBXW7) complex when phosphorylated by CDK1 leading to its proteasomal degradation (By similarity). Ubiquitinated by SIAH2; leading to its proteasomal degradation (By similarity). Rapidly ubiquitinated in response to inf...
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250|UniProtKB:Q3UV55}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q3UV55}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q3UV55}. Note=Localizes to the cytoplasm, dendrites and dendritic spine in the presence of OPH...
null
null
null
null
null
FUNCTION: Transcriptional repressor which coordinates circadian rhythm and metabolic pathways in a heme-dependent manner. Integral component of the complex transcription machinery that governs circadian rhythmicity and forms a critical negative limb of the circadian clock by directly repressing the expression of core c...
Ovis aries (Sheep)
B3TLD6
LNBB_BIFB1
MEKSSNRRFGVRTVAAIVAGLMVGGMCTAMTASAADDSAAGYSATAPVNLTRPATVPSMDGWTDGTGAWTLGEGTRVVSSDALAARAQSLASELTKFTDVDIKAATGSATGKDISLTLDASKKAELGDEGFKLNIGSKGLEVIGATDIGVFYGTRSVSQMLRQGQLTLPAGTVATKPKYKERGATLCACQINISTDWIDRFLSDMADLRLNYVLLEMKLKPEEDNTKKAATWSYYTRDDVKKFVKKANNYGIDVIPEINSPGHMNVWLENYPEYQLADNSGRKDPNKLDISNPEAVKFYKTLIDEYDGVFTTKYWHMGAD...
3.2.1.140
null
carbohydrate metabolic process [GO:0005975]
plasma membrane [GO:0005886]
beta-N-acetylhexosaminidase activity [GO:0004563]; lacto-N-biosidase activity [GO:0047403]; N-acetyl-beta-D-galactosaminidase activity [GO:0102148]
PF02368;PF00754;PF00728;PF02838;PF14200;
2.60.40.1080;2.80.10.50;3.30.379.10;2.60.120.260;3.20.20.80;
Glycosyl hydrolase 20 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}; Extracellular side {ECO:0000305|PubMed:18469123}.
CATALYTIC ACTIVITY: Reaction=beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc + H2O = beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine + lactose; Xref=Rhea:RHEA:21568, ChEBI:CHEBI:15377, ChEBI:CHEBI:17716, ChEBI:CHEBI:27707, ChEBI:CHEBI:30248; EC=3.2.1.140; Evidence={ECO:0000269|PubMed:18469123, ECO:000026...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=626 uM for lacto-N-tetraose {ECO:0000269|PubMed:23479733}; KM=68 uM for chromogenic LNB-beta-pNP (beta-D-Gal-(1->3)-beta-D-GlcNAc-pNP) {ECO:0000269|PubMed:18469123}; Note=kcat is 41.1 sec(-1) with lacto-N-tetraose as substrate (PubMed:23479733). kcat is 89 sec(-1) ...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 with LNB-beta-pNP as substrate and pH 6.0 with PA-lacto-N-tetraose. {ECO:0000269|PubMed:18469123};
null
FUNCTION: Present in the infant gut, this enzyme is involved in the assimilation of type-1 human milk oligosaccharides (HMOs). It hydrolyzes via a retaining mechanism the beta-D-GlcNAc-(1->3)-beta-D-Gal linkage in lacto-N-tetraose (LNT or beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc), an abundant HMO ...
Bifidobacterium bifidum (strain DSM 20082 / JCM 1254 / BCRC 11844 / KCTC 3440 / E319f (Variant a))
B3TMR8
KIJDR_ACTKI
MENPANANPIRVGVIGCADIAWRRALPALEAEPLTEVTAIASRRWDRAKRFTERFGGEPVEGYPALLERDDVDAVYVPLPAVLHAEWIDRALRAGKHVLAEKPLTTDRPQAERLFAVARERGLLLMENFMFLHHPQHRQVADMLDEGVIGEIRSFAASFTIPPKPQGDIRYQADVGGGALLDIGVYPIRAAGLFLGADLEFVGAVLRHERDRDVVVGGNALLTTRQGVTAQLTFGMEHAYTNNYEFRGSTGRLWMNRVFTPPATYQPVVHIERQDHAEQFVLPAHDQFAKSIRAFAQAVLSGEHPREWSEDSLRQASLVD...
1.1.1.384
null
antibiotic biosynthetic process [GO:0017000]; D-xylose catabolic process [GO:0042843]
null
D-xylose 1-dehydrogenase (NADP+) activity [GO:0047837]; nucleotide binding [GO:0000166]
PF01408;PF02894;
3.40.50.720;
Gfo/Idh/MocA family
null
null
CATALYTIC ACTIVITY: Reaction=dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP(+) = dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H(+) + NADPH; Xref=Rhea:RHEA:44624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:84537, ChEBI:CHEBI:84540; EC=1.1.1.384; Evidence={ECO:0000269|PubMed:21598943};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=116.4 uM for dTDP-glucose {ECO:0000269|PubMed:21598943}; KM=6.31 mM for NADPH {ECO:0000269|PubMed:21598943}; Vmax=0.01 mmol/min/mg enzyme {ECO:0000269|PubMed:21598943}; Note=kcat is 6.24 sec(-1) for dTDP-glucose as substrate. {ECO:0000269|PubMed:21598943};
PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:21598943}.
null
null
FUNCTION: Involved in the biosynthesis of L-digitoxose, an unusual dideoxysugar attached to various pharmacologically active natural products, including the antitumor antibiotic tetrocarcin A, and the antibiotics kijanimicin and jadomycin B. Catalyzes the reduction of the C-3 keto moiety of dTDP-3,4-diketo-2,6-dideoxy-...
Actinomadura kijaniata
B3TP03
CTR2_CHICK
MLPCGPALTFVRCLVRKKNIKGEGLEDSLCRCLSTLDLIALGVGSTLGAGVYVLAGEVAKSDSGPSIVVSFLIAALASVMAGLCYAEFGARVPKTGSAYLYTYVAVGELWAFITGWNLILSYVIGTSSVARAWSGTFDELLGKQISHFFKTYFKMNYPGLAEYPDFFAVFLILLLSGLLSFGVKESAWVNKIFTAINILVLLFVMISGFVKGDVDNWRISEEYLINLSEIAENFSSYKNVTSIYGSGGFMPYGFTGTLAGAATCFYAFVGFDCIATTGEEVRNPQKAIPIGIVVSLLVCFMAYFGVSAALTLMMPYYLLD...
null
null
L-arginine import across plasma membrane [GO:0097638]; L-lysine import across plasma membrane [GO:0097639]; L-ornithine transmembrane transport [GO:1903352]
cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]
L-arginine transmembrane transporter activity [GO:0061459]; L-lysine transmembrane transporter activity [GO:0015189]; L-ornithine transmembrane transporter activity [GO:0000064]
PF13520;PF13906;
1.20.1740.10;
Amino acid-polyamine-organocation (APC) superfamily, Cationic amino acid transporter (CAT) (TC 2.A.3.3) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18581}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18581}.
CATALYTIC ACTIVITY: Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143, ChEBI:CHEBI:32682; Evidence={ECO:0000250|UniProtKB:P18581}; CATALYTIC ACTIVITY: Reaction=L-lysine(in) = L-lysine(out); Xref=Rhea:RHEA:70935, ChEBI:CHEBI:32551; Evidence={ECO:0000250|UniProtKB:P18581}; CATALYTIC ACTIVITY: Reaction=L-orn...
null
null
null
null
FUNCTION: Low-affinity, high capacity permease involved in the transport of the cationic amino acids (L-arginine, L-lysine, L-ornithine and L-homoarginine). {ECO:0000250|UniProtKB:P18581, ECO:0000250|UniProtKB:P52569}.
Gallus gallus (Chicken)
B3VI55
LGK_LIPST
MPIATSTGDNVLDFTVLGLNSGTSMDGIDCALCHFYQKTPDAPMEFELLEYGEVPLAQPIKQRVMRMILEDTTSPSELSEVNVILGEHFADAVRQFAAERNVDLSTIDAIASHGQTIWLLSMPEEGQVKSALTMAEGAILASRTGITSITDFRISDQAAGRQGAPLIAFFDALLLHHPTKLRACQNIGGIANVCFIPPDVDGRRTDEYYDFDTGPGNVFIDAVVRHFTNGEQEYDKDGAMGKRGKVDQELVDDFLKMPYFQLDPPKTTGREVFRDTLAHDLIRRAEAKGLSPDDIVATTTRITAQAIVDHYRRYAPSQEI...
2.7.1.232
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:26354439, ECO:0000269|PubMed:28196882}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:26354439, ECO:0000269|PubMed:28196882};
amino sugar metabolic process [GO:0006040]; peptidoglycan turnover [GO:0009254]; phosphorylation [GO:0016310]
null
ATP binding [GO:0005524]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]
PF03702;
3.30.420.40;
Anhydro-N-acetylmuramic acid kinase family
null
null
CATALYTIC ACTIVITY: Reaction=ATP + H2O + levoglucosan = ADP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:63428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:30997, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.232; Evidence={ECO:0000269|PubMed:21719279, ECO:0000269|PubMed:26354439, ECO:00002...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=105.3 mM for levoglucosan {ECO:0000269|PubMed:26354439, ECO:0000269|Ref.1}; KM=0.2 mM for ATP {ECO:0000269|Ref.1};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|Ref.1};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|Ref.1};
FUNCTION: Levoglucosan kinase that catalyzes the transfer of a phosphate group from ATP to levoglucosan (1,6-anhydro-beta-D-glucopyranose, LG) to yield glucose 6-phosphate in the presence of magnesium ion and ATP (PubMed:21719279, PubMed:26354439, Ref.1). In addition to the canonical kinase phosphotransfer reaction, th...
Lipomyces starkeyi (Oleaginous yeast)
B3WFY8
DYF5_CAEEL
MSSAVKLADRYLMTKRLGDGTFGEVMLAKKIDTGDRVAIKRMKKKFYSWEEAMSLREVKSLKKLNHPNIIKLREVIRENDILYFVFEFMQENLYELMKDRDRYFPESVIRNIIYQVLQGLAFMHKNGFFHRDMKPENIMCNGTELVKIADFGLAREIRSKPPYTDYVSTRWYRAPEILLRSTSYNSPIDMWALGCIMAELYILRPLFPGTSEMDQLFKIISILGTPNKDEWPEGYQLASAMNFRFQQVVATPMEQVVNTISKEGMKLMMDMMLWNPEKRPNANQSLRYKYFQVAEKLGAPVVSQPAPGSIRKTSAASVKS...
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9JKV2};
cilium assembly [GO:0060271]; intracellular signal transduction [GO:0035556]; intraciliary anterograde transport [GO:0035720]; intraciliary transport [GO:0042073]; negative regulation of non-motile cilium assembly [GO:1902856]; non-motile cilium assembly [GO:1905515]; phosphorylation [GO:0016310]; positive regulation o...
axon [GO:0030424]; cilium [GO:0005929]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; non-motile cilium [GO:0097730]; nucleus [GO:0005634]; perikaryon [GO:0043204]
ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, RCK subfamily
null
SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:17420466}. Cell projection, dendrite {ECO:0000269|PubMed:17420466}. Cell projection, axon {ECO:0000269|PubMed:17420466}. Cell projection, cilium {ECO:0000269|PubMed:17420466}. Note=Enriched at the transition zone between the base of the cilia and the dendrites and to...
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9JKV2}; CATALYTI...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase which is required for ciliogenesis. Regulates the length and the morphology of sensory neuron cilia. In addition, plays a role in the anterograde intraflagellar transport (IFT) in the cilia by regulating the undocking of kinesin-II motor complex (composed of klp-11, klp-20 and ...
Caenorhabditis elegans
B3Y613
TLR2_PANTR
MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDVTSSVECLELRDTDLDTFRFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIP...
null
null
cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; toll-like receptor signaling pathway [GO:0002224]
Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670]
NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]; triacyl lipopeptide binding [GO:0042497]
PF00560;PF13855;PF01463;PF01582;
3.80.10.10;3.40.50.10140;
Toll-like receptor family
PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}.
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts b...
null
null
null
null
null
FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secr...
