TOR3A_RAT
ID TOR3A_RAT Reviewed; 395 AA.
AC Q5M936;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Torsin-3A;
DE AltName: Full=Torsin family 3 member A;
DE Flags: Precursor;
GN Name=Tor3a;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- SUBUNIT: May not form homohexamers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum lumen
CC {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
CC {ECO:0000305}.
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DR EMBL; BC087678; AAH87678.1; -; mRNA.
DR RefSeq; NP_001009683.1; NM_001009683.1.
DR AlphaFoldDB; Q5M936; -.
DR SMR; Q5M936; -.
DR STRING; 10116.ENSRNOP00000005726; -.
DR GlyGen; Q5M936; 1 site.
DR jPOST; Q5M936; -.
DR PaxDb; Q5M936; -.
DR Ensembl; ENSRNOT00000005726; ENSRNOP00000005726; ENSRNOG00000004307.
DR GeneID; 304884; -.
DR KEGG; rno:304884; -.
DR UCSC; RGD:1310101; rat.
DR CTD; 64222; -.
DR RGD; 1310101; Tor3a.
DR eggNOG; KOG2170; Eukaryota.
DR GeneTree; ENSGT00950000182888; -.
DR HOGENOM; CLU_053537_0_0_1; -.
DR InParanoid; Q5M936; -.
DR OMA; EIAQMMV; -.
DR OrthoDB; 1453168at2759; -.
DR PhylomeDB; Q5M936; -.
DR TreeFam; TF314941; -.
DR PRO; PR:Q5M936; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000004307; Expressed in quadriceps femoris and 19 other tissues.
DR Genevisible; Q5M936; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:RGD.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010448; Torsin.
DR InterPro; IPR030552; Torsin-3A.
DR PANTHER; PTHR10760; PTHR10760; 1.
DR PANTHER; PTHR10760:SF3; PTHR10760:SF3; 1.
DR Pfam; PF06309; Torsin; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Endoplasmic reticulum; Glycoprotein;
KW Nucleotide-binding; Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..395
FT /note="Torsin-3A"
FT /id="PRO_0000228149"
FT BINDING 165..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 395 AA; 45166 MW; 2147EDAFD4466A7F CRC64;
MFFGAFWLLL LLLLPPLRPP GAQGHRGAKS PEQEADEPIP WPSIQRLREQ LRTAGTLSKR
YWALFSCTLW PDHCEDQETP VPPLGWSLPL WGRRSLDMLT SWFCRFQDCC SAGNCRISNN
FTGLESDLRV RLHGQHLASK LVLEAVKGYL EMPQVGKALA LSFHGWSGTG KNFVARMLVD
NLYRDGMRSD CVKMFISTFH FPHPKYVDLY KEDLQRQMQE TQRRCQQSTF VFDEAEKLHP
GLLELLEPYL EPRSPETHGA ELPRAIFLLL SNLGGSVINE VVLGLLKAGW SREEITLQHL
EMPLQAEIIK SADSSFGSSR LLKKHLIDLF IPFLPLEYRH VRLCVRDAFL GQDLPYTEEA
LDEIAKMMTY VPEEEQLFSS QGCKSISQRI NLVLP