ID   ASTER_PIG               Reviewed;         106 AA.
AC   Q6Q7K0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 66.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=15625692; DOI=10.1002/mrd.20204;
RA   Hwang K.C., Lee H.Y., Cui X.S., Kim J.H., Kim N.H.;
RT   "Identification of maternal mRNAs in porcine parthenotes at the 2-cell
RT   stage: a comparison with the blastocyst stage.";
RL   Mol. Reprod. Dev. 70:314-323(2005).
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: The PAT complex includes WDR83OS/Asterix and CCDC47.
CC       {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 during early cleavage-stage embryos
CC       before zygotic gene activation (ZGA), metaphase II (MII) oocyte, 1-
CC       cell, and 2-cell stage embryos. {ECO:0000269|PubMed:15625692}.
CC   -!- SIMILARITY: Belongs to the Asterix family. {ECO:0000305}.
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DR   EMBL; AY553921; AAS76542.1; -; mRNA.
DR   RefSeq; NP_001001645.1; NM_001001645.1.
DR   AlphaFoldDB; Q6Q7K0; -.
DR   STRING; 9823.ENSSSCP00000014591; -.
DR   PaxDb; Q6Q7K0; -.
DR   GeneID; 414435; -.
DR   KEGG; ssc:414435; -.
DR   CTD; 51398; -.
DR   eggNOG; KOG3462; Eukaryota.
DR   InParanoid; Q6Q7K0; -.
DR   OrthoDB; 1608233at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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   Acetylation; Chaperone; Endoplasmic reticulum; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y284"
FT   CHAIN           2..106
FT                   /note="PAT complex subunit Asterix"
FT                   /id="PRO_0000071607"
FT   TRANSMEM        40..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y284"
SQ   SEQUENCE   106 AA;  11942 MW;  0CB2D4249AD258E7 CRC64;
     MSANSMSDPR SPNKVLRYKP PPSECNPALD DPTPDYMNLL GMIFSMCGLM LKLKWCAWVA
     VYCSFISFAN SRSSEDTKQM MSSFMLSISA VVMSYLQNPQ PMTPPW