Pan troglodytes (Chimpanzee)
B3Y614
TLR2_PANPA
MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYESKSLKSIQNVSHLILHMKQHILLLEIFVDVSSSVECLELRDTDLDTFRFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIP...
null
null
cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; toll-like receptor signaling pathway [GO:0002224]
Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670]
NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; transmembrane signaling receptor activity [GO:0004888]; triacyl lipopeptide binding [GO:0042497]
PF00560;PF13855;PF01463;PF01582;
3.80.10.10;3.40.50.10140;
Toll-like receptor family
PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}.
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts b...
null
null
null
null
null
FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secr...
Pan paniscus (Pygmy chimpanzee) (Bonobo)
B3Y615
TLR2_GORGO
MPHTLWMVWVLGVIISLSKEESSNQASLSCDRNGICKGSSGSLNSIPSGLTEAVKSLDLSNNRITYISNSDLQRCVNLQALVLTSNGINTIEEDSFSSLGSLEHLDLSYNYLSNLSSSWFKPLSSLTFLNLLGNPYKTLGETSLFSHLTKLQILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDVTSSVECLELRDTDLDTFHFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLNQISGLLELEFDDCTLNGVGNFRASDNDRVIDPGKVETLTIRRLHIP...
null
null
cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to lipoteichoic acid [GO:0071223]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; cellular response to type II interferon [GO:0071346]; defense response to Gram-positive bacterium [GO:0050830]; defense response to virus ...
cell surface [GO:0009986]; Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670]; Toll-like receptor 1-Toll-like receptor 2 protein complex [GO:0035354]; Toll-like receptor 2-Toll-like receptor 6 protein complex [GO:0035355]
amyloid-beta binding [GO:0001540]; identical protein binding [GO:0042802]; lipopolysaccharide binding [GO:0001530]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; pattern recognition receptor activity [GO:0038187]; peptidoglycan binding [GO:0042834]; protein-containing complex binding [GO:0044877]; signa...
PF00560;PF13855;PF01463;PF01582;
3.80.10.10;3.40.50.10140;
Toll-like receptor family
PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}.
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts b...
null
null
null
null
null
FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secr...
Gorilla gorilla gorilla (Western lowland gorilla)
B3Y618
TLR2_MACMU
MPHTLWMVWVLGVIISLSKEESSNQASLSCDHNGICKGSSGSLNSIPSVLTEAVKCLDLSNNRITYISNSDLQRYVNLQALVLTSNGINTIEEDSFSSLGRLEHLDLSYNYLSNLSSSWFKPLSSLKFLNLLGNPYKTLGETSLFSHLTKLRILRVGNMDTFTKIQRKDFAGLTFLEELEIDASDLQSYEPKSLKSIQNVSHLILHMKQHILLLEIFVDLTSSVECLELRDTDLNTFHFSELSTGETNSLIKKFTFRNVKITDESLFQVMKLLSQISGLLELEFDDCTLNGVGDFRGSDNDRVIDPGKVETLTIRRLHIP...
null
null
cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to triacyl bacterial lipopeptide [GO:0071727]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; toll-like receptor signaling pathway [GO:0002224]
Golgi apparatus [GO:0005794]; membrane raft [GO:0045121]; phagocytic vesicle membrane [GO:0030670]
NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]; triacyl lipopeptide binding [GO:0042497]
PF13855;PF01463;PF01582;
3.80.10.10;3.40.50.10140;
Toll-like receptor family
PTM: Ubiquitinated at Lys-754 by PPP1R11, leading to its degradation. Deubiquitinated by USP2. {ECO:0000250|UniProtKB:Q9QUN7}.; PTM: Glycosylation of Asn-442 is critical for secretion of the N-terminal ectodomain of TLR2. {ECO:0000250|UniProtKB:O60603}.
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q9QUN7}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O60603}. Note=Does not reside in lipid rafts b...
null
null
null
null
null
FUNCTION: Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secr...
Macaca mulatta (Rhesus macaque)
B4EUF7
ENO_PROMH
MSKIVKVLGREIIDSRGNPTVEAEVHLEGGFVGMAAAPSGASTGSREALELRDGDKSRFLGKGVLKAVEAVNGPIAKALLGQDAKDQANIDKIMIDLDGTENKSNFGANAILAVSLANAKAAAAAKGMPLYEHISDLNGTHGQYSMPLPMMNIINGGEHADNNVDIQEFMIQPVGAPTLKEAVRMGSEIFHHLAKVLKAKGMNTAVGDEGGYAPNLESNAAALAAIKEAVEAAGYVLGKDVTLAMDCAASEFYNNETGNYELKGEGKTFTSQEFTHYLEELTKQYLIVSIEDGLNESDWDGFAYQTKVLGDKIQLVGDDL...
4.2.1.11
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00318}; Note=Binds a second Mg(2+) ion via substrate during catalysis. {ECO:0000255|HAMAP-Rule:MF_00318};
glycolytic process [GO:0006096]
cell surface [GO:0009986]; extracellular region [GO:0005576]; phosphopyruvate hydratase complex [GO:0000015]
magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]
PF00113;PF03952;
3.20.20.120;3.30.390.10;
Enolase family
PTM: Acetylated and 2-hydroxyisobutyrylated at Lys-326 and Lys-343, respectively, reducing the enolase activity (PubMed:31328167). Deacetylated and de-2-hydroxyisobutyrylated by NpdA/CobB, increasing the enolase activity (PubMed:31328167). {ECO:0000269|PubMed:31328167}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. {ECO:0000255|HAMAP-Rule:MF_00318}.
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:31328167}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165; Evidence={ECO...
null
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00318}.
null
null
FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP) (PubMed:31328167). It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:31328167}.
Proteus mirabilis (strain HI4320)
B4EY22
CAIT_PROMH
MSKDNKKAGIEPKVFFPPLIIVGILCWLTVRDLDASNEVINAVFSYVTNVWGWAFEWYMVIMFGGWFWLVFGRYAKKRLGDEKPEFSTASWIFMMFASCTSAAVLFWGSIEIYYYISSPPFGMEGYSAPAKEIGLAYSLFHWGPLPWATYSFLSVAFAYFFFVRKMEVIRPSSTLTPLVGEKHVNGLFGTVVDNFYLVALILAMGTSLGLATPLVTECIQYLFGIPHTLQLDAIIISCWILLNAICVAFGLQKGVKIASDVRTYLSFLMLGWVFIVGGASFIVNYFTDSVGTLLMYMPRMLFYTDPIGKGGFPQAWTVFY...
null
null
4-(trimethylammonio)butanoate transport [GO:1900751]; carnitine metabolic process [GO:0009437]
plasma membrane [GO:0005886]
(R)-carnitine:4-(trimethylammonio)butanoate antiporter activity [GO:0044667]
PF02028;
null
BCCT transporter (TC 2.A.15) family, CaiT subfamily
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000269|PubMed:20829798, ECO:0000269|PubMed:24101465}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000269|PubMed:20829798, ECO:0000269|PubMed:24101465}.
CATALYTIC ACTIVITY: Reaction=(R)-carnitine(out) + 4-(trimethylamino)butanoate(in) = (R)-carnitine(in) + 4-(trimethylamino)butanoate(out); Xref=Rhea:RHEA:29427, ChEBI:CHEBI:16244, ChEBI:CHEBI:16347; Evidence={ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000269|PubMed:20829798, ECO:0000269|PubMed:24101465};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=46 uM for L-carnitine {ECO:0000269|PubMed:20829798}; KM=8.5 uM for L-carnitine {ECO:0000269|PubMed:24101465}; Vmax=4672 nmol/min/mg enzyme {ECO:0000269|PubMed:20829798}; Vmax=5172 nmol/min/mg enzyme {ECO:0000269|PubMed:24101465}; Note=kcat is 263 min(-1) with L-car...
PATHWAY: Amine and polyamine metabolism; carnitine metabolism. {ECO:0000255|HAMAP-Rule:MF_01049}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:24101465};
null
FUNCTION: Catalyzes the exchange of L-carnitine for gamma-butyrobetaine. {ECO:0000255|HAMAP-Rule:MF_01049, ECO:0000269|PubMed:20829798, ECO:0000269|PubMed:24101465}.
Proteus mirabilis (strain HI4320)
B4EZY7
SIAT_PROMH
MQLHDFGFINYAVLFGYLAAMLLVGVYFSKRQKTADDYFRGGGRVPGWAAGVSVFATTLSSITFMSIPAKAYTSDWTFIIGQYLAIAILPLVFYFYIPFFRKLKITSAYEYLEARFDVRSRLFASLSFMLFHIGRVAIITYLTVLALRPFMGIDPVVLIVLISLLCIIYTWMGGIEGVIWTDVIQGLLLSGGAVLIFIMICFKVDGGISEIFTTTAQADKFFPTTQWRWSWTDSTIPVLMIGFLFANIQQFTASQDVVQRYIVTDSIKETKRTLITNAKLVAIIPIFFFAIGSALFVYYQQNPSLLPAGFNTGGILPLFI...
null
null
sodium ion transport [GO:0006814]
extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]
symporter activity [GO:0015293]
PF00474;
1.20.1730.10;
Sodium:solute symporter (SSF) (TC 2.A.21) family
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:29717135}; Multi-pass membrane protein {ECO:0000269|PubMed:29717135}.
CATALYTIC ACTIVITY: Reaction=N-acetyl-alpha-neuraminate(out) + 2 Na(+)(out) = N-acetyl-alpha-neuraminate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:78535, ChEBI:CHEBI:29101, ChEBI:CHEBI:58770; Evidence={ECO:0000269|PubMed:29717135}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78536; Evidence={ECO:0000269|PubMed:2971713...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16 uM for Neu5Ac {ECO:0000269|PubMed:29717135}; Vmax=187 nmol/min/mg enzyme {ECO:0000269|PubMed:29717135};
null
null
null
FUNCTION: Symporter that uses the Na(+) gradient as the driving force for the uptake of the sialic acid N-acetylneuraminic acid (Neu5Ac) (PubMed:29717135). It allows the use of host-derived Neu5Ac as an energy source by P.mirabilis (PubMed:29717135). Also binds N-glycolylneuraminic acid (Neu5Gc) and ketodeoxynonulosoni...
Proteus mirabilis (strain HI4320)
B4F6I3
FSP1_XENTR
MGSKVSVEESVRVVIVGGGFAGIAAATQLKSFGIPFVLVDLKDAFHHNVAALRASVESGFARKTFISYKDTFQDNFIQGKVVGINLQTQRVILESNEELQFSHLIIATGSNGPFPGKINNVISKDQAIQVYEDLVKEIQKAKHVVVVGGGSAGVEMAAEVKTDYPEKEVTLVHSKVALADVQLQPKVRRTVKEILLSKGVRLILAQKVTNLDQVTSNVAQENTVLQLDKNSEVVTCDLVLCCTGYKISSSSYSSAFGDKLAEDGALIVNDYLQVQGHANVYAVGDCAYINEPKMAYYAGIHARVAATNVRNSLIGKSLKT...
1.6.5.-
COFACTOR: Name=6-hydroxy-FAD; Xref=ChEBI:CHEBI:60470; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; Note=Binds 6-hydroxy-FAD non-covalently. {ECO:0000250|UniProtKB:Q9BRQ8};
apoptotic mitochondrial changes [GO:0008637]; positive regulation of apoptotic process [GO:0043065]; vitamin K metabolic process [GO:0042373]
lipid droplet [GO:0005811]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
electron-transferring-flavoprotein dehydrogenase activity [GO:0004174]; flavin adenine dinucleotide binding [GO:0050660]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]
PF07992;
3.50.50.100;
FAD-dependent oxidoreductase family
PTM: N-myristoylation at Gly-2 mediates the recruitment to lipid droplets and plasma membrane. {ECO:0000250|UniProtKB:Q9BRQ8}.
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q9BRQ8}. Cell membrane {ECO:0000250|UniProtKB:Q9BRQ8}; Lipid-anchor {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q9BRQ8}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9BRQ8}. Nucleus {ECO:0000250|UniProtKB:Q9BRQ8}.
CATALYTIC ACTIVITY: Reaction=H(+) + NADH + ubiquinone-10 = NAD(+) + ubiquinol-10; Xref=Rhea:RHEA:61984, ChEBI:CHEBI:15378, ChEBI:CHEBI:46245, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64183; Evidence={ECO:0000250|UniProtKB:Q9BRQ8}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61985; Evidence={ECO:000025...
null
null
null
null
FUNCTION: A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis. At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis. Acts in parallel to GPX4 to supp...
