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Database: UniProt
Entry: M3ZTX2_XIPMA
LinkDB: M3ZTX2_XIPMA
Original site: M3ZTX2_XIPMA 
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
//
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