TORS_CAEEL
ID TORS_CAEEL Reviewed; 356 AA.
AC Q95NU5; Q95NY6;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Torsin-like protein;
DE AltName: Full=Abnormal oocyte formation protein 5;
DE Flags: Precursor;
GN Name=ooc-5; ORFNames=C18E9.11;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RA Basham S.E., Rose L.S.;
RT "OOC-5, required for polarity in the 2-cell embryo, encodes a AAA+ ATPase
RT related to the human disease protein Torsin A.";
RL (In) Proceedings of the 13th international C. elegans meeting, pp.159-159,
RL Los Angeles (2001).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: May serve as a molecular chaperone assisting in the proper
CC folding of secreted and/or membrane proteins. {ECO:0000269|Ref.2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|Ref.2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=Q95NU5-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q95NU5-2; Sequence=VSP_001107;
CC -!- DISRUPTION PHENOTYPE: Worms show defects in asymmetric divisions in
CC early embryos. In particular, mutations specifically affect the
CC reestablishment of asymmetric PAR protein domains in the P1 cell at the
CC 2-cell stage. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.
CC {ECO:0000305}.
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DR EMBL; Z70034; CAC44293.1; -; Genomic_DNA.
DR EMBL; Z49910; CAC44293.1; JOINED; Genomic_DNA.
DR EMBL; Z70034; CAC44294.1; -; Genomic_DNA.
DR EMBL; Z49910; CAC44294.1; JOINED; Genomic_DNA.
DR RefSeq; NP_495916.1; NM_063515.1. [Q95NU5-1]
DR RefSeq; NP_495917.1; NM_063516.3. [Q95NU5-2]
DR AlphaFoldDB; Q95NU5; -.
DR SMR; Q95NU5; -.
DR BioGRID; 39760; 1.
DR STRING; 6239.C18E9.11b; -.
DR iPTMnet; Q95NU5; -.
DR EPD; Q95NU5; -.
DR PaxDb; Q95NU5; -.
DR PeptideAtlas; Q95NU5; -.
DR EnsemblMetazoa; C18E9.11a.1; C18E9.11a.1; WBGene00003870. [Q95NU5-2]
DR EnsemblMetazoa; C18E9.11b.1; C18E9.11b.1; WBGene00003870. [Q95NU5-1]
DR GeneID; 174433; -.
DR KEGG; cel:CELE_C18E9.11; -.
DR UCSC; C18E9.11a; c. elegans. [Q95NU5-1]
DR CTD; 174433; -.
DR WormBase; C18E9.11a; CE28283; WBGene00003870; ooc-5. [Q95NU5-2]
DR WormBase; C18E9.11b; CE28284; WBGene00003870; ooc-5. [Q95NU5-1]
DR eggNOG; KOG2170; Eukaryota.
DR GeneTree; ENSGT00950000182888; -.
DR InParanoid; Q95NU5; -.
DR OMA; HFPHRSE; -.
DR OrthoDB; 1453168at2759; -.
DR PhylomeDB; Q95NU5; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR PRO; PR:Q95NU5; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003870; Expressed in embryo and 3 other tissues.
DR GO; GO:0005818; C:aster; IDA:WormBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:WormBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IEA:InterPro.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005819; C:spindle; IDA:WormBase.
DR GO; GO:0000922; C:spindle pole; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0071218; P:cellular response to misfolded protein; IDA:WormBase.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010448; Torsin.
DR InterPro; IPR030553; Torsin-like.
DR InterPro; IPR017378; Torsin_1/2.
DR PANTHER; PTHR10760; PTHR10760; 1.
DR PANTHER; PTHR10760:SF2; PTHR10760:SF2; 1.
DR Pfam; PF06309; Torsin; 1.
DR PIRSF; PIRSF038079; Torsin_2A; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Endoplasmic reticulum; Glycoprotein;
KW Nucleotide-binding; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..356
FT /note="Torsin-like protein"
FT /id="PRO_0000005511"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 26..31
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_001107"
SQ SEQUENCE 356 AA; 40814 MW; 4D83C971D5349BDE CRC64;
MKLDYVLLLL FHLCFVNTEL ISVITGKIKD SGTTIAISAG AFWGLKDRLK CYLYECCHEP
DVNFNYHTLD ADIANLLFGQ HLVKDVVVNS IKSHWYNENP RKPLVLSFHG YTGSGKNYVA
EIIANNTFRL GLRSTFVQHI VATNDFPDKN KLEEYQVELR NRILTTVQKC QRSIFIFDEA
DKLPEQLLGA IKPFLDYYST ISGVDFRRSI FILLSNKGGG EIARITKEQY ESGYPREQLR
LEAFERELMN FSYNEKGGLQ MSELISNHLI DHFVPFLPLQ REHVRSCVGA YLRKRGRGDL
VSNVDFVERV LNSLQYFPES SKAFSSSGCK RVDAKTDLEM AKIRPLLSSV HFDDEL
