MX1_PONAB
ID MX1_PONAB Reviewed; 662 AA.
AC Q5R5G3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Interferon-induced GTP-binding protein Mx1;
DE AltName: Full=Myxoma resistance protein 1;
DE AltName: Full=Myxovirus resistance protein 1;
GN Name=MX1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP REVIEW, AND INDUCTION.
RX PubMed=18062906; DOI=10.1016/j.micinf.2007.09.010;
RA Haller O., Stertz S., Kochs G.;
RT "The Mx GTPase family of interferon-induced antiviral proteins.";
RL Microbes Infect. 9:1636-1643(2007).
CC -!- FUNCTION: Interferon-induced dynamin-like GTPase with antiviral
CC activity. {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Oligomerizes into multimeric filamentous or
CC ring-like structures by virtue of its stalk domain. Oligomerization is
CC critical for GTPase activity, protein stability, and recognition of
CC viral target structures (By similarity). Interacts with TRPC1, TRPC3,
CC TRPC4, TRPC5, TRPC6 and TRPC7 (By similarity). Interacts with HSPA5 (By
CC similarity). Interacts with TUBB/TUBB5 (By similarity). Interacts with
CC DDX39A and DDX39B (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P20591}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20591};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P20591}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P20591}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P20591}. Note=Binds preferentially to negatively
CC charged phospholipids. {ECO:0000250|UniProtKB:P20591}.
CC -!- INDUCTION: By type I and type III interferons.
CC {ECO:0000269|PubMed:18062906}.
CC -!- DOMAIN: The C-terminal GTPase effector domain (GED) is involved in
CC oligomerization and viral target recognition. {ECO:0000250}.
CC -!- DOMAIN: The middle domain mediates self-assembly and oligomerization.
CC {ECO:0000250}.
CC -!- PTM: ISGylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
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DR EMBL; CR860897; CAH93003.1; -; mRNA.
DR RefSeq; NP_001127618.1; NM_001134146.1.
DR AlphaFoldDB; Q5R5G3; -.
DR SMR; Q5R5G3; -.
DR STRING; 9601.ENSPPYP00000012765; -.
DR GeneID; 100174697; -.
DR KEGG; pon:100174697; -.
DR CTD; 4599; -.
DR eggNOG; KOG0446; Eukaryota.
DR InParanoid; Q5R5G3; -.
DR OrthoDB; 494748at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR11566; PTHR11566; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Antiviral defense; Cytoplasm; Endoplasmic reticulum;
KW GTP-binding; Immunity; Innate immunity; Membrane; Nucleotide-binding;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..662
FT /note="Interferon-induced GTP-binding protein Mx1"
FT /id="PRO_0000319956"
FT DOMAIN 67..340
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 574..662
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 77..84
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 102..104
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 178..181
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 247..250
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 279..282
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 341..366
FT /note="Bundle signaling element (BSE)"
FT /evidence="ECO:0000250"
FT REGION 366..533
FT /note="Middle domain"
FT /evidence="ECO:0000250"
FT REGION 367..632
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT REGION 554..557
FT /note="Critical for lipid-binding"
FT /evidence="ECO:0000250"
FT BINDING 77..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 178..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 247..250
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P20591"
SQ SEQUENCE 662 AA; 75486 MW; CD42B0E2568B4B5F CRC64;
MVLSEVDIAK ADPAAASHPV LLNGDANVAQ KNLGSVAENN LCSQYEEKVR PCIDLIDSLR
ALGVEQDLAL PAIAVIGDQS SGKSSVLEAL SGVALPRGSG IVTRCPLVLK LKKLVNEDKW
RGKVSYQDYE IEISDASEVE KEINKAQNTI AGEGMGISHE LITLEISSRD VPDLTLIDLP
GITRVAVGNQ PADIGYKIKT LIKKYIQRQE TISLVVVPSN VDIATTEALS MAQEVDPEGD
RTIGILTKPD LVDKGTEDKV VDVVRNLVFH LKKGYMIVKC RGQQEIQDQL SLSEALQREK
IFFEDHPYFR DLLEEGKATV PCLAEKLTSE LITHICKSLP LLENQIRESH QRITEELQKY
GVDVPEDENE KMFFLIDKIN AFNQDITALI QGEETVGEED IRLFTRLRHE FHKWSIIIEN
NFQEGHKILS RKIQKFENQY RGRGLPGFVN YRTFETIVKQ QIKALEEPAV DMLHTVTDMV
RLAFTDVSIK NFEEFFNLHR TAKSKIEDIR AEQEREGEKL IRLHFQMEQI VYCQDQVYRG
ALQKVREKEL EEEKKKKSWD FGAFQSSSAT DSSMEEIFQH LMAYHQEASK RISSHIPLII
QFFMLQTYGQ QLQKAMLQLL QDKDTYSWLL KERGDTSDKR KFLKERLARL TQARRRLAQF
PG
