ID M3ZTX2_XIPMA Unreviewed; 858 AA.
AC M3ZTX2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Interferon-induced GTP-binding protein Mx {ECO:0000256|ARBA:ARBA00015210};
DE EC=3.6.5.5 {ECO:0000256|ARBA:ARBA00011980};
DE AltName: Full=Interferon-inducible Mx protein {ECO:0000256|ARBA:ARBA00031810};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000005665.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000005665.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000005665.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001837};
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; M3ZTX2; -.
DR Ensembl; ENSXMAT00000005671.2; ENSXMAP00000005665.2; ENSXMAG00000005602.2.
DR eggNOG; KOG0446; Eukaryota.
DR GeneTree; ENSGT00940000155214; -.
DR HOGENOM; CLU_008964_1_1_1; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd08771; DLP_1; 1.
DR CDD; cd01256; PH_dynamin; 1.
DR Gene3D; 1.20.120.1240; Dynamin, middle domain; 2.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, 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|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003932};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852}.
FT DOMAIN 28..294
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 529..635
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 670..761
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 641..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..847
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 96512 MW; CA24AB9FDA45D7EF CRC64;
MGNRGMEDLI PLVNRMQDAF SAIGQNANLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
SGIVTRRPLV LQLMNCPTEH AEFLHCKGKK FTDFDEVRQE IEAETDRITG ANKGISPVPI
NLRVYSPHVL NLTLVDLPGM TKVPVGDQPA DIEAQIRDML LQFVTKENCL MLAVSPANSD
LANSDALKIA KEVDPQGMRT IGVITKLDLM DEGTDAKDIL ENKLLPLRRG YIGVVNRSQK
DIDGKKDINA AIAAERKFFL THPAYRHLAE RMGTPYLQKV LNQQLTNHIR DTLPGLRAKL
QSQLLSIEKE VEEYKNFRPD DPSRKTKALL QMVQQFSVDF EKCIEGSGDQ IDTAELSGGA
RINRIFHERF PFELVKMEFD EKELRKEISY AIKNIHGIRT GLFTPDMAFE TIVKRQIGKI
KEPCTKCVDM VISELVNTVR QCTKKLAQYP MLREEMERIV TQHIRDRENR TKGQVLLLID
IELSYMNTNH EDFIGFANAQ QRINQMNKKK TAGNQDEIMP ERGVNDRYKV IRKGWLTINN
IGIMKGGAKE YWFVLTAESL SWYKDDEEKE KKYMLPVDNL KLRDVEKGFM SSKHIFALFN
TEQRNVYKDY RQLELACESQ EDVDAWKASF LRAGVYPERV TEKEGKSEGS DENGSDNFMH
SMDPQLERQV ETIRNLVDSY MAIVNKTVRD LIPKTVMHLM INNTKEFINA ELLAQLYSCG
DQNTLMEESQ EQAQHRDEML RMYHALREAL SIIGDISTTT VSTSMPPPVD DSWLQVQRGG
SGGRSPATSP TPNRRAPPGP PARPGSRGPP PGPPPAGGPP VPSRPGASPD PHGGPPPTVP
SRPNRAPPSV PRITITDR
//