TOIP2_RAT
ID TOIP2_RAT Reviewed; 578 AA.
AC Q6P752;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Torsin-1A-interacting protein 2;
GN Name=Tor1aip2;
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=Prostate;
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 -!- FUNCTION: Required for endoplasmic reticulum integrity. Regulates the
CC distribution of TOR1A between the endoplasmic reticulum and the nuclear
CC envelope as well as induces TOR1A, TOR1B and TOR3A ATPase activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TOR1A and TOR1B (ATP-bound). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Nucleus envelope
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TOR1AIP family. {ECO:0000305}.
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DR EMBL; BC061831; AAH61831.1; -; mRNA.
DR RefSeq; NP_954531.1; NM_199100.2.
DR RefSeq; XP_006250105.1; XM_006250043.3.
DR RefSeq; XP_006250106.1; XM_006250044.3.
DR RefSeq; XP_006250107.1; XM_006250045.3.
DR AlphaFoldDB; Q6P752; -.
DR SMR; Q6P752; -.
DR BioGRID; 258008; 1.
DR STRING; 10116.ENSRNOP00000039176; -.
DR GlyGen; Q6P752; 1 site.
DR iPTMnet; Q6P752; -.
DR PhosphoSitePlus; Q6P752; -.
DR PaxDb; Q6P752; -.
DR Ensembl; ENSRNOT00000050734; ENSRNOP00000039176; ENSRNOG00000024849.
DR GeneID; 304881; -.
DR KEGG; rno:304881; -.
DR UCSC; RGD:735059; rat.
DR CTD; 163590; -.
DR RGD; 735059; Tor1aip2.
DR eggNOG; ENOG502QUV7; Eukaryota.
DR GeneTree; ENSGT00390000012166; -.
DR HOGENOM; CLU_034263_1_1_1; -.
DR InParanoid; Q6P752; -.
DR OMA; DKTEHEN; -.
DR OrthoDB; 575658at2759; -.
DR PhylomeDB; Q6P752; -.
DR TreeFam; TF329438; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000024849; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q6P752; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:UniProtKB.
DR GO; GO:0090435; P:protein localization to nuclear envelope; ISO:RGD.
DR Gene3D; 3.40.50.12190; -; 1.
DR InterPro; IPR038599; LAP1C-like_C_sf.
DR InterPro; IPR008662; TOIP1/2.
DR PANTHER; PTHR18843; PTHR18843; 2.
DR Pfam; PF05609; LAP1C; 2.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..578
FT /note="Torsin-1A-interacting protein 2"
FT /id="PRO_0000228840"
FT TOPO_DOM 1..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 344..578
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..578
FT /note="Interaction with TOR1A"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFQ8"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFQ8"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFQ8"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFQ8"
FT MOD_RES 301
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFQ8"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 578 AA; 61698 MW; 841EFB9842F4F40A CRC64;
MSQTLKSQDT NMSDSGYRDP VEDSQNVLGN DPSVNSQAQD PIVTPSNTVE AQTLHPTSDL
KEDHHEIGAK GQEHADTGDR AESSEEPALE KPPLDKAELE RSPSSQDTEQ RHHPYSEHVG
GDTLVLDPNY SQSDLGGRAD AHLESSSAAP TEGAGEGGEA GAHLESSCAA LPVGADEGGR
ANAHLESSSA APTEGAGEGG EADVHLESSS AVPPEEAHLE SSSAAPSEGA GEGGEADAHL
ESSSAAPSEG AGEGGETAQN LLAVDSTDAQ SPCHSSAGPG SQDSLRRRLP VTEAERHEEE
TQLVTEKEEV AQETLRKTEK KSLWTYGSMF LGCLIVAVVL SSVNSYYSSP AQQVPQNPAL
EAFLAQFSQL REKFPGQSAF LWQRGRKFLQ KHLNASNPSE PATVIFTAAR EGKETLKCLS
YHVANAYTSS QKVTAVSIDG AERALQDSDT VKLLVDLELS YGFENGHKAA VVHHFESLPA
GSTLIFYKYC DHENAAFKDV ALVLTVLLEE ETLEASVSPR ETEEKVRDLL WAKFTDSGTP
SSFSHMDSDK LSGLWSRISH LVLPVQPVKN IEERGCLL