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
B4F6I5
FICD_XENTR
MAVTECEWASLGSRIGLRAALVLLSGSLLVVLFPLSGLEHQYRTALNILLQCNLWGGDDRHTFTGQTRGLAVASTAIELLVLKQKPTSDVKFEAKAALNQALEMKRQGKKEKAHKLLHHALKMDPDHVDALNELGILLEEEKDIIQADYLYSKALTISPHNEKALINRDRTLPLVEEIDQRYFSLIDSKVKKLMSIPKGNPALRRVMEESYYHHIYHTVAIEGNTLSLSEIRHIIETRYAVPGKSLEEQNEVIGMHAAMKYVNATLVSRIGSVTIDNILEIHRRILGYVDPVEAGRFRRNQVFVGHHIPPHPRDVEKLMQ...
2.7.7.108; 3.1.4.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; Note=Divalent metal cation. Prefers Mn(2+) over Mg(2+). {ECO:0000250|UniProtKB:Q9BVA6};
protein adenylylation [GO:0018117]; protein deadenylylation [GO:0044602]; regulation of IRE1-mediated unfolded protein response [GO:1903894]; response to endoplasmic reticulum stress [GO:0034976]; response to unfolded protein [GO:0006986]
endoplasmic reticulum membrane [GO:0005789]
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]
PF02661;
1.10.3290.10;1.25.40.10;
Fic family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVA6}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9BVA6}.
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV...
null
null
null
null
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-222 determines which of the two op...
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
B4F6N6
LOXL2_XENTR
MLVTHIFLLTLSLSVPTLGQYEHWLYYPEYQASQAPEPLPTPARNVPQIHVRLAGEKRKHNEGRVEVYYEGEWGTVCDDDFSMYAAHIVCRELGYQDAVSWSPSSKYGKGEGRIWLDNVNCNGREKSIASCGSNGWGVTDCKHSEDVGVQCSDRRIPGFKVSNELPGQLEGLNIQVEEVRIRAILSAYRKRVPVTEGFVEVKVQGSWRQVCNAEWSSKNSRVVCGMFGFPAEKKFNNKVYKLFSSRRKHTYWQFSANCTGNEAHLSSCKVGGVLTPDPKTNQTCSDGSPAVVSCTPGRAFAPSPGTGFGKAFRQEQPLVR...
1.4.3.13
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; COFACTOR: Name=lysine tyrosylquinone residue; Xref=ChEBI:CHEBI:20489; Evidence={ECO:0000250|UniProtKB:Q9Y4K0}; Note=Contains 1 lysine tyrosylquinone. {ECO:0000250|UniProtKB:P33072, ECO:0000250|UniProtKB:Q9Y4K0};
collagen fibril organization [GO:0030199]; endothelial cell migration [GO:0043542]; endothelial cell proliferation [GO:0001935]; epithelial to mesenchymal transition [GO:0001837]; heterochromatin organization [GO:0070828]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of stem cell...
basement membrane [GO:0005604]; chromatin [GO:0000785]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634]
calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; oligosaccharide binding [GO:0070492]; protein-lysine 6-oxidase activity [GO:0004720]
PF01186;PF00530;
3.10.250.10;
Lysyl oxidase family
PTM: The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine. {ECO:0000250|UniProtKB:Q9Y4K0}.
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9Y4K0}. Nucleus {ECO:0000250|UniProtKB:Q9Y4K0}. Chromosome {ECO:0000250|UniProtKB:Q9Y4K0}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y4K0}. Note=Associated with chromatin. It is unclear how LOXL2 is...
CATALYTIC ACTIVITY: Reaction=H2O + L-lysyl-[protein] + O2 = (S)-2-amino-6-oxohexanoyl-[protein] + H2O2 + NH4(+); Xref=Rhea:RHEA:24544, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12448, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:131803; EC=1.4.3.13; Evidence={ECO:...
null
null
null
null
FUNCTION: Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transc...
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
B4F753
ABD12_XENTR
MRKRAEPVPPEHESFGRAPLDRECSIKQKLRIPGTKGHYPHDSDCDSKGMKRFGRRYGLWSRLRMFLIFLLGLYIAIPFLVKICPAIQTQLVFLNLVRFPYFIDLKRPEDQGLNHTCNFYLQPEEDVSIGVWHTVPAVLWKDAQGKDLEWYEEVLSTSYPVILYLHGNAGTRGGDHRVQLYKVLSSMGYHVISFDYRGWGDSVGSPSESGMTYDALHVFDWIKARSGDNPVYIWGHSLGTGVATNLVRRLCERETPPDSLILESPFTNIREEAKSHPFSVIYRYFPGFDWFFLDPITASGIKFANDDNVKYISCPLLILH...
3.1.-.-; 3.1.1.23
null
acylglycerol catabolic process [GO:0046464]; monoacylglycerol catabolic process [GO:0052651]; phosphatidylserine catabolic process [GO:0006660]; phospholipid catabolic process [GO:0009395]
endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
acylglycerol lipase activity [GO:0047372]; lysophospholipase activity [GO:0004622]; phospholipase activity [GO:0004620]
PF00561;
3.40.50.1820;
Serine esterase family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8N2K0}; Single-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617; Evidence={ECO:0000250|UniProtKB:Q8N2K0}; CATALYTIC ACTIVI...
null
null
null
null
FUNCTION: Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (By similarity). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous syst...
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
B4F769
SMAL1_RAT
MSLPLTEEQRKKIEENRQKALARRAEKLWAEQPQSTASGSSAARPSQCKQNSLLNLPAEPSKPEGHATISKGQNLNNSLPAAQRPHSSPCFQPSTAEEAKGLWKSEGKMSAACPNPSPPEVSNQQLLGSKSSEGHPQATQDTAASCPRPFPRDPKLEAKAGRPSTSGQSISDTFYALGEKTPKTDGRPAKALQTSPQKASCLRGMCLRTGDRFRVKIGYNKELIEVFKSLPSRRYDSFTKTWDFSMSDYRALMKAVERLSTVSLQPLEEVDGTGGQTSLPSAPSLTFVTGRCMLISRARFEVDIGYSEVVIALFKQMESR...
3.6.4.-
null
DNA damage response [GO:0006974]; DNA repair [GO:0006281]; double-strand break repair via nonhomologous end joining [GO:0006303]; regulation of transcription by RNA polymerase II [GO:0006357]; replication fork processing [GO:0031297]
DNA replication factor A complex [GO:0005662]; nuclear replication fork [GO:0043596]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]
ATP binding [GO:0005524]; ATP-dependent activity, acting on DNA [GO:0008094]; ATP-dependent chromatin remodeler activity [GO:0140658]; ATP-dependent DNA/DNA annealing activity [GO:0036310]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787]
PF07443;PF00271;PF00176;
3.40.50.300;3.40.50.10810;
SNF2/RAD54 helicase family, SMARCAL1 subfamily
PTM: DNA damage-regulated phosphorylation by kinases that may include ATM, ATR and PRKDC. {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Recruited to damaged DNA regions. {ECO:0000250}.
null
null
null
null
null
FUNCTION: ATP-dependent annealing helicase that binds selectively to fork DNA relative to ssDNA or dsDNA and catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing ...
Rattus norvegicus (Rat)
B4F779
DP13B_RAT
MPAVDKLLLEEALQDSPQTRSLLSVFEEDAGTLTDYTNQLLQAMQRVYGAQNEMCLATQQLSRQLLAYEKQNFALGKGDEEVISTLHYFSKVMDELNGLHSELAKQLADTMVLPVIQFREKDLTEVSTLKDLFGLASNEHDLSMAKYSRLPKRKENERVKTDVAKEVAAARRKQHLSSLQYYCALNALQYRKRAAMMEPLIGFAHGQINFFKKGAEMFSKSMDGFLSSVTDMVQSIQVELEAEADKMRVSQQELLSVSESVYTPDIDVATPQINRNLIQKTGYLNLRNKTGLVTTTWERLYFFTQGGNLMCQPRGAVAGG...
null
null
adiponectin-activated signaling pathway [GO:0033211]; cell cycle [GO:0007049]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; cold acclimation [GO:0009631]; diet induced thermogenesis [GO:0002024]; glucose homeostasis [GO:0042593]; negative regulation of cellular response to insulin stimulus [GO:1...
cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; early endosome membrane [GO:0031901]; early phagosome [GO:0032009]; early phagosome membrane [GO:0036186]; endosome [GO:0005768]; endosome membrane [GO:0010008]; macropinosome [GO:0044354]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886...
identical protein binding [GO:0042802]; phosphatidylinositol binding [GO:0035091]; phosphatidylserine binding [GO:0001786]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]
PF16746;PF00169;PF00640;
1.20.1270.60;2.30.29.30;
null
null
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250|UniProtKB:Q8NEU8}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8NEU8}. Nucleus {ECO:0000250|UniProtKB:Q8NEU8}. Cell membrane {ECO:0000250|UniProtKB:Q8NEU8}. Endosome membrane {ECO:0000250|UniProtKB:Q8NEU8}. Cytoplasm {ECO:0000250|UniProtKB:Q8K3G9}. Cyto...
null
null
null
null
null
FUNCTION: Multifunctional adapter protein that binds to various membrane receptors, nuclear factors and signaling proteins to regulate many processes, such as cell proliferation, immune response, endosomal trafficking and cell metabolism. Regulates signaling pathway leading to cell proliferation through interaction wit...
Rattus norvegicus (Rat)
B4F795
CTL2_RAT
MGKDSQHYYGKHGTPQKYDPTFKGPIYNRGCTDIICCVLLFLAIVGYVAVGIIAWTHGDPRKVIYPTDSRGEFCGQKGTKNADKPFLFYFNIVKCASPLVLLEFHCPTPQICVKQCPDRYLTFLSARNSRDFDYYKQFCVPGFKNNKGVAEVLRDGECPAVIIPSKPLAQRCFPAIHASKGVLMVGNETTYEDGHGTRKNVTDLVEGAKKANKVLEARQLAMQIFEDYTVSWYWIVIGLVIAMLLSLMFIVLLRFLAGVMVWVMIVMVILVLGYGIFHCYAEYSRLRGEAGSDVSLVDLGFQTDLRVYLHLRQTWMAFMI...
null
null
choline transport [GO:0015871]; ethanolamine transport [GO:0034229]; transmembrane transport [GO:0055085]
membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
antiporter activity [GO:0015297]; choline transmembrane transporter activity [GO:0015220]; ethanolamine transmembrane transporter activity [GO:0034228]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; salt transmembrane transporter activity [GO:1901702]; transmembrane transporter activity [GO...
PF04515;
null
CTL (choline transporter-like) family
PTM: N-glycosylated. {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19236841}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:19236841}; Multi-pass membrane protein {ECO:0000255}. Note=Mainly expressed in mitochondria. {ECO:0000269|PubMed:19236841}.
CATALYTIC ACTIVITY: Reaction=choline(out) + n H(+)(in) = choline(in) + n H(+)(out); Xref=Rhea:RHEA:75463, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:19236841}; CATALYTIC ACTIVITY: Reaction=ethanolamine(out) + n H(+)(in) = ethanolamine(in) + n H(+)(out); Xref=Rhea:RHEA:75467, ChEBI:CHEBI:15378, C...
null
null
null
null
FUNCTION: Exhibits choline transporter activity, as choline/H+ antiporter (PubMed:19236841). Also acts as a low-affinity ethanolamine/H+ antiporter, regulating the supply of extracellular ethanolamine (Etn) for the CDP-Etn pathway, redistribute intracellular Etn and balance the CDP-Cho and CDP-Etn arms of the Kennedy p...
Rattus norvegicus (Rat)
B4F7B7
DUS15_RAT
MGNGMTKVLPGLYLGNFIDAKDPDQLGRNKITHIVSIHESPQPLLQDITYLRISVSDTPEVPIKKHFKECVHFIHSCRLNGGNCLVHCFAGISRSTTVVIAYVMTVTGLGWQEVLEAIKASRPIANPNPGFRQQLEEFGWANSQKLRRQLEERFGEIPFRDEEDLRALLPLCRRCRQGPGTSAPSATTASSAASEGTLQRLVPRSPRESHRPLPLLARVKQTFFCLPRCLSRKGGK
3.1.3.16; 3.1.3.48
null
dephosphorylation [GO:0016311]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; regulation of oligodendrocyte differentiation [GO:0048713]; signal transduction [GO:0007165]
cytosol [GO:0005829]; plasma membrane [GO:0005886]
myosin phosphatase activity [GO:0017018]; phosphatase activity [GO:0016791]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]
PF00782;
3.90.190.10;
Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H1R2}; Lipid-anchor; Cytoplasmic side.
