SC61A_KLULA
ID SC61A_KLULA Reviewed; 480 AA.
AC Q6CPY9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Protein transport protein SEC61 subunit alpha;
GN Name=SEC61; OrderedLocusNames=KLLA0E01144g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
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DR EMBL; CR382125; CAG99087.1; -; Genomic_DNA.
DR RefSeq; XP_454000.1; XM_454000.1.
DR AlphaFoldDB; Q6CPY9; -.
DR SMR; Q6CPY9; -.
DR STRING; 28985.XP_454000.1; -.
DR EnsemblFungi; CAG99087; CAG99087; KLLA0_E01145g.
DR GeneID; 2894202; -.
DR KEGG; kla:KLLA0_E01145g; -.
DR eggNOG; KOG1373; Eukaryota.
DR HOGENOM; CLU_031763_2_1_1; -.
DR InParanoid; Q6CPY9; -.
DR OMA; KWGIGSG; -.
DR Proteomes; UP000000598; Chromosome E.
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..480
FT /note="Protein transport protein SEC61 subunit alpha"
FT /id="PRO_0000131785"
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; 52631 MW; 3DEF674D73FCB8D0 CRC64;
MSGRVLDLFK PFEAYLPEVI APERPVPYKQ KLIWTGVSLL VFLVLGQIPL YGIVSSETSD
PLYWLRAMLA SNRGTLMELG VSPIITSSMI FQFLQGTQLL QVNMENKQDR ELYQIAQKVF
AILLTFGQAI VVVLTGNYGK PSDLGLAISL LLIFQLIFAS FTVLLLDELL SKGYGLGSGI
SLFTATNIAE QITWKAFAPT TVNVGRGQEF EGAVIALFHL LAIRKDKKRA LVEAFYRENL
PNMFQVFSTI GVFLSVLYLQ GFRYELPIKS TRTRGQYGSY PIKLFYTSNT PIMLQSALTS
NIFLISQILY QRFSTNPLVK LLGVWGTRAG APAGQQVALS GLSYYIQPPF SVTDALLDPI
KTVVYVGFVL GACALFSKTW IEISGTSPRD VAKQFKDQGL TINGKRETNV YKELKKIIPT
AAAFGGAVIG ALSVGSDLLG TLGSGTSILM ATTTIYGYYE VAAKEGGFTK NLVSGFSEMM
