ID   TOR2A_XENLA             Reviewed;         314 AA.
AC   Q68F68;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Torsin-2A;
DE   AltName: Full=Torsin family 2 member A;
DE   Flags: Precursor;
GN   Name=tor2a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC079976; AAH79976.1; -; mRNA.
DR   RefSeq; NP_001087470.1; NM_001094001.1.
DR   AlphaFoldDB; Q68F68; -.
DR   SMR; Q68F68; -.
DR   DNASU; 447294; -.
DR   GeneID; 447294; -.
DR   KEGG; xla:447294; -.
DR   CTD; 447294; -.
DR   Xenbase; XB-GENE-6254129; tor2a.L.
DR   OrthoDB; 611758at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 447294; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010448; Torsin.
DR   InterPro; IPR017378; Torsin_1/2.
DR   PANTHER; PTHR10760; PTHR10760; 1.
DR   Pfam; PF06309; Torsin; 1.
DR   PIRSF; PIRSF038079; Torsin_2A; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Endoplasmic reticulum; Glycoprotein; Nucleotide-binding;
KW   Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..314
FT                   /note="Torsin-2A"
FT                   /id="PRO_0000228832"
FT   BINDING         86..93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   314 AA;  35945 MW;  AF8DAAA3AC534135 CRC64;
     MAVRWWIIPM LLLVPGSSGA WEVLSLPFSL YNFYECGFKV DIEALDCDLA RNVFGQHLAQ
     ELLFKSVKEF IESDNPSKPL VLSLHGWSGT GKTFVSSLLV KHLFKEGSQS RFVHFFSPVL
     HFPRVQNLEQ YKVDLKGWIQ GNLTACGRSL FVFEEMDKMH PGLIDAIVPF LGTSWVVYGS
     NYRKAIFLFI SNAGGDDINE VALDFWRQRK DREDIRLHHL ESAISKAVFS NPKHGFWQSQ
     IINQHLIDVI VPFLPLRPSH VRQCVRTEMV QQGLEPEEVL VNNITDSFVY FPEDEKVFSS
     TGCKTVASRI NYFV