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:Q9H1R2, ECO:0000255|PROSITE-ProRu...
null
null
null
null
FUNCTION: May play a role in the regulation of oligodendrocyte differentiation. May play a role in the regulation of myelin formation (PubMed:27532821). Involved in the regulation of Erk1/2 phosphorylation in Schwann cells; the signaling may be linked to the regulation of myelination (PubMed:27891578). May dephosphoryl...
Rattus norvegicus (Rat)
B4F7C5
LRRT4_RAT
MGFRLITQLKGMSVLLVLFPTLLLVMLTGAQRACPKNCRCDGKIVYCESHAFADIPENISGGSQGLSLRFNSIQKLKSNQFAGLNQLIWLYLDHNYISSVDEDAFQGIRRLKELILSSNKITYLHNKTFHPVPNLRNLDLSYNKLQTLQSEQFKGLRKLIILHLRSNSLKTVPIRVFQDCRNLDFLDLGYNRLRSLSRNAFAGLLKLKELHLEHNQFSKINFAHFPRLFNLRSIYLQWNRIRSVSQGLTWTWSSLHTLDLSGNDIQAIEPGTFKCLPNLQKLNLDSNKLTNVSQETVNAWISLISITLSGNMWECSRSIC...
null
null
AMPA glutamate receptor clustering [GO:0097113]; neurotransmitter-gated ion channel clustering [GO:0072578]; positive regulation of synapse assembly [GO:0051965]; regulation of presynaptic membrane organization [GO:1901629]; regulation of synapse assembly [GO:0051963]; synapse organization [GO:0050808]
AMPA glutamate receptor complex [GO:0032281]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; photoreceptor ribbon synapse [GO:0098684]; postsynaptic density membrane [GO:0098839]; postsynaptic membrane [GO:0045211]; synapse [GO:0...
heparan sulfate proteoglycan binding [GO:0043395]
PF13855;
3.80.10.10;
LRRTM family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
null
null
null
null
null
FUNCTION: May play a role in the development and maintenance of the nervous system (By similarity). Exhibits strong synaptogenic activity, restricted to excitatory presynaptic differentiation. {ECO:0000250, ECO:0000269|PubMed:19285470}.
Rattus norvegicus (Rat)
B4F7E7
PALS1_RAT
MTTSYMNGHVTEESDSGIKNLGLASPEEHPKHREMAVDCPGDLGTRLMPVRRSAQLERIRQQQEDMRRRREEEGKKQELDLNSSMRLKKLAQIPPKTGIDNPIFDTEEGIVLESPHYAVKILEVEDLFSSLKHIQHTLVDSQSQEDISLLLQLVQNRDFQNAFKIHNAVTVHMNKASPPFPLIANVQDLVQEVQTVLKPVHQKEGQELTALLNAPHIQALLLAHDKVAEQEMQLEPITDERVYESIGHYGGETVKIVRIEKARDIPLGATVRNEMDSVIISRIVKGGAAEKSGLLHEGDEVLEINGIEIRGKDVNEVFDL...
null
null
central nervous system neuron development [GO:0021954]; cerebral cortex development [GO:0021987]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; establishment or maintenance of polarity of embryonic epithelium [GO:0016332]; gene expression [GO:0010467]; generation of neurons [GO:004...
adherens junction [GO:0005912]; apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; axon [GO:0030424]; bicellular tight junction [GO:0005923]; Golgi apparatus [GO:0005794]; lateral loop [GO:0043219]; myelin sheath adaxonal region [GO:0035749]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; pr...
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; kinase activity [GO:0016301]; protein domain specific binding [GO:0019904]
PF00625;PF02828;PF09060;PF00595;PF07653;
2.30.42.10;1.10.287.650;3.40.50.300;2.30.30.40;
MAGUK family
null
SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q8N3R9}. Cell membrane {ECO:0000250|UniProtKB:Q9JLB2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JLB2}. Endomembrane system {ECO:0000250|UniProtKB:Q9JLB2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JLB2}. Cell junction, tight junction {E...
null
null
null
null
null
FUNCTION: Plays a role in tight junction biogenesis and in the establishment of cell polarity in epithelial cells (By similarity). Also involved in adherens junction biogenesis by ensuring correct localization of the exocyst complex protein EXOC4/SEC8 which allows trafficking of adherens junction structural component C...
Rattus norvegicus (Rat)
B4FK49
NDK1_MAIZE
MESTFIMIKPDGVQRGLIGEIISRFEKKGFYLKALKLVNVERSFAEKHYADLASKPFFQGLVDYIISGPVVAMVWEGKSVVTTGRKIIGATNPLASEPGTIRGDFAVDIGRNVIHGSDSIESANKEIALWFPEGPADWQSSQHPWIYEK
2.7.4.6
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P22392};
CTP biosynthetic process [GO:0006241]; GTP biosynthetic process [GO:0006183]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310]; protein hexamerization [GO:0034214]; UTP biosynthetic process [GO:0006228]
nucleus [GO:0005634]
ATP binding [GO:0005524]; DNA binding [GO:0003677]; nucleoside diphosphate kinase activity [GO:0004550]
PF00334;
3.30.70.141;
NDK family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; Evidence={ECO:0000255|RuleBase:RU004013, ECO:0000269|PubMed:25679041}; CATALYTIC ACT...
null
null
null
null
FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity). Involved in transcription regulation (Probable). Has G-quadruplex (G4) DNA-bindin...
Zea mays (Maize)
B4FZ81
PTA12_MAIZE
MASCYNPWRLFPGMSTAVPAGPVTAPAHSRTCKSSKVFSALPHRRGLLFLGTRRARIKCVKDDSLHFDPSKIEPPPYSSYFDSTSGQLEPASGARASIPGKEYWPEGTAARVRAARAPAPVGESAGMPSFGTKPGSRRRGYKEQVTSASGTEGAQTDDRKDGDEPDVAIIGSGDDALEEIKDSVDEYVIYETPEEEELSEYDMDKMMGRPHPFIDPAKAMSLGEPKTSEELWWHWRRKSQEEEMWSRWQRRRPDVDTVFAKAMAETGQIKIFGDHPSRTEAALAKTRRHLYKEERLEAEQRRLEEIGPIAYYSEWVEAYK...
null
null
plastid transcription [GO:0042793]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of red or far-red light signaling pathway [GO:0090228]; positive regulation of thermomorphogenesis [GO:0140922]; protein catabolic process [GO:0030163]; regulation of gene expression [GO:0010468]; re...
chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; nucleus [GO:0005634]; plastid-encoded plastid RNA polymerase complex [GO:0000427]
single-stranded DNA binding [GO:0003697]; single-stranded RNA binding [GO:0003727]; transcription regulator activator activity [GO:0140537]
null
null
null
null
SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:25599833}. Nucleus {ECO:0000269|PubMed:25599833}.
null
null
null
null
null
FUNCTION: Required for the activity of the plastid-encoded RNA polymerase (PEP) and full expression of genes transcribed by PEP (PubMed:24246379, PubMed:25599833). Required for the proper build-up and formation of the PEP-complex. Binds single-stranded (ss) DNA and RNA, but not double-stranded (ds) DNA (PubMed:25599833...
Zea mays (Maize)
B4G2I8
HH_DROPE
MDNHNEVPMSMSAPWASAARVTCLSLDAKCHRPCPSSISASASASGCASDSAAIATTKLRHIAYTQRCSSRLTMLMTVLLLLLPLSFTPAHSCGPGRGLGRRRERNLYPLVLKQTIPNLSEYQSGASGPLEGEIKRDSPKFKDLVPNYNRDILFRDEEGTGADRLMTKRCKEKLNVLAYSVMNEWPGVRLLVTESWDEDHQHGQESLHYEGRAVTIATSDREPSRYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSISSHVHGCFTPESTALLESGITKPLSEIAIGDRVLSMGSNGQPVYSEVILFMDRNLEQMQNF...
3.1.-.-
null
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; cell-cell signaling involved in cell fate commitment [GO:0045168]; intein-mediated protein splicing [GO:0016539]; protein autoprocessing [GO:0016540]; regulation of gene expression [GO:0010468]; segment polarity determination [GO:000...
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
PF01085;PF01079;
3.30.1380.10;2.170.16.10;
Hedgehog family
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results ...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR ...
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI...
null
null
null
null
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that res...
Drosophila persimilis (Fruit fly)
B4G437
SPAST_DROPE
MVRTKNQSSSSSASSSSHKSPIKSHGGSGSAAAGTAGHPVSRSSSSHRTSIDDRKSATNVSSSSNRRTTPGSSPDGDGDDDTTTTDDLTPTSTSAPRSAGGPSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNNSNNKDQKHQQLTSSQSLNYPLEVTSGEAASEQQVQQPLPQQRYRALQPLEMAGANRSGSGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREE...
5.6.1.1
null
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regul...
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
PF00004;PF17862;
1.10.8.60;3.40.50.300;1.20.58.80;
AAA ATPase family, Spastin subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-...
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
null
null
null
null
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Inv...
Drosophila persimilis (Fruit fly)
B4GAJ1
LIS1_DROPE
MKMVLSQRQREELNQAIADYLGSNGYGDSLETFRKEADVSTESEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKYSLTGHRASITRVIFHPIFGLMVSASEDATIKIWDFETGEYERSLKGHTDSVQDVAFDSQGKLLASCSADLSIKLWDFQQSYECVKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDHTIRVWLMNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKT...
null
null
border follicle cell migration [GO:0007298]; brain morphogenesis [GO:0048854]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]...
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cytoplasmic microtubule [GO:0005881]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; nuclear envelope [GO:...
dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010]
PF08513;PF00400;
1.20.960.30;2.130.10.10;
WD repeat LIS1/nudF family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
null
null
null
null
null
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
Drosophila persimilis (Fruit fly)
B4GBH0
PTK7_DROPE
MDMDVMMISMCILASTLMAPGWASTSGFLRVPQSQSIVENEAADFGCEATDPASYLHYEWLHNGREISYDKRVYRIGSHLHIEAVQREEDVGDYVCIATSLASGAREASPPAKLSVIYLESASVQLLGSNRNELLLKCHVEGASGDEPLQIEWYRDSARLASWGNVHLEEHRLLVRQPSPSDDGLYRCTASNAAGRVMSKQGYVYQANIKCLPRLLKKNQKLPESWGKQTFLCRGKRGGSGGLDQALSPAPEDLRIVQGPAGQLLIKEGDSAALSCLYELPAELQNQRIQLRWRKDGKLLRHVELGGAIPIPGHAHDSGK...
null
null
cell adhesion [GO:0007155]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell axon guidance [GO:0072499...
axon [GO:0030424]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; W...
PF07679;PF13927;PF07714;
2.60.40.10;1.10.510.10;
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}.
null
null
null
null
null
FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in t...
Drosophila persimilis (Fruit fly)
B4GFJ8
RAS1_DROPE
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLTTWNVKNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRRGRKLNKPNRRFKCKIL
3.6.5.2
null
border follicle cell migration [GO:0007298]; cellular response to starvation [GO:0009267]; chorion-containing eggshell pattern formation [GO:0030381]; defense response to virus [GO:0051607]; determination of adult lifespan [GO:0008340]; dorsal closure, spreading of leading edge cells [GO:0007395]; epidermal growth fact...
membrane [GO:0016020]; plasma membrane [GO:0005886]
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; protein serine/threonine kinase activator activity [GO:0043539]
PF00071;
3.40.50.300;
Small GTPase superfamily, Ras family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08646}; Lipid-anchor {ECO:0000250|UniProtKB:P08646}; Cytoplasmic side {ECO:0000250|UniProtKB:P08646}.
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112};
null
null
null
null
FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormo...
Drosophila persimilis (Fruit fly)
B4GJC1
FICD_DROPE
MAMTILHASEKVNAEAEATTCPPTEKVKEEQQQQEQLQHSKTSKRVQFYRFALFFIAGSFAAFSFHALTSSSSWRLRQLHHLPNAHYLQTREEFAVYSVEELNAFKEFYDKSISDSVGASYSEAEQTNIKEALGALRLAQDMHLSGKDDKASRLFEHALALAPKHPEVLLRYGEFLEHNQRNIVLADQYYFQALTLCPSNSEALANRQRTAEVVQTLDERRLQSLDSKRDALSAIHESSSALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKLEITIKDILELH...
