ID   ASTER_BOVIN             Reviewed;         106 AA.
AC   Q2M2T6;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the Asterix family. {ECO:0000305}.
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DR   EMBL; BC111635; AAI11636.1; -; mRNA.
DR   RefSeq; NP_001039475.1; NM_001046010.1.
DR   AlphaFoldDB; Q2M2T6; -.
DR   STRING; 9913.ENSBTAP00000008194; -.
DR   PaxDb; Q2M2T6; -.
DR   PRIDE; Q2M2T6; -.
DR   Ensembl; ENSBTAT00000008194; ENSBTAP00000008194; ENSBTAG00000006244.
DR   GeneID; 508733; -.
DR   KEGG; bta:508733; -.
DR   CTD; 51398; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006244; -.
DR   VGNC; VGNC:52897; WDR83OS.
DR   eggNOG; KOG3462; Eukaryota.
DR   GeneTree; ENSGT00390000002121; -.
DR   HOGENOM; CLU_128526_1_1_1; -.
DR   InParanoid; Q2M2T6; -.
DR   OMA; CGLMIRM; -.
DR   OrthoDB; 1608233at2759; -.
DR   TreeFam; TF315003; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000006244; Expressed in laryngeal cartilage and 107 other tissues.
DR   ExpressionAtlas; Q2M2T6; baseline and differential.
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   3: Inferred from homology;
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_0000245357"
FT   TRANSMEM        40..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..96
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;  12038 MW;  9C2BDDAF92681606 CRC64;
     MSANNMSDPR RPNKVLRYKP PPSECNPALD DPTPDYMNLL GMIFSMCGLM LKLKWCAWVA
     VYCSFISFAN SRSSEDTKQM MSSFMLSISA VVMSYLQNPQ PMTPPW