ASTER_HUMAN
ID ASTER_HUMAN Reviewed; 106 AA.
AC Q9Y284; B2R4T8; Q9BVI3;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=PAT complex subunit Asterix {ECO:0000303|PubMed:32814900};
DE AltName: Full=Protein associated with the ER translocon of 10kDa {ECO:0000303|PubMed:12475939};
DE Short=PAT-10 {ECO:0000303|PubMed:12475939};
DE Short=PAT10 {ECO:0000303|PubMed:32814900};
DE AltName: Full=WD repeat domain 83 opposite strand;
DE AltName: Full=WDR83 opposite strand;
GN Name=WDR83OS {ECO:0000312|HGNC:HGNC:30203}; Synonyms=C19orf56;
GN ORFNames=CGI-140, My006, PTD008;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Mao Y.M., Xie Y., Zhou Z.X.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary tumor;
RA Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
RA Luo M., Chen J., Hu R.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, Liver, and 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).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12475939; DOI=10.1091/mbc.e02-04-0198;
RA Meacock S.L., Lecomte F.J., Crawshaw S.G., High S.;
RT "Different transmembrane domains associate with distinct endoplasmic
RT reticulum components during membrane integration of a polytopic protein.";
RL Mol. Biol. Cell 13:4114-4129(2002).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCDC47.
RX PubMed=32814900; DOI=10.1038/s41586-020-2624-y;
RA Chitwood P.J., Hegde R.S.;
RT "An intramembrane chaperone complex facilitates membrane protein
RT biogenesis.";
RL Nature 584:630-634(2020).
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 (PubMed:32814900). The PAT
CC complex acts as an intramembrane chaperone by directly interacting with
CC nascent transmembrane domains (TMDs), releasing its substrates upon
CC correct folding, and is needed for optimal biogenesis of multi-pass
CC membrane proteins (PubMed:32814900). WDR83OS/Asterix is the substrate-
CC interacting subunit of the PAT complex, whereas CCDC47 is required to
CC maintain the stability of WDR83OS/Asterix (PubMed:12475939,
CC PubMed:32814900). 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 (PubMed:12475939,
CC PubMed:32814900). The PAT complex favors the binding to TMDs with
CC exposed hydrophilic amino acids within the lipid bilayer and provides a
CC membrane-embedded partially hydrophilic environment in which TMD1 binds
CC (PubMed:32814900). {ECO:0000269|PubMed:12475939,
CC ECO:0000269|PubMed:32814900}.
CC -!- SUBUNIT: The PAT complex includes WDR83OS/Asterix and CCDC47.
CC {ECO:0000269|PubMed:32814900}.
CC -!- INTERACTION:
CC Q9Y284; Q96A33: CCDC47; NbExp=2; IntAct=EBI-6309120, EBI-720151;
CC Q9Y284; Q76KX8: ZNF534; NbExp=3; IntAct=EBI-6309120, EBI-17208605;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12475939, ECO:0000269|PubMed:32814900}; Multi-pass
CC membrane protein {ECO:0000305|PubMed:12475939}.
CC -!- SIMILARITY: Belongs to the Asterix family. {ECO:0000305}.
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DR EMBL; AF059620; AAG43119.1; -; mRNA.
DR EMBL; AF078861; AAD44493.1; -; mRNA.
DR EMBL; AF151898; AAD34135.1; -; mRNA.
DR EMBL; AK311944; BAG34885.1; -; mRNA.
DR EMBL; CH471106; EAW84285.1; -; Genomic_DNA.
DR EMBL; BC001192; AAH01192.1; -; mRNA.
DR EMBL; BC042919; AAH42919.1; -; mRNA.
DR EMBL; BC061912; AAH61912.1; -; mRNA.
DR CCDS; CCDS12274.1; -.
DR RefSeq; NP_057229.1; NM_016145.3.
DR RefSeq; XP_016882353.1; XM_017026864.1.
DR AlphaFoldDB; Q9Y284; -.
DR BioGRID; 119522; 7.
DR ComplexPortal; CPX-7020; PAT intramembrane chaperone complex.
DR IntAct; Q9Y284; 4.
DR STRING; 9606.ENSP00000468969; -.
DR TCDB; 8.A.142.1.1; the pat intramembrane chaperone complex (pat) family.
DR iPTMnet; Q9Y284; -.
DR PhosphoSitePlus; Q9Y284; -.
DR BioMuta; WDR83OS; -.
DR DMDM; 12585211; -.
DR EPD; Q9Y284; -.
DR MassIVE; Q9Y284; -.
DR MaxQB; Q9Y284; -.
DR PaxDb; Q9Y284; -.
DR PeptideAtlas; Q9Y284; -.
DR PRIDE; Q9Y284; -.
DR ProteomicsDB; 85693; -.
DR TopDownProteomics; Q9Y284; -.
DR Antibodypedia; 26085; 32 antibodies from 14 providers.
DR DNASU; 51398; -.
DR Ensembl; ENST00000596731.7; ENSP00000468969.1; ENSG00000105583.11.
DR GeneID; 51398; -.
DR KEGG; hsa:51398; -.
DR MANE-Select; ENST00000596731.7; ENSP00000468969.1; NM_016145.4; NP_057229.1.
DR UCSC; uc002mud.3; human.
DR CTD; 51398; -.
DR DisGeNET; 51398; -.
DR GeneCards; WDR83OS; -.
DR HGNC; HGNC:30203; WDR83OS.
DR HPA; ENSG00000105583; Low tissue specificity.
DR MIM; 618474; gene.
DR neXtProt; NX_Q9Y284; -.
DR PharmGKB; PA162378666; -.
DR VEuPathDB; HostDB:ENSG00000105583; -.
DR eggNOG; KOG3462; Eukaryota.
DR GeneTree; ENSGT00390000002121; -.
DR InParanoid; Q9Y284; -.
DR OMA; CGLMIRM; -.
DR PhylomeDB; Q9Y284; -.
DR TreeFam; TF315003; -.
DR PathwayCommons; Q9Y284; -.
DR SignaLink; Q9Y284; -.
DR BioGRID-ORCS; 51398; 131 hits in 1080 CRISPR screens.
DR ChiTaRS; WDR83OS; human.
DR GenomeRNAi; 51398; -.
DR Pharos; Q9Y284; Tdark.
DR PRO; PR:Q9Y284; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y284; protein.
DR Bgee; ENSG00000105583; Expressed in right adrenal gland and 98 other tissues.
DR ExpressionAtlas; Q9Y284; baseline and differential.
DR Genevisible; Q9Y284; HS.
DR GO; GO:0101031; C:chaperone complex; IPI:ComplexPortal.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0044183; F:protein folding chaperone; IDA:UniProtKB.
DR GO; GO:0045048; P:protein insertion into ER membrane; IDA:UniProtKB.
DR InterPro; IPR005351; ASTER.
DR PANTHER; PTHR13193; PTHR13193; 1.
DR Pfam; PF03669; UPF0139; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..106
FT /note="PAT complex subunit Asterix"
FT /id="PRO_0000071605"
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:0007744|PubMed:19413330"
FT VARIANT 104
FT /note="P -> A (in dbSNP:rs3209404)"
FT /id="VAR_052498"
SQ SEQUENCE 106 AA; 12068 MW; 7D2BDDAF9279071B CRC64;
MSTNNMSDPR RPNKVLRYKP PPSECNPALD DPTPDYMNLL GMIFSMCGLM LKLKWCAWVA
VYCSFISFAN SRSSEDTKQM MSSFMLSISA VVMSYLQNPQ PMTPPW