2.7.7.108; 3.1.4.-
null
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
plasma membrane [GO:0005886]
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
PF02661;
1.10.3290.10;1.25.40.10;
Fic family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV...
null
null
null
null
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-261 determines which of the two op...
Drosophila persimilis (Fruit fly)
B4GZN1
WLS_DROPE
MSGTILENLSGRKLSILVGSLLLCQVLCFLLGGLYAPVPAGHTNVLGSLCRENHARQNDTSFFLYSRGEGSCTQVTREEVEQDSMKLANQIVHVFQMPLPRDSRVLDYSRWQQNLIGVLQVEFGYDSSSELREPPKELQLTIDMRLAYRNKGDPDHAWKLYAHGVEHRYLDCVAAHIGSSETLYTCDMIPLFELGALHHSFYLLNLRFPLDTPKQMNLQFGHMHDLTLTAIHQNGGFTHVWLMLKTLLFPFVVGIMVWFWRRVHLLQRSPALLEYMLLYLGGALTFLNLPLEYLSLTIEMPYMLLLSDIRQGIFYAMLLS...
null
null
compound eye morphogenesis [GO:0001745]; cuticle pattern formation [GO:0035017]; Golgi to plasma membrane protein transport [GO:0043001]; imaginal disc-derived leg morphogenesis [GO:0007480]; imaginal disc-derived wing margin morphogenesis [GO:0008587]; intracellular protein transport [GO:0006886]; positive regulation ...
cell projection [GO:0042995]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; multivesicular body [GO:0005771]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membr...
Wnt-protein binding [GO:0017147]
PF06664;
null
Wntless family
null
SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass memb...
null
null
null
null
null
FUNCTION: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to ...
Drosophila persimilis (Fruit fly)
B4H3U8
SWS_DROPE
MDVLELLRVSGSNMYYSTFLADAWCYYISNQITMTMYLYCALGVLSMLFIGWFVYFKRLARLRLRHEIARSLSAVTMASGGDLRGPRFRKRDKMLFYGRRMLRKMKNVSGQMYSSGKGYKRRAVIRFARRILQLRRENMPLEVRTVEPPAEYLEETMEGSDRVPPDALYMLQSIRIFGHFEKPIFLRLCKHTQLLELMGGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVTSLLSFIDVLSGNPSYYKTVTAKAIEKSVVIRLPMAAFQEVFKDSPDVMIRVIQVIMIRLQRVLFTALRNYLGLNA...
3.1.1.5
null
ensheathment of neurons [GO:0007272]; glial cell apoptotic process [GO:0034349]; lipid catabolic process [GO:0016042]; membrane lipid metabolic process [GO:0006643]; membrane organization [GO:0061024]; neuron apoptotic process [GO:0051402]; phosphatidylcholine metabolic process [GO:0046470]; photoreceptor cell maintena...
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; protein kinase A catalytic subunit binding [GO:0034236]
PF00027;PF01734;
3.40.1090.10;2.60.120.10;
NTE family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}.
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969};
null
null
null
null
FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in...
Drosophila persimilis (Fruit fly)
B4HBU3
PLK4_DROPE
MMSTRTFGETIEEYEVQHLLGKGGFASVYKARCLHSHQDVAIKMIDKKLIQGTGLTSRVRQEVEIHSRLKHPSVLQLYTFFQDVNYVYLVLELAHNGELQRYMKQHLLRPFTESEGATILRQVVAGLLYLHSHNIMHRDISLSNLLLSKEMHIKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRLSHGLPADVWSVGCMLYTLLVGRPPFETEGVESTLNKVVMSEFMMPSHLSFEAQDLIHKLLKKSPHERITLEQVLRHPFLKRTVGGSSYSTTPGALNEFSQSLASSDSGIVTFASSDSRKSHRLRSVDNSSG...
2.7.11.21
null
centriole replication [GO:0007099]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of protein catabolic process [GO:0045732]; regulation of centriole replication [GO:0046599]; regulation of protein stability [GO:0031647]; sperm ax...
centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922]
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;PF18190;PF18409;
2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
PTM: Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as sas-6. When overexpressed, it is...
Drosophila persimilis (Fruit fly)
B4HFB7
HH_DROSE
MDNHSSVPWASAASVTCLSLDAKCHSSSSKSAASSISASPETQTMRHIAHTQRCLSRLTSLVALLLIVLPMMFSPAHSCGPGRGLGRHRARNLYPLVLKQTIPNLSEYTNSASGPLEGVIRRDSPKFKDLVPNYNRDILFRDEEGTGADRLMSKRCKEKLNVLAYSVMNEWPGIRLLVTESWDEDYHHGQESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSISSHVHGCFTPESTALLESGVRKPLGELSIGDRVLSMTANGQAVYSEVILFMDRNLEQMQNFVQLHTDGGAVLTVT...
3.1.-.-
null
Bolwig's organ morphogenesis [GO:0001746]; cell-cell signaling involved in cell fate commitment [GO:0045168]; cytoneme assembly [GO:0035231]; epithelial cell migration, open tracheal system [GO:0007427]; genital disc anterior/posterior pattern formation [GO:0035224]; glial cell migration [GO:0008347]; gonadal mesoderm ...
cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; endosome [GO:0005768]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
PF01085;PF01079;
3.30.1380.10;2.170.16.10;
Hedgehog family
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results ...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR ...
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI...
null
null
null
null
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that res...
Drosophila sechellia (Fruit fly)
B4HGG6
SPAST_DROSE
MVRTKNQSSSSSASSSSTKSPIKSSSGAGSSGGGVGGRQSTHRSSSASNVAAVVAGGSSAAGGGSSSNRRSPGSSPDGDDDTTTTDDLTPTTCSPRSGHHHSYGGYSSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNSSKEQQQSLNHPSELNREGDGQEQQLSNQPQRFRPIQPLEMAANRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREQDLQMQRL...
5.6.1.1
null
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regul...
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
PF00004;PF17862;PF09336;
1.10.8.60;3.40.50.300;1.20.58.80;
AAA ATPase family, Spastin subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-...
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
null
null
null
null
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Inv...
Drosophila sechellia (Fruit fly)
B4HKC7
RAS1_DROSE
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLASWNVNNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRRGRKMNKPNRRFKCKML
3.6.5.2
null
border follicle cell migration [GO:0007298]; cellular response to starvation [GO:0009267]; chorion-containing eggshell pattern formation [GO:0030381]; defense response to virus [GO:0051607]; determination of adult lifespan [GO:0008340]; dorsal closure, spreading of leading edge cells [GO:0007395]; epidermal growth fact...
plasma membrane [GO:0005886]
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; protein serine/threonine kinase activator activity [GO:0043539]
PF00071;
3.40.50.300;
Small GTPase superfamily, Ras family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08646}; Lipid-anchor {ECO:0000250|UniProtKB:P08646}; Cytoplasmic side {ECO:0000250|UniProtKB:P08646}.
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112};
null
null
null
null
FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormo...
Drosophila sechellia (Fruit fly)
B4HNW4
PTK7_DROSE
MISIYGLVMALMMASVLASSSRFQRVPQSQSVVENESVKFECESTDSYSELHYDWLHNAHRIAYDKRVHQIGSNLHIEAVRRTEDVGNYVCIATNLASGAREASPPAKLSVIYLESASVQLLGSNRNELLLKCHVEGASGDLEPLEIEWYRNSEKLSTWKNVQLDQHRLIIRQPGSEDDGLYRCTASNAAGRVMSKQGYVYQSSVKCLPRLPRRKNQKMMESWDKQTFLCRGKRGGAAGLESLPAAPEDLRIVQGPVGQSIIKEGEPTALTCLYELPDELKNQRIQLRWRKDGKLLRQVELGGSAPIIGHSFDSGKDALL...
null
null
cell adhesion [GO:0007155]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell axon guidance [GO:0072499...
axon [GO:0030424]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; W...
PF07679;PF13927;PF07714;
2.60.40.10;1.10.510.10;
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}.
null
null
null
null
null
FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in t...
Drosophila sechellia (Fruit fly)
B4HSL3
LIS1_DROSE
MKMVLSQRQREELNQAIADYLGSNGYADSLETFRKEADLSTEVEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKFSLTGHRASITRVIFHPIFALMVSASEDATIRIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQSYECIKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDQTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKT...
null
null
border follicle cell migration [GO:0007298]; brain morphogenesis [GO:0048854]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]...
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cytoplasmic microtubule [GO:0005881]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; nuclear envelope [GO:...
dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010]
PF08513;PF00400;
1.20.960.30;2.130.10.10;
WD repeat LIS1/nudF family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
null
null
null
null
null
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
Drosophila sechellia (Fruit fly)
B4HWI2
IRS1_DROSE
MASISDDGMALSGNLKKLKTMKKKFFVLYEETSTSSARLEYYDTEKKFLQRAEPKRVIYLKNCFNINRRLDTKHRFVIVLSSRDGGFGIVLENENDLRKWLDKLLVLQRNIANSNGTAHSPYDQVWQVVIQKKGISEKVGITGTYHCCLTSKSLTFVCIGPEKTPNGEDRVASIEILLTTIRRCGHASPQCIFYVELGRQSVLGSGDLWMETDNAAVATNMHNMILSAMSAKTESNTNLINVYQNRPDLSHEPMRKRSSSANEASKPINVNVIQNSQNSLELRSCSSPHNYGFSRERCDSLPTRNGTLSESSNQTYFGSN...
null
null
cellular response to starvation [GO:0009267]; determination of adult lifespan [GO:0008340]; germ-line stem-cell niche homeostasis [GO:0060250]; glucose homeostasis [GO:0042593]; growth of a germarium-derived egg chamber [GO:0007295]; insulin receptor signaling pathway [GO:0008286]; insulin-like growth factor receptor s...
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
insulin receptor binding [GO:0005158]; insulin-like growth factor receptor binding [GO:0005159]; phosphatidylinositol 3-kinase binding [GO:0043548]
PF02174;
2.30.29.30;
null
null
null
null
null
null
null
null
FUNCTION: Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit. May mediate the control of various cellular processes by insulin-like peptides. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains. Involved in control of cell prol...
Drosophila sechellia (Fruit fly)
B4I1V5
FICD_DROSE
MCTEAEQPSPPAQQQEQGNPPLCKAQNPKPARLYRLVLLFVAGSLAAWTFHALSSTNLVWKLRQLHHLPTAHYLQTRDEFALYSVEELNAFKEFYDKSVSDSVGASYTEAEQTNIKEALGALRMAQDLYLAGKDDKAARLFEHALALAPRHPEVLLRYGEFLEHNQRNIVLADQYYFQALTISPSNSEALANRQRTADVVQSLDERRLESLDSKRDALSAIHESNGALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKIDITIKDILELHRRVLGHVDPIEGGE...
2.7.7.108; 3.1.4.-
null
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
plasma membrane [GO:0005886]
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
PF02661;
1.10.3290.10;1.25.40.10;
Fic family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV...
null
null
null
null
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-247 determines which of the two op...
Drosophila sechellia (Fruit fly)
B4IAQ8
PLK4_DROSE
MLSNRAFGETIEDYEVQHLLGKGGFATVYKARCLHTHQDVAIKMIDKKLIQGTGLTSRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIARHFTETEAASILKQVVAGLLYLHSHNIMHRDISLSNLLLSREMHVKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRSSHGLPADVWSVGCMLYTLLVGRPPFETDAVQSTLNKVVMSEYIMPAHLSYEAQDLINKLLKKLPHERITLEAVLCHPFMLKCSNGGHSAPGALNMFSQSMESGDSGIITFASSDSRNSQQIRSVENSGPQQV...
2.7.11.21
null
centriole replication [GO:0007099]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of protein catabolic process [GO:0045732]; regulation of centriole replication [GO:0046599]; regulation of protein stability [GO:0031647]; sperm ax...
centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922]
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;PF18190;PF18409;
2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
PTM: Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as sas-6. When overexpressed, it is...
