ID  P54811;
PN  Transitional endoplasmic reticulum ATPase homolog 1;
GN  cdc;
OS  6239;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:25721663}. Cytoplasm {ECO:0000269|PubMed:17369820}. Note=Colocalizes with ubxn-1, ubxn-2 and ubxn-3 to the perinuclear region in spermatocytes (PubMed:20977550). Localizes to the perinuclear region in intestinal cells (PubMed:25721663). {ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:25721663}.
DR  UNIPROT: P54811;
DR  Pfam: PF00004;
DR  Pfam: PF17862;
DR  Pfam: PF02933;
DR  Pfam: PF02359;
DR  Pfam: PF09336;
DR  PROSITE: PS00674;
DE  Function: ATP-dependent chaperone which probably uses the energy provided by ATP hydrolysis to generate mechanical force to unfold substrate proteins, disassemble protein complexes, and disaggregate protein aggregates (PubMed:18854144, PubMed:18782221, PubMed:22768338). Can also prevent aggregation of unfolded proteins also in an ATP- independent manner (PubMed:18782221). Targets polyubiquitinated proteins for proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin chains (PubMed:19545544). Involved in the cytoplasmic elimination of misfolded proteins exported from the ER (PubMed:16647269, PubMed:17825049, PubMed:21317884, PubMed:22768338, PubMed:25652260). This pathway, known as ERAD, prevents the activation of the unfolded protein response (UPR) caused by the accumulation of misfolded proteins in the ER (PubMed:16647269, PubMed:17825049, PubMed:21317884, PubMed:22768338, PubMed:25652260). In association with helicase him-6 and GTPase crp-1, regulates the unfolded protein response (UPR) following ER stress, probably independently of the ERAD pathway (PubMed:18458060). Together with udf-2 and chn-1, regulates myosin assembly in body wall muscles by targeting myosin chaperone unc- 45 for proteasomal degradation (PubMed:17369820). Together with the ufd-1-npl-4 complex, controls the switch from spermatogenesis to oogenesis by regulating E3 ligase cul-2 complex-mediated tra-1 proteasomal degradation (PubMed:19773360). During oocyte meiosis and together with cdc-48.2, required for chromosome condensation at the diakinesis phase in prophase I and for progression of metaphase I (PubMed:17512499). During the first embryonic cell division, regulates DNA replication and thus chromosome segregation and decondensation, and nuclear envelope re-assembly (PubMed:18097415, PubMed:18854144, PubMed:18728180, PubMed:21981920, PubMed:26842564, PubMed:28368371). In S phase and in association with ufd-1, npl-4.1 and/or npl-4.2 and ubxn- 3, ensures the degradation of DNA licensing factor cdt-1 after the initiation of DNA replication and thus the disassembly of the DNA replication CMG helicase complex by promoting the dissociation from chromatin of several of its components including cdc-45 and sld-5 (PubMed:21981920, PubMed:26842564, PubMed:28368371). Regulates ubxn-3 nuclear localization during S phase (PubMed:26842564). During the first embryonic cell divisions and together with cdc-48.2, regulates the re- assembly of the nuclear envelope after mitosis possibly by inactivating kinase air-2, a component of the chromosomal passenger complex (CPC) (PubMed:18097415). However, in another study, cdc-48.1 does not appear to be implicated in the regulation of air-2 (PubMed:18854144). {ECO:0000269|PubMed:16647269, ECO:0000269|PubMed:17369820, ECO:0000269|PubMed:17512499, ECO:0000269|PubMed:17825049, ECO:0000269|PubMed:18097415, ECO:0000269|PubMed:18458060, ECO:0000269|PubMed:18728180, ECO:0000269|PubMed:18782221, ECO:0000269|PubMed:18854144, ECO:0000269|PubMed:19545544, ECO:0000269|PubMed:19773360, ECO:0000269|PubMed:21317884, ECO:0000269|PubMed:21981920, ECO:0000269|PubMed:22768338, ECO:0000269|PubMed:25652260, ECO:0000269|PubMed:26842564, ECO:0000269|PubMed:28368371}.
DE  Reference Proteome: Yes;
DE  Interaction: Q9TXH9; IntAct: EBI-2412436; Score: 0.62
DE  Interaction: G5EC44; IntAct: EBI-344171; Score: 0.00
DE  Interaction: Q17425; IntAct: EBI-2411420; Score: 0.49
DE  Interaction: P54812; IntAct: EBI-2412428; Score: 0.62
DE  Interaction: Q22557; IntAct: EBI-2412451; Score: 0.49
DE  Interaction: O17850; IntAct: EBI-2412440; Score: 0.49
DE  Interaction: Q94230; IntAct: EBI-2412444; Score: 0.49
DE  Interaction: Q22560; IntAct: EBI-6458355; Score: 0.37
DE  Interaction: P54811; IntAct: EBI-6460441; Score: 0.55
GO  GO:0005737;
GO  GO:0005829;
GO  GO:0005654;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0034098;
GO  GO:0005524;
GO  GO:0016887;
GO  GO:0042802;
GO  GO:0031593;
GO  GO:0044877;
GO  GO:0097352;
GO  GO:0008340;
GO  GO:0009792;
GO  GO:0071712;
GO  GO:0051228;
GO  GO:0045977;
GO  GO:0032436;
GO  GO:1905634;
GO  GO:0030970;
GO  GO:0030433;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MASVPTHQSEKEKKNDELSTAILKDKVKPNRLIVDQSEQDDNSVIAVSQAKMDELGLFRGDAVILKGKKRKESVAIIVSD
SQ  ESCPNEKVRMNRVVRNNLRIRLGDVVSITPAPNLSYGTRIHVLPIDDTIEGLTGNLFDVFLKPYFLEAYRPLHKGDIFTV
SQ  QAAMRTVEFKVVETEPAPACIVSPDTMIHYEGDPIKREEEEESMNDIGYDDLGGVRKQLAQIKEMVELPLRHPQLFKAIG
SQ  IKPPRGILLFGPPGTGKTLIARAVANETGSFFFLINGPEVMSKMSGESESNLRKAFEECEKNQPAILFIDEIDAIAPKRE
SQ  KTNGEVERRIVSQLLTLMDGVKGRSNLVVIAATNRPNSIDGALRRFGRFDREIDIGIPDAVGRLEILRIHTKNMKLADDV
SQ  DLEQIANECHGFVGADLASLCSEAALQQIREKMELIDLEDDQIDAEVLNSLAVTMENFRFAQGKSSPSALREAVVETPNT
SQ  TWSDIGGLQNVKRELQELVQYPVEHPEKYLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISIKGPELLTMWFGE
SQ  SEANVRDVFDKARAAAPCVLFFDELDSIAKARGGGAGGDGGGASDRVINQVLTEMDGMNAKKNVFIIGATNRPDIIDPAV
SQ  LRPGRLDQLIYIPLPDEASRHQILKASLRKTPLSKDLDLTFLAKNTVGFSGADLTEICQRACKLAIRESIEKEIRIEKER
SQ  QDRQARGEELMEDDAVDPVPEITRAHFEEAMKFARRSVTDNDIRKYEMFAQTLQQSRGFGNNFKFPGEQRGSDAPSAPVP
SQ  AQDDDDLYN
//