SC61A_ASHGO
ID SC61A_ASHGO Reviewed; 480 AA.
AC Q752H7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein transport protein SEC61 subunit alpha;
GN Name=SEC61; OrderedLocusNames=AFR596W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Appears to play a crucial role in the insertion of secretory
CC and membrane polypeptides into the ER. It is required for assembly of
CC membrane and secretory proteins and is essential for cell growth. It
CC interacts with other membrane proteins required for protein
CC translocation. Upon binding to SEC62/63 complex, secretory precursor
CC polypeptides may engage SEC61 to begin membrane penetration event. A
CC cycle of assembly and disassembly of SEC62/63 from SEC61 may govern the
CC activity of the translocase (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimeric complex composed of SEC61-alpha, SEC61-beta and
CC SEC61-gamma. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; AE016819; AAS53967.1; -; Genomic_DNA.
DR RefSeq; NP_986143.1; NM_212279.1.
DR AlphaFoldDB; Q752H7; -.
DR SMR; Q752H7; -.
DR STRING; 33169.AAS53967; -.
DR EnsemblFungi; AAS53967; AAS53967; AGOS_AFR596W.
DR GeneID; 4622426; -.
DR KEGG; ago:AGOS_AFR596W; -.
DR eggNOG; KOG1373; Eukaryota.
DR HOGENOM; CLU_031763_2_1_1; -.
DR InParanoid; Q752H7; -.
DR OMA; KWGIGSG; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005784; C:Sec61 translocon complex; IBA:GO_Central.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:EnsemblFungi.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0070843; P:misfolded protein transport; IEA:EnsemblFungi.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IBA:GO_Central.
DR GO; GO:0044743; P:protein transmembrane import into intracellular organelle; IEA:EnsemblFungi.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IEA:EnsemblFungi.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
DR Gene3D; 1.10.3370.10; -; 1.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR InterPro; IPR019561; Translocon_Sec61/SecY_plug_dom.
DR PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF10559; Plug_translocon; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR PROSITE; PS00755; SECY_1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..480
FT /note="Protein transport protein SEC61 subunit alpha"
FT /id="PRO_0000131780"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..75
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..118
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..145
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..362
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..441
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 480 AA; 52732 MW; AA8B53EF4E07BF39 CRC64;
MSGRLLDLFK PFEAFLPEVI APERKVPYNQ KLIWTAVSLL IFLVLGQIPL YGIVSSEGSD
PLQWLRAMLA SNRGTLMELG VSPIITSSMI FQFLQGTQLL QVNLESKQDR ELFQIAQKVC
AIVLTLGQAI VVVLTGNYGS VSNLGIAISL LLILQLVFAS FIVLLLDELL IKGYGLGSGI
SLFTATNIAE QIFWKAFAPT TVNNGRGTEF EGAVVALFHL LSVRKDKKRA LVEAFYRDYL
PNMFQVLSTV FVFLFVLYLQ GFRYELPVRS TRTRGQVGSY PIKLFYTSNT PIMLQSALTS
NIFLTSQLLY QKFPNNPIVK MLGVWGTRSD APYSPNAAIS GLSYYIQPPF SFTEALLDPI
KTVVYVTFVL GACAMFSRTW IDVSGTSPRD VSKQFKEQGL VINGRRETSV YRELKKVIPT
AAAFGGATIG ALSVGSDLLG TLGSGTSILM ATTTIYGYYE TAAKEGGFAK NLVAGFSEML