Drosophila sechellia (Fruit fly)
B4IL64
SWS_DROSE
MDVLEMLRASASGSYNTIFSDAWCQYVSKQITATVYMYCALVMMSLLFIAWFLYFKRMARLRLRDELARSISTATNSSGDLRGLRFRKRDKMLFYGRRMLRKVKNVSGQMYSSGKGYKRRAVMRFARRILQLRRDNMPLEMRTVEPPAEYLEETIEGSDRVPPDALYMLQSIRIFGHFEKPVFLRLCKHTQLLELMAGDYLFKITDPDDSVYIVQSGMINVYISNADGSTLSLKTVRKGESVTSLLSFIDVLSGNPSYYKTVTAKAIEKSVVIRLPMQAFEEVFQDNPDVMIRVIQVIMIRLQRVLFTALRNYLGLNAEL...
3.1.1.5
null
ensheathment of neurons [GO:0007272]; glial cell apoptotic process [GO:0034349]; lipid catabolic process [GO:0016042]; membrane lipid metabolic process [GO:0006643]; membrane organization [GO:0061024]; neuron apoptotic process [GO:0051402]; phosphatidylcholine metabolic process [GO:0046470]; photoreceptor cell maintena...
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; protein kinase A catalytic subunit binding [GO:0034236]
PF00027;PF01734;
3.40.1090.10;2.60.120.10;
NTE family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}.
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969};
null
null
null
null
FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in...
Drosophila sechellia (Fruit fly)
B4J2W3
WLS_DROGR
MSGTILENLSGRKLSILVSSLMLCQVVCFLMGGLFAPVPAGHQTVLGSKCRDVPGRQNDTSFFLYSRGNGACKSLQDIDIEQDELKMANQLVYVFQMPLPRDNNTLQYSRWQQNLIGVLQVDIAYDSASELREPPKELQLTIDTRLAYRNQKDADTDWKLYAHSVEQRYLDCHASHVGRLETLYTCDIIPLFELGALHHNFYLLNLRFPMDTPKQMNLQFGHMHDLTLTAIHQNGGFTQVWLVLKTLLFPFVIGIMMWFWRRVHILQRSPALLEYMLFYLGGALSFLNLPLELLTLGVEMPYMLLLSDVRQGIFYAMLLS...
null
null
compound eye morphogenesis [GO:0001745]; cuticle pattern formation [GO:0035017]; Golgi to plasma membrane protein transport [GO:0043001]; imaginal disc-derived leg morphogenesis [GO:0007480]; imaginal disc-derived wing margin morphogenesis [GO:0008587]; intracellular protein transport [GO:0006886]; positive regulation ...
cell projection [GO:0042995]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; multivesicular body [GO:0005771]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membr...
Wnt-protein binding [GO:0017147]
PF06664;
null
Wntless family
null
SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass memb...
null
null
null
null
null
FUNCTION: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to ...
Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi)
B4JBN5
FICD_DROGR
METGKVTQEPKQMKFTYRFAFFFIAGSLATFVFHALTSSSSVSLFGWRLQLRQLHHLPTAHYLQTRDEFAVYSVDELNAFKEFYDKSVSDSVGASYTEAEQTNIKEALGAMRLALDMHISGKDDKAARLFEHALALAPKHPEVLLRYGEFLEHNQRNIVLADQYYFQALSISPSNSEAFANRQRTANVVQTLDERRLVSLDEKRDALSAIHEANAALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSVLETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKLEITLKDILELHRRVLGHVDPIEGGEFRRTQVYVGGH...
2.7.7.108; 3.1.4.-
null
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
plasma membrane [GO:0005886]
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
PF02661;
1.10.3290.10;1.25.40.10;
Fic family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV...
null
null
null
null
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-236 determines which of the two op...
Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi)
B4JII0
SPAST_DROGR
MVRTKNQSSSSSASSSTKSPVKISGGTTNRSRSCSDALIDDGNSKSSSKPTSNNRQRTTTNNNTTAITTTPGSSPDNDDDDTTTTDADLTPTSGNAPRGGNSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRSPNRRDCNIEIVVQNSKEQQQQHQHQQAIIHCPLERRGNISGIEQTLAQALPQRQRAIQPLEMAGNRAGGNYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREEDLQLQ...
5.6.1.1
null
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regul...
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
PF00004;PF17862;PF09336;
1.10.8.60;3.40.50.300;1.20.58.80;
AAA ATPase family, Spastin subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-...
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
null
null
null
null
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Inv...
Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi)
B4JTF5
HH_DROGR
MDNEAVSALWSCASATCLSLDVKRHCSDANVDSQARTQSQATPMTNETDPRKLRHIAHTPRGSCFMTLLLLLLLALNFRHAHSCGPGRGLGRRRDRNLYPLVLKQTVPNLSEYQSGASGPLEGVIDRKSPKFKDLVPLYNSDILFRDEEGTGADRMMTKRCKEKLVMLATSVMNEWPGVKLLVTESWDEDHHHGEQSLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSSSISHVHGCFTPESTAQLESGAKKPLGELAIGDRVLSMDAKGQAVYSEVILFMDRNLEQMETFVQLHTDGG...
3.1.-.-
null
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; cell-cell signaling involved in cell fate commitment [GO:0045168]; intein-mediated protein splicing [GO:0016539]; protein autoprocessing [GO:0016540]; regulation of gene expression [GO:0010468]; segment polarity determination [GO:000...
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
PF01085;PF01079;
3.30.1380.10;2.170.16.10;
Hedgehog family
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results ...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR ...
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI...
null
null
null
null
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that res...
Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi)
B4JWA1
LIS1_DROGR
MKMVLSQRQREELNQAIADYLGTNGYADSLEAFRKEADLSTEAEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKYSLTGHRASITRVIFHPIFGLMVSASEDATIKIWDFETGEYERTLKGHTDSVQDVAFDAQGKLLVSCSADLSIKLWDFQQSYECVKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDHTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKT...
null
null
border follicle cell migration [GO:0007298]; brain morphogenesis [GO:0048854]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]...
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cytoplasmic microtubule [GO:0005881]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; nuclear envelope [GO:...
dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010]
PF08513;PF00400;
1.20.960.30;2.130.10.10;
WD repeat LIS1/nudF family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
null
null
null
null
null
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi)
B4K4M0
HH_DROMO
MDNNQAVSALWSCASATCLSLDAKRHSLEPSSPDGQASLDVNNKSAPVDAHARKLRHIAHTPRGSCFMALLLLLLLALNFRHAHSCGPGRGLGRRRERNLYPLVLKQTVPNLSEYHNGASGPLEGVIHRDSPKFKNLVLNYNKDILFRDEEGTGADRVMSKRCREKLNMLAYSVMNEWPGVRLLVTESWDEDHQHGQESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSPSISHVHGCFTPESTALLESGAEKALSELAIGDRVLSMDTKGQPVYSEVILFMDRNLEQVQNFVQLHTD...
3.1.-.-
null
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; cell-cell signaling involved in cell fate commitment [GO:0045168]; intein-mediated protein splicing [GO:0016539]; protein autoprocessing [GO:0016540]; regulation of gene expression [GO:0010468]; segment polarity determination [GO:000...
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
PF01085;PF01079;
3.30.1380.10;2.170.16.10;
Hedgehog family
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results ...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR ...
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI...
null
null
null
null
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that res...
Drosophila mojavensis (Fruit fly)
B4K799
SPAST_DROMO
MVRTKNQSSSSSASSSTKSPVKISGGGSSGANRSRSCSEALIDDGKTSSKLSSNRQRATITTTTTSTTPGSSPDDDTTDADLTPTSGYGPRGGTSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYCASTKVIYRSPHRRDCNIEIVVQNSKEQQSIICPLERNTSDGIEKAQQLLPQRQRALLPLEMATNRGGSGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHEKMQTNLSMARDRLHFLALREEDLQMQRLSLMDPPKNKQQVTSK...
5.6.1.1
null
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regul...
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
PF00004;PF17862;PF09336;
1.10.8.60;3.40.50.300;1.20.58.80;
AAA ATPase family, Spastin subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-...
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
null
null
null
null
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Inv...
Drosophila mojavensis (Fruit fly)
B4KFW6
FICD_DROMO
MAMATGKATEEEQPEQGQQQQQLQQQQKQTTLQSTYRFALFFIAGCLAAFGFHALTSSSGSLLGWRLRLHHLPTAHYLQTRDEFAVYSVDELNAFKEFYDKSVSDSVGASLSEAEETNIKEAMGALRLAQEMYMTGKDDKAARLFEHALALAPKHPEVLLRYGEFLEHNQRNIVLADQYYFQALSINPSNTEALANRQRTADVVQLLDERRLSSLDEKRDALSAIHEANSALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSVLETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKLYITLKDILELHRRVLGHVDPI...
2.7.7.108; 3.1.4.-
null
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
plasma membrane [GO:0005886]
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
PF02661;PF13428;
1.10.3290.10;1.25.40.10;
Fic family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV...
null
null
null
null
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-251 determines which of the two op...
Drosophila mojavensis (Fruit fly)
B4KPU0
PTK7_DROMO
MPIVMDMNMLLMLSLAFTVMAPASASSSRFTQPPQSQAIVENDAADFSCEATGPSGDLHYEWLHNGQQIGYDSRVLQIGSNLRIESVQREDAGDYVCIAASAASGARQASPPAKLSVIFLDAVTVQLLGSNRNELLLKCHVEGASGDEPLQIEWYRDSAKLSSWQNVELQQHRLLVRQPSSADDGLYRCIASNAAARVMSKQGYVYEHLASVAPGSTKCLPKLKRNQKMPESWGKQVFLCRGKRGGSTGMDQSQSLPPSPEGLRIVQGPNDKLIIKEGEPTTLSCLYELPAELQNQRIQLRWRKDGKILRHVELGDAVVP...
null
null
cell adhesion [GO:0007155]; dendrite self-avoidance [GO:0070593]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260...
axon [GO:0030424]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; cell-cell adhesion mediator activity [GO:0098632]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane recept...
PF07679;PF13927;PF07714;
2.60.40.10;1.10.510.10;
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}.
null
null
null
null
null
FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in t...
Drosophila mojavensis (Fruit fly)
B4KT48
LIS1_DROMO
MKMVLSQRQREELNQAIADYLGSNGYADSLETFRKEADLSTESEKKYGGLLEKKWTSVIRLQKKVMDLEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKYSLTGHRASITRVIFHPIFGLMVSASEDATIKIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQSYECVKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDHTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKT...
null
null
border follicle cell migration [GO:0007298]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]; establishment of mitotic spindle...
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; CIA complex [GO:0097361]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; spindle pole centrosome [GO:00316...
dynein complex binding [GO:0070840]
PF08513;PF00400;
1.20.960.30;2.130.10.10;
WD repeat LIS1/nudF family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
null
null
null
null
null
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
Drosophila mojavensis (Fruit fly)
B4L184
WLS_DROMO
MSGTILENLSGRKLSILVSSLLLCQVACFLIGGLYAPVPAGHQIVMGIKCRDVAGRQNDTSFFLYSRGNGACDSVQDIDIEQDPLKMANQLVYVFQMPLPRDNRTLDYSRWQQNLIGVLQMDIAYDSSSELREPPKELQLTIDTRLAYRNKNDEDADWKPYAHSIEKRFLDCRAAHVGLQEILYTCDIIPLFELGALHHSFYLLNLRFPMDTPKRLNLQFGHMHDIILTAIHQNGGFTQVWLLLKSVLFPFIIGIMVWFWRRVHILQRSPALLEYMLLYLGGALSFLNLPLEYLTLSFEMPYMLLLSDVRQGIFYAMLLS...
null
null
compound eye morphogenesis [GO:0001745]; cuticle pattern formation [GO:0035017]; Golgi to plasma membrane protein transport [GO:0043001]; imaginal disc-derived leg morphogenesis [GO:0007480]; imaginal disc-derived wing margin morphogenesis [GO:0008587]; intracellular protein transport [GO:0006886]; positive regulation ...
cell projection [GO:0042995]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; multivesicular body [GO:0005771]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membr...
Wnt-protein binding [GO:0017147]
PF06664;
null
Wntless family
null
SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass memb...
null
null
null
null
null
FUNCTION: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to ...
Drosophila mojavensis (Fruit fly)
B4L535
SWS_DROMO
MDVLELLRASVNGCYNTLFSDAWSQYVSKQIATTTYWYGALLAIGALFIAWFLYFKRLASLRLRDESARTLSALTAASGGDHRGLRFRKRDKMLFYGRRMLRKMKNVSGQMYSSGKGYKRRAVMRFARRILQLQRENRPLEMKTVEPPAEYLEETIDGSDRVPPDALYMLQSIRIFGHFEKPIFLKLCKHTQLLQLMAGDYLFKITDPDDSVYIVQSGMINVYICNADGSTLSLKTVRKGESVTSLLSFIDVLSGNSSYYKTVTAKAMEKSVVIRLPMQAFEEVFNENPDVMIRVIQVIMIRLQRVLFTALRNYLGLNAE...
