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Database: UniProt
Entry: G3TQQ5_LOXAF
LinkDB: G3TQQ5_LOXAF
Original site: G3TQQ5_LOXAF 
ID   G3TQQ5_LOXAF            Unreviewed;       845 AA.
AC   G3TQQ5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=dynamin GTPase {ECO:0000256|ARBA:ARBA00011980};
DE            EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
GN   Name=DNM1 {ECO:0000313|Ensembl:ENSLAFP00000017903.2};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000017903.2, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000017903.2, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017903.2,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000017903.2}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017903.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC       superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
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DR   AlphaFoldDB; G3TQQ5; -.
DR   STRING; 9785.ENSLAFP00000017903; -.
DR   Ensembl; ENSLAFT00000022770.2; ENSLAFP00000017903.2; ENSLAFG00000005112.4.
DR   eggNOG; KOG0446; Eukaryota.
DR   GeneTree; ENSGT00940000155214; -.
DR   HOGENOM; CLU_008964_1_1_1; -.
DR   InParanoid; G3TQQ5; -.
DR   OMA; MQMVQTF; -.
DR   TreeFam; TF300362; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0030117; C:membrane coat; IEA:Ensembl.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR   GO; GO:0098684; C:photoreceptor ribbon synapse; IEA:Ensembl.
DR   GO; GO:0098835; C:presynaptic endocytic zone membrane; IEA:Ensembl.
DR   GO; GO:0019003; F:GDP binding; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:Ensembl.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR   GO; GO:0099049; P:clathrin coat assembly involved in endocytosis; IEA:Ensembl.
DR   GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR   GO; GO:0097494; P:regulation of vesicle size; IEA:Ensembl.
DR   GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IEA:Ensembl.
DR   GO; GO:0099050; P:vesicle scission; IEA:Ensembl.
DR   CDD; cd08771; DLP_1; 1.
DR   CDD; cd01256; PH_dynamin; 1.
DR   Gene3D; 1.20.120.1240; Dynamin, middle domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR019762; Dynamin_GTPase_CS.
DR   InterPro; IPR045063; Dynamin_N.
DR   InterPro; IPR000375; Dynamin_stalk.
DR   InterPro; IPR030381; G_DYNAMIN_dom.
DR   InterPro; IPR003130; GED.
DR   InterPro; IPR020850; GED_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR11566; DYNAMIN; 1.
DR   PANTHER; PTHR11566:SF32; DYNAMIN-1; 1.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS00410; G_DYNAMIN_1; 1.
DR   PROSITE; PS51718; G_DYNAMIN_2; 1.
DR   PROSITE; PS51388; GED; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW   GTP-binding {ECO:0000256|RuleBase:RU003932};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003932};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT   DOMAIN          28..294
FT                   /note="Dynamin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51718"
FT   DOMAIN          520..626
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          660..751
FT                   /note="GED"
FT                   /evidence="ECO:0000259|PROSITE:PS51388"
FT   REGION          751..845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..782
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..845
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   845 AA;  95235 MW;  0DB9FD867AE1D55C CRC64;
     MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
     SGIVTRRPLV LQLVNATTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI
     NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD
     LANSDALKIA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
     DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKI LNQQLTNHIR DTLPGLRNKL
     QSQLLSIEKE VDEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA
     RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRH TGLFTPDLAF EATVKKQVQK
     LKEPSIKCVD MVVSELTATI RKCSEKLQQY PRLREEMERI VTTHIREREG RTKEQVMLLI
     DIELAYMNTN HEDFIGFANA QQRSNQMNKK KASGNQVREG VIRKGWLTIS NIGIMKGGSK
     EYWFVLTAEN LSWYKDDEEK EKKYMLSVDN LKLRDVEKGF MSSKHIFALF NTEQRNVYKD
     YRQLELACET QEEVDSWKAS FLRAGVYPER VGDKEKASET EENGSDNFMH SMDPQLERQV
     ETIRNLVDSY MAIVNKTVRD LMPKTIMHLM INNTKEFIFS ELLANLYSCG DQNTLMEESA
     EQAQRRDEML RMYHALKEAL SIIGDINTTT VSTPMPPPVD DSWLQVQSVP TGRRSPTSSP
     TPQRRAPAVP PARPGSRGPA PGPPPAGSAL GGAPPVPSRP GASPDPFGPP PQVPSRPNRA
     PPGVP
//
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