SC61A_CANGA
ID SC61A_CANGA Reviewed; 479 AA.
AC Q6FRY3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Protein transport protein SEC61 subunit alpha;
GN Name=SEC61; OrderedLocusNames=CAGL0H04961g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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; CR380954; CAG59944.1; -; Genomic_DNA.
DR RefSeq; XP_447011.1; XM_447011.1.
DR AlphaFoldDB; Q6FRY3; -.
DR SMR; Q6FRY3; -.
DR STRING; 5478.XP_447011.1; -.
DR EnsemblFungi; CAG59944; CAG59944; CAGL0H04961g.
DR GeneID; 2888525; -.
DR KEGG; cgr:CAGL0H04961g; -.
DR CGD; CAL0130012; CAGL0H04961g.
DR VEuPathDB; FungiDB:CAGL0H04961g; -.
DR eggNOG; KOG1373; Eukaryota.
DR HOGENOM; CLU_031763_2_1_1; -.
DR InParanoid; Q6FRY3; -.
DR OMA; KWGIGSG; -.
DR Proteomes; UP000002428; Chromosome H.
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; IEA:EnsemblFungi.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:EnsemblFungi.
DR GO; GO:0005048; F:signal sequence binding; IEA:EnsemblFungi.
DR GO; GO:0070843; P:misfolded protein transport; IEA:EnsemblFungi.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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.
DR PROSITE; PS00756; SECY_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..479
FT /note="Protein transport protein SEC61 subunit alpha"
FT /id="PRO_0000131782"
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..361
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..415
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..440
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 479 AA; 52640 MW; C8CFE731451FD573 CRC64;
MSDRILSLFK PFEAFLPEVI SPERKVPYNQ KLIWTGVSLL IFLVLGQIPL YGIVSAETSD
PLYWLRAMLA SNRGTLMELG VSPIITSSMI FQFLQGTQLL QVSLDSKEDR ELYQIAQKVC
AIILTFGQAL VVVMTGNYGS PSDLGIAISL LLIFQLMFAS FIVLLLDELL TKGYGLGSGI
SLFTATNIAE NIFWKAFAPT TVNSGRGKEF EGAVIAFFHL LAVRKDKKRA LVEAFYRENL
PNMFQVIATV FVFLFVLYLQ GFRYELPVKS TKVRGQMAIY PIKLFYTSNT PIMLQSALSS
NIFLISQILF QKYPSNPVIR LFGVWGIRPG TNGPQVPLSG ISYYLQPIGS LKMALLDPIK
TVIYTAFVLG TCALFSKTWI EISGTSAKDV AKQFKEQGMV INGKRETSVY KELKKIIPTA
AAFGGATIGA LSVGSDLLGA LGSGASILLA TTTIYGYYEV AAKEGGFTKN LVNGFSEMM