3.1.1.5
null
ensheathment of neurons [GO:0007272]; glial cell apoptotic process [GO:0034349]; lipid catabolic process [GO:0016042]; membrane lipid metabolic process [GO:0006643]; membrane organization [GO:0061024]; neuron apoptotic process [GO:0051402]; phosphatidylcholine metabolic process [GO:0046470]; photoreceptor cell maintena...
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; protein kinase A catalytic subunit binding [GO:0034236]
PF00027;PF01734;
3.40.1090.10;2.60.120.10;
NTE family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}.
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969};
null
null
null
null
FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in...
Drosophila mojavensis (Fruit fly)
B4LC58
WLS_DROVI
MSGTILENLSGRKLSILVSSLMLCQVACFLMGGLYAPVPAGHQTVVGIKCRDVPGRQNDTNFFLYSRGNGACKSLQDMDIEQDPLKMANQLVYVFQMPLPRDNRTLDYSRWQQNLIGVLQVDIAYDSSSELREPPKELQLTIDTRLAYRNKKDADTDWKLYAHSVEQRYLDCHAAHVGLLETLYTCDIIPLFELGALHHNFYLLNLRFPIDTPKRMNLQFGHMHDLTLTAIHQNGGFTQVWLLLKTLLFPFVVGIMIWFWRRVHILQRSPALLEYMLLYLGGALSFLNLPLEYLTLSIEMPYMLLLSDVRQGIFYAMLLS...
null
null
compound eye morphogenesis [GO:0001745]; cuticle pattern formation [GO:0035017]; Golgi to plasma membrane protein transport [GO:0043001]; imaginal disc-derived leg morphogenesis [GO:0007480]; imaginal disc-derived wing margin morphogenesis [GO:0008587]; intracellular protein transport [GO:0006886]; positive regulation ...
cell projection [GO:0042995]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; multivesicular body [GO:0005771]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membr...
Wnt-protein binding [GO:0017147]
PF06664;
null
Wntless family
null
SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass memb...
null
null
null
null
null
FUNCTION: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to ...
Drosophila virilis (Fruit fly)
B4LG38
UBP36_DROVI
MPVSLAVCETANVVNAALRESLGSGIGGGGGCVAAAASRSSAGSGSGSVAGVDEAKIGDVSGTDNLQSQIVANAKRVLLAKIEYEEVENYHESVLAKLKSKYIVIKPDNNNGAANCNYKTNGKAVGSNGHDNNTVNGGTVNGNRKQTVDSGQSNQNSSANPNELPKPKRVLYPRENIRIGWKQSERKWQVGAGMLNVGNTCYLNSTLQALFHIPALANWLVSETSHVENCNISESCGSGGCIICAMAKTLQTTQSNQSAVRPFLIYTKLRQICKHMVVGRQEDAHEFLRFLVEAMEKAYLMRFRNFKELDQLVKETTPIS...
3.4.19.12
null
germ-line stem cell population maintenance [GO:0030718]; heterochromatin formation [GO:0031507]; negative regulation of antimicrobial peptide production [GO:0002785]; negative regulation of innate immune response [GO:0045824]; negative regulation of macroautophagy [GO:0016242]; negative regulation of peptidoglycan reco...
cytosol [GO:0005829]; nucleolus [GO:0005730]
cysteine-type deubiquitinase activity [GO:0004843]; K63-linked deubiquitinase activity [GO:0061578]
PF00443;
3.90.70.10;
Peptidase C19 family
null
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
null
null
null
null
FUNCTION: Required for maintaining multiple types of adult stem cells, including male and female germline, epithelial follicle cell and intestinal stem cells. May function as a transcriptional repressor by continually deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, thereby prev...
Drosophila virilis (Fruit fly)
B4LQ21
LIS1_DROVI
MKMVLSQRQREELNQAIADYLGSNGYADSLEAFRKEADLSTEAEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKYSLTGHRASITRVIFHPIFGLMVSASEDATIKIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLASCSADLSIKLWDFQQSYECVKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSIFATCSNDHTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKT...
null
null
border follicle cell migration [GO:0007298]; brain morphogenesis [GO:0048854]; centrosome localization [GO:0051642]; centrosome separation [GO:0051299]; chorion-containing eggshell pattern formation [GO:0030381]; clathrin-dependent endocytosis involved in vitellogenesis [GO:0061883]; dendrite morphogenesis [GO:0048813]...
axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cytoplasmic microtubule [GO:0005881]; dendrite [GO:0030425]; dynactin complex [GO:0005869]; dynein complex [GO:0030286]; growth cone [GO:0030426]; kinetochore [GO:0000776]; kinetochore microtubule [GO:0005828]; neuronal cell body [GO:0043025]; nuclear envelope [GO:...
dynein complex binding [GO:0070840]; microtubule plus-end binding [GO:0051010]
PF08513;PF00400;
1.20.960.30;2.130.10.10;
WD repeat LIS1/nudF family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03141}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03141}. Note=Localizes to the plus end of microtubules and to the centrosome. {ECO:0000255|HAMAP-Rule:MF_03141}.
null
null
null
null
null
FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. {ECO:0000255|HAMAP-Rule:MF_03141}.
Drosophila virilis (Fruit fly)
B4LQT7
FICD_DROVI
MAKAKAKQEPQQQRQTLQATYRFVLFFIAGSLAAFAFHALTSSTGSLMGWRLRLHHLPTAHYLQTRDEFAVYSVDELNAFKEFYDKSISDSVGASFTEAEQTNIKEAMGALRLAQEMYMAGKDDKAARLFEHALALAPKHPEVLLRYGEFLEHNQRNIVLADQYYFQALCISPSNSEALANRQRTADVVQTLDERRLISLDEKRDALSAIHEANSALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSVLETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKLEITLKDILELHRRVLGHVDPIEGGEFRRNQVYVGGH...
2.7.7.108; 3.1.4.-
null
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
plasma membrane [GO:0005886]
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
PF02661;PF13428;
1.10.3290.10;1.25.40.10;
Fic family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV...
null
null
null
null
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-236 determines which of the two op...
Drosophila virilis (Fruit fly)
B4LX81
SPNE_DROVI
MDSDLMDFFDFSKQFKRGTALKGCITGDPNALTTESRDSKPIKREKIGTDYVNEIVEKEKQLMNKLVDGQSVAKRNRTLDELDSDDEEENMQEQPSVRSDEAYYEKYRFDLNRNKNLPIYAQREQIMKAIRENPVVILKGETGCGKTTQVPQYILDEACKRREFCNIVVTQPRRIAAISIANRVCQERQWQPGTVCSYQVGLHRQSNVEDTRLLYCTTGVLLNNLIRLKTLTHYTHIVLDEVHERDQDMDFLLIVVRRLLALNSRHVKVILMSATIDTREFSKYFATSSAFPPVVTASHGRKYPLVKYYRDQLKNIHWKD...
3.6.4.13
null
dorsal appendage formation [GO:0046843]; germarium-derived oocyte fate determination [GO:0007294]; global gene silencing by mRNA cleavage [GO:0098795]; heterochromatin formation [GO:0031507]; intracellular mRNA localization [GO:0008298]; mitotic chromosome condensation [GO:0007076]; oocyte karyosome formation [GO:00307...
nucleus [GO:0005634]; P granule [GO:0043186]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]
PF00270;PF21010;PF00271;PF00567;
1.20.120.1080;2.30.30.140;2.40.50.90;3.40.50.300;
DEAD box helicase family, DEAH subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Component of the nuage, also named P granule, a germ-cell-specific organelle required to repress transposon during meiosis. {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
null
null
null
null
FUNCTION: Probable ATP-binding RNA helicase which plays a central role during spermatogenesis and oogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements d...
Drosophila virilis (Fruit fly)
B4LY29
RAS1_DROVI
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLASWNVQNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRKGRKTNKPNRRFKCKML
3.6.5.2
null
border follicle cell migration [GO:0007298]; cellular response to starvation [GO:0009267]; chorion-containing eggshell pattern formation [GO:0030381]; defense response to virus [GO:0051607]; determination of adult lifespan [GO:0008340]; dorsal closure, spreading of leading edge cells [GO:0007395]; epidermal growth fact...
membrane [GO:0016020]; plasma membrane [GO:0005886]
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; protein serine/threonine kinase activator activity [GO:0043539]
PF00071;
3.40.50.300;
Small GTPase superfamily, Ras family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08646}; Lipid-anchor {ECO:0000250|UniProtKB:P08646}; Cytoplasmic side {ECO:0000250|UniProtKB:P08646}.
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112};
null
null
null
null
FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells. During larval development, mediates Ptth/tor signaling leading to the production of ecdysone, a hormo...
Drosophila virilis (Fruit fly)
B4LZT9
HH_DROVI
MDNQTVAAIWSCASATCLSLDAKRHSVETNTNDRQAPPGLSNSNNNNNNNKSTAVDADPRKLRHIAHTPRGSCFMALLLLLLLALNFRHAHSCGPGRGLGRRRERNLYPLVLKQTVPNLSEYMSGASGPIEGVIQRDSPNFKDLVPNYNRDIIFRDEEGTGADRLMSKRCREKLNTLSYSVMNEWPGVRLLVTESWDEDHQHGQESLHYEGRAVTIATSDRDQSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSPFISHVHGCFTPESTALLESGAKKPLSELAIGDRVLSMNGKGQAVYSEVILFMDRNLEQMQN...
3.1.-.-
null
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; cell-cell signaling involved in cell fate commitment [GO:0045168]; intein-mediated protein splicing [GO:0016539]; protein autoprocessing [GO:0016540]; regulation of gene expression [GO:0010468]; segment polarity determination [GO:000...
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
PF01085;PF01079;
3.30.1380.10;2.170.16.10;
Hedgehog family
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results ...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR ...
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI...
null
null
null
null
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that res...
Drosophila virilis (Fruit fly)
B4M0H8
SPAST_DROVI
MVRTKNQSSSSSASSSTKSPVKISGGGGGGGGSSSSTNRSRSCSEALIDDGKSSSKLSSNRQRTTTTITTTTTTPGSSPDDDTTDADLTPTSGNVPRGGQSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRSPHRRDCNIEIVVQNSKEQQAIICPLEGSGVNIEQAQILPQRQRALQTLEMAASRGGTGAGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHEKMQTNLSMARDRLHFLALREEDLQMQRLSLKEQPKKQ...
5.6.1.1
null
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regul...
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
PF00004;PF17862;PF09336;
1.10.8.60;3.40.50.300;1.20.58.80;
AAA ATPase family, Spastin subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-...
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
null
null
null
null
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Inv...
Drosophila virilis (Fruit fly)
B4M709
SWS_DROVI
MDVLELLRASANGCYNTLFSDAWFQYVSKQIATTMYWYGALLVIGVLFIAWFLYFKRLARLRLRDEIARSLSAVTSSGGDHRGLRFRKRDKMLFYGRRMLRKMKNVSGQMYSSGKGYKRRAVMRFARRILQLQRENRPLEMKTVEPPAEYLEETIEGSDRVPPDALYMLQSIRIFGHFEKPIFLKLCKHTQLLQLMAGDYLFKITDPDDSVYIVQSGMINVYICNADGSTLSLKTVRKGESVTSLLSFIDVLSGNSSYYKTVTAKAMEKSVVIRLPMQAFEEVFEENPDVMIRVIQVIMIRLQRVLFTALRNYLGLNAEL...
3.1.1.5
null
ensheathment of neurons [GO:0007272]; glial cell apoptotic process [GO:0034349]; lipid catabolic process [GO:0016042]; membrane lipid metabolic process [GO:0006643]; membrane organization [GO:0061024]; neuron apoptotic process [GO:0051402]; phosphatidylcholine metabolic process [GO:0046470]; photoreceptor cell maintena...
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; protein kinase A catalytic subunit binding [GO:0034236]
PF00027;PF01734;
3.40.1090.10;2.60.120.10;
NTE family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9U969}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9U969}. Note=Sws tethers Pka-C3 to the membrane. {ECO:0000250|UniProtKB:Q9U969}.
CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:Q9U969};
null
null
null
null
FUNCTION: Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy. Plays a role in...
