ID   ASTER_CHICK             Reviewed;         101 AA.
AC   F8RT80;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=PAT complex subunit Asterix {ECO:0000250|UniProtKB:Q9Y284};
DE   AltName: Full=Protein WDR83OS homolog;
DE   AltName: Full=Protein associated with the ER translocon of 10kDa {ECO:0000250|UniProtKB:Q9Y284};
DE            Short=PAT-10 {ECO:0000250|UniProtKB:Q9Y284};
DE            Short=PAT10 {ECO:0000250|UniProtKB:Q9Y284};
GN   Name=WDR83OS;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=21559472; DOI=10.1371/journal.pone.0019157;
RA   Pinho S., Simonsson P.R., Trevers K.E., Stower M.J., Sherlock W.T.,
RA   Khan M., Streit A., Sheng G., Stern C.D.;
RT   "Distinct steps of neural induction revealed by Asterix, Obelix and TrkC,
RT   genes induced by different signals from the organizer.";
RL   PLoS ONE 6:E19157-E19157(2011).
CC   -!- FUNCTION: Component of the PAT complex, an endoplasmic reticulum (ER)-
CC       resident membrane multiprotein complex that facilitates multi-pass
CC       membrane proteins insertion into membranes. The PAT complex acts as an
CC       intramembrane chaperone by directly interacting with nascent
CC       transmembrane domains (TMDs), releasing its substrates upon correct
CC       folding, and is needed for optimal biogenesis of multi-pass membrane
CC       proteins. WDR83OS/Asterix is the substrate-interacting subunit of the
CC       PAT complex, whereas CCDC47 is required to maintain the stability of
CC       WDR83OS/Asterix. WDR83OS/Asterix associates with the first
CC       transmembrane domain (TMD1) of the nascent chain, independently of the
CC       N-glycosylation of the chain and irrespective of the amino acid
CC       sequence and transmembrane topology of TMD1. The PAT complex favors the
CC       binding to TMDs with exposed hydrophilic amino acids within the lipid
CC       bilayer and provides a membrane-embedded partially hydrophilic
CC       environment in which TMD1 binds. {ECO:0000250|UniProtKB:Q9Y284}.
CC   -!- SUBUNIT: Component of the PAT complex. {ECO:0000250|UniProtKB:Q9Y284}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9Y284}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9Y284}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the early neural plate of embryos.
CC       Expressed in the hypoblast and Koller's sickle at pre-primitive streak
CC       stages. At stage 4, expression is detected in the node, the lips of the
CC       streak and the epiblast in the middle of the area pellucida. By the
CC       start of neurulation, expression becomes progressively concentrated in
CC       the neural plate, neural tube and sensory placodes including lens, otic
CC       and olfactory placodes. Expressed in the notochord and the sensory
CC       placodes at stage 16. Expressed in somites and persists in the myotome
CC       at later stages. {ECO:0000269|PubMed:21559472}.
CC   -!- INDUCTION: Up-regulated by FGF. {ECO:0000269|PubMed:21559472}.
CC   -!- SIMILARITY: Belongs to the Asterix family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HQ184923; AEJ33671.1; -; mRNA.
DR   RefSeq; NP_001292021.1; NM_001305092.1.
DR   AlphaFoldDB; F8RT80; -.
DR   STRING; 9031.ENSGALP00000042682; -.
DR   PaxDb; F8RT80; -.
DR   GeneID; 777443; -.
DR   CTD; 51398; -.
DR   eggNOG; KOG3462; Eukaryota.
DR   HOGENOM; CLU_128526_1_1_1; -.
DR   InParanoid; F8RT80; -.
DR   OrthoDB; 1608233at2759; -.
DR   PRO; PR:F8RT80; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0044183; F:protein folding chaperone; ISS:UniProtKB.
DR   GO; GO:0045048; P:protein insertion into ER membrane; ISS:UniProtKB.
DR   InterPro; IPR005351; ASTER.
DR   PANTHER; PTHR13193; PTHR13193; 1.
DR   Pfam; PF03669; UPF0139; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Endoplasmic reticulum; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..101
FT                   /note="PAT complex subunit Asterix"
FT                   /id="PRO_0000415288"
FT   TRANSMEM        34..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   101 AA;  11479 MW;  A4D59A158432B24F CRC64;
     MADPRRPARV TRYKPPTTES NPALEDPTPD YMNLLGMVFS MCGLMLKLKW CAWIAVYCSF
     ISFANSRSSE DTKQMMSSFM LSISAVVMSY LQNPQPMSPP W