MX1_RAT
ID MX1_RAT Reviewed; 652 AA.
AC P18588;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 129.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=2173790; DOI=10.1128/jvi.64.12.6263-6269.1990;
RA Meier E., Kunz G., Haller O., Arnheiter H.;
RT "Activity of rat Mx proteins against a rhabdovirus.";
RL J. Virol. 64:6263-6269(1990).
RN [2]
RP PROTEIN SEQUENCE OF 148-175, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [3]
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 which has antiviral
CC activity against influenza A virus, (IAV) and Thogoto virus (THOV).
CC Inhibits IAV by interefering with the process of primary transcription,
CC probably by affecting the viral polymerase function (By similarity).
CC {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: Nucleus {ECO:0000269|PubMed:2173790}. Cytoplasm
CC {ECO:0000250|UniProtKB:P20591}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P20591}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P20591}; Cytoplasmic side
CC {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; X52711; CAA36935.1; -; mRNA.
DR PIR; S11735; S11735.
DR AlphaFoldDB; P18588; -.
DR SMR; P18588; -.
DR STRING; 10116.ENSRNOP00000043001; -.
DR PaxDb; P18588; -.
DR UCSC; RGD:3127; rat.
DR RGD; 3127; Mx1.
DR eggNOG; KOG0446; Eukaryota.
DR InParanoid; P18588; -.
DR PhylomeDB; P18588; -.
DR PRO; PR:P18588; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0140374; P:antiviral innate immune response; ISO:RGD.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0070106; P:interleukin-27-mediated signaling pathway; ISO:RGD.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISO:RGD.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Antiviral defense; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; GTP-binding; Immunity; Innate immunity; Membrane;
KW Nucleotide-binding; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..652
FT /note="Interferon-induced GTP-binding protein Mx1"
FT /id="PRO_0000206595"
FT DOMAIN 58..331
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 564..652
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..75
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 93..95
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 169..172
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 238..241
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 270..273
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 332..357
FT /note="Bundle signaling element (BSE)"
FT /evidence="ECO:0000250"
FT REGION 357..526
FT /note="Middle domain"
FT /evidence="ECO:0000250"
FT REGION 358..622
FT /note="Stalk"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68..75
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 169..173
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 238..241
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 652 AA; 74469 MW; 603468914B0C6F6F CRC64;
MKERTSACRH GTPQKHPDTS EESQAMESVD NLCSQYEEKV RPCIDLIDSL RALGVEQDLA
LPAIAVIGDQ SSGKSSVLEA LSGVALPRGS GIVTRCPLVL KLKQLKQGEK WSGKVIYKDT
EIEISHPSLV EREINKAQNL IAGEGLKISS DLISLEVSSP HVPDLTLIDL PGITRVAVGD
QPADIEHKIK RLITEYIQKQ ETINLVVVPS NVDIATTEAL KMAQEVDPQG DRTIGILTKP
DLVDRGTEDK VVDVVRNLVC HLKKGYMIVK CRGQQDIQEQ LSLAEALQKE QVFFKEHPQF
RVLLEDGKAT VPCLAKRLTM ELTSHICKSL PILENQINVN HQIASEELQK YGADIPEDDS
KRLSFLMNKI NVFNKDILSL VQAQENISWE ESRLFTKLRN EFLAWNDYIE EHFKKTLGSS
EKHSQMEKFE SHYRGRELPG FVDYKAFENI IKKEVKALEE PALNMLHRVT TMVKNAFTKV
SSNNFGDFLN LHSTAKSKIE DIRFNQEKEA EKLIRLHFQM EHIVYCQDQA YKKALQEIRE
KEAEKEKSTF GAFQHNSPRK ELTTTEMTQH LNAYYQECGR NIGRQIPLII QYSILQTFGQ
EMEKAMLQLL QDTSKCNWFL TEQSDSREKK KFLKRRLLRL DEAQRKLAKF SN