Drosophila virilis (Fruit fly)
B4MR28
PTK7_DROWI
MDMLMMWSICLFVCIFMAPFSCGSGSSSRFIQVPESQSIVENDSVDFNCEATTDPSTDLHYEWLHNGHQIVYDKRVYQIGANLHIESVQRGEDVGDYVCIAMSLSSGAREASPTAKLSVIFLDSASVQLLGSNRNELLLKCHVEGASGNEALQIEWYRNSAKLSSWQNIELDEHRLLVRQPTGSDDGLYRCIASNAAGRVMSKQGFVYQHQQQQQAGAKCLPRLKKNQKFLPESWGKQIFLCRGKRGGNVEAGLAPSPEGLRLVQGPDDQITIKEGEPATLSCLYEIPAELQNQRIQLRWRKDGKLLRQVELGASLPRGM...
null
null
cell adhesion [GO:0007155]; imaginal disc-derived female genitalia morphogenesis [GO:0048804]; imaginal disc-derived male genitalia morphogenesis [GO:0048803]; internal genitalia morphogenesis [GO:0035260]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; photoreceptor cell axon guidance [GO:0072499...
axon [GO:0030424]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; signaling receptor activity [GO:0038023]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; W...
PF07679;PF13927;PF07714;
2.60.40.10;1.10.510.10;
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6AWJ9}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6AWJ9}.
null
null
null
null
null
FUNCTION: Acts as a calcium-dependent, homophilic cell adhesion molecule that regulates neural recognition during the development of the nervous system. Component of the repulsive Plexin signaling response to regulate motor axon guidance at the embryonic stage. Also component of a receptor complex that is required in t...
Drosophila willistoni (Fruit fly)
B4MUQ2
FICD_DROWI
MPWEFLKKCDRQKAEVRGEKEEQEPVPGNPHFQVQFHVTSCRFAFLAFLAGSFLAFSLHALISSNLFWRLRQLHHLPTAHYLQTRDEFAVYSVDELNAFKEFYDKSTADSVGATYTEAEETNIKEALSSLRLAQDMYMAGKDDKAARLFEHALALAPRHPEVLLRYGEFLEHNQRNIVLADQYYFQALTINPSHSEALANRQRTADVVQTLDERRLASLDAKRAALSAIHEANSALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKLEITIKDILELHRRVLGH...
2.7.7.108; 3.1.4.-
null
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
plasma membrane [GO:0005886]
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
PF02661;
1.10.3290.10;1.25.40.10;
Fic family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV...
null
null
null
null
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-255 determines which of the two op...
Drosophila willistoni (Fruit fly)
B4MXR8
PLK4_DROWI
MLPVRNYGETIEEYEVQHLLGKGGFASVYKARCRRTYQDVAIKMIDKKLIHGTGLSSRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNQQMSHPFTEADAATILQQVVAGLLYLHSHNIMHRDISLSNLLLSKDMHVKIADFGLATQLKRPDEKHMTMCGTPNFISPEVVSRLSHGLAADVWSVGCLLYTLVVGRPPFDTDAVQSTLNKVVMSEFIMPTHLSFEACDLIEKLLKKNPHERISLEQVLRHPFMSKRSAGAEEPQYNSSKPGACDFYMEAQGQSVASGDSGIVTFASNESRSSQRL...
2.7.11.21
null
centriole replication [GO:0007099]; male meiotic nuclear division [GO:0007140]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of protein catabolic process [GO:0045732]; regulation of centriole replication [GO:0046599]; regulation of protein stability [GO:0031647]; sperm ax...
centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; nucleus [GO:0005634]; spindle pole [GO:0000922]
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;PF18190;PF18409;
2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
PTM: Ubiquitinated by the SCF(Slimb) ubiquitin ligase complex; leading to its degradation by the proteasome during interphase and regulating centriole number and ensuring the block to centriole reduplication. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.21; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as sas-6. When overexpressed, it is...
Drosophila willistoni (Fruit fly)
B4N5D3
WLS_DROWI
MSGTILENLSGRKLSILVSILLLCQVLCFLLGGIFAPVPAGHLTILGSLCRENHARQNDTNFFLYSRGDGACKQVTSEEVDADALKLANQIVHVFQLPLPRENKILEYTRWQQNLIGVLQVEFGYDSSPELHEPAKELQLTIDMRLAYRNNDDADNDWKLYAHSVEHRYLDCDTSHIGPTETLYTCDMIPLFELGALHHSFYLLNLRFPLDSPKQMNLQFGHMHDLTLTAIHQNGGFTKVWLFLKSVLFPFVVGIMVWFWRRVHLLQRSPALLEYMLIYLGGALTFLNLPLEYLTLGLEMPYMLLLSDIRQGIFYAMLLS...
null
null
compound eye morphogenesis [GO:0001745]; cuticle pattern formation [GO:0035017]; Golgi to plasma membrane protein transport [GO:0043001]; imaginal disc-derived leg morphogenesis [GO:0007480]; imaginal disc-derived wing margin morphogenesis [GO:0008587]; intracellular protein transport [GO:0006886]; positive regulation ...
cell projection [GO:0042995]; early endosome [GO:0005769]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; multivesicular body [GO:0005771]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membr...
Wnt-protein binding [GO:0017147]
PF06664;
null
Wntless family
null
SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q95ST2}. Cell membrane {ECO:0000250|UniProtKB:Q95ST2}; Multi-pass memb...
null
null
null
null
null
FUNCTION: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to ...
Drosophila willistoni (Fruit fly)
B4NBP4
SPAST_DROWI
MVRTKSSSSSASSSSQKSPIKSNNGAGGGGSSSSHRQSHRTSIDERKSSSHAHSNNSNVSSSSRRAATATSGSSSPEGDDDTTTDDLTPTGSSPRSCNGRGHSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVLYRPHRRDCNIEIVVQNSKEQQLQLQQHQHNQTLSYSLETGGVSGGSGGEQQVQVQPQRIRALQPLEMATNRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWNGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREEDL...
5.6.1.1
null
adult locomotory behavior [GO:0008344]; cell division [GO:0051301]; hemocyte migration [GO:0035099]; microtubule severing [GO:0051013]; mitotic chromosome movement towards spindle pole [GO:0007079]; mitotic spindle elongation [GO:0000022]; negative regulation of microtubule depolymerization [GO:0007026]; negative regul...
centrosome [GO:0005813]; chromosome [GO:0005694]; lipid droplet [GO:0005811]; membrane [GO:0016020]; microtubule [GO:0005874]; neuromuscular junction [GO:0031594]; spindle [GO:0005819]; synaptic vesicle [GO:0008021]; terminal bouton [GO:0043195]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
PF00004;PF17862;PF09336;
1.10.8.60;3.40.50.300;1.20.58.80;
AAA ATPase family, Spastin subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000255|HAMAP-...
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03021};
null
null
null
null
FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Inv...
Drosophila willistoni (Fruit fly)
B4NJP3
HH_DROWI
MDSQSNQTPWASASVTCLSLDAKRHSQCLDDAIKSGHQVNYSPARSLRYIAYTQRCGIRLTMLMLIMCLTFMPAHSCGPGRGLGRRRVQNLYPLVLKQTVPNLSEHQLGASGPLEGEIPRDSPKFKDLVPNYNRDIVFKDEEGTGADRLMTKRCREKLNALAYSVMNEWPGVRLLVIESWDEDHDHGQESLHYEGRAVTIGTNDRDLSKYGMLARLAVEAGFDWVSYVSRRHIYCSVKSDSSTISHVHGCFTPESTAQMENGEKKPLSQLSIGDRVLSMGSNGQPVYSEVILFMDRNLEQLENFVQLHTDGGAVLTVTPA...
3.1.-.-
null
anatomical structure morphogenesis [GO:0009653]; cell fate specification [GO:0001708]; cell-cell signaling involved in cell fate commitment [GO:0045168]; intein-mediated protein splicing [GO:0016539]; protein autoprocessing [GO:0016540]; regulation of gene expression [GO:0010468]; segment polarity determination [GO:000...
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]; cholesterol-protein transferase activity [GO:0140853]; morphogen activity [GO:0016015]; patched binding [GO:0005113]; peptidase activity [GO:0008233]
PF01085;PF01079;
3.30.1380.10;2.170.16.10;
Hedgehog family
PTM: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that results ...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q02936}. Cytoplasm {ECO:0000250|UniProtKB:Q02936}. Note=Nuclear up to embryonic stage 10 and then at stage 11 shifts to the cytoplasm. Also secreted in either cleaved or uncleaved form to mediate signaling to other cells. {ECO:0000250|UniProtKB:Q02936}.; SUBCELLULAR ...
CATALYTIC ACTIVITY: [Protein hedgehog]: Reaction=cholesterol + glycyl-L-cysteinyl-[protein] + H(+) = [protein]-C-terminal glycyl cholesterol ester + N-terminal L-cysteinyl-[protein]; Xref=Rhea:RHEA:59504, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:15369, Rhea:RHEA-COMP:15374, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI...
null
null
null
null
FUNCTION: [Protein hedgehog]: The C-terminal part of the hedgehog protein precursor displays an autoproteolysis activity that results in the cleavage of the full-length protein into two parts (N-product and C-product) (By similarity). In addition, the C-terminal part displays a cholesterol transferase activity that res...
Drosophila willistoni (Fruit fly)
B4NZY8
IHOG_DROYA
MTLLTSSLLFFSLLTSRLEAIPVLEKSPAHPAHSAHPAHPSHPSPGVRILRAPESLVAPLGDEVVLECETSLQPERFEWSHRSSRSSGAGFKYLRTGTAKANVSQEAAISRLKVLVRQDTLGEYRCVGWFGPLVVTSTIARLELASTSLLGGQESESPLQWRVSAGNSVLWPCGKQVKSNPSASWSYYRNGVEIKPEFIGTNGNIFLSNVSSESSGSYSCQATNPASGERIQLTGSLQLQVTPEQRSQSKSPHLLNGQPNSQEITIREGSSLLLLCPGVGSPPPTVVWSSPDVVGAVKNKRSKVIGHALEISNTRVQDAG...
null
null
compound eye development [GO:0048749]; cuticle pattern formation [GO:0035017]; homotypic cell-cell adhesion [GO:0034109]; maintenance of protein location in extracellular region [GO:0071694]; segment specification [GO:0007379]; smoothened signaling pathway [GO:0007224]; wing disc anterior/posterior pattern formation [G...
cell surface [GO:0009986]; cytoneme [GO:0035230]; membrane [GO:0016020]; plasma membrane [GO:0005886]
coreceptor activity [GO:0015026]; hedgehog family protein binding [GO:0097108]; heparin binding [GO:0008201]; patched binding [GO:0005113]; protein homodimerization activity [GO:0042803]
PF00041;PF13895;PF13927;
2.60.40.10;
Immunoglobulin superfamily, IHOG family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9VM64, ECO:0000255}.
null
null
null
null
null
FUNCTION: Mediates response to the active Hedgehog (Hh) protein signal in embryos, functioning upstream or at the level of patched (ptc). {ECO:0000250|UniProtKB:Q9VM64}.
Drosophila yakuba (Fruit fly)
B4P0E1
FICD_DROYA
MGTEAEQPSPPSPPAQQQEQTNPPLWNAQNQKPARLYRLVLFFIAGSLAAWTIHALSNSNLVWKLRQLHHLPTAHYLQTRDEFAVYSVEELNAFKEIYDKSVSDSVGASYTKDEQTSINEALVSLRMAQDMYLAGKDDKASRLFEHALALAPRHPEVLLRYGEFLEHSQRNIVLADQYYFQALTISPSNSEALANRQRTADVVQTLDERRLQSLDSKRDALSAIHESNGALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKIDITIKDILELHRRVLGHVDPIE...
2.7.7.108; 3.1.4.-
null
detection of light stimulus involved in visual perception [GO:0050908]; histamine transport [GO:0051608]; protein adenylylation [GO:0018117]; response to endoplasmic reticulum stress [GO:0034976]; visual behavior [GO:0007632]
plasma membrane [GO:0005886]
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; protein adenylylhydrolase activity [GO:0044603]; protein homodimerization activity [GO:0042803]
PF02661;
1.10.3290.10;1.25.40.10;
Fic family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8SWV6}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8SWV6}.
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV...
null
null
null
null
FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-250 determines which of the two op...
Drosophila yakuba (Fruit fly)