SC61A_YARLI
ID SC61A_YARLI Reviewed; 471 AA.
AC P78979; O00099; Q6C514;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein transport protein SEC61 subunit alpha;
GN Name=SEC61; OrderedLocusNames=YALI0E21912g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RX PubMed=9427389; DOI=10.1242/jcs.110.21.2715;
RA Broughton J., Swennen D., Wilkinson B.M., Joyet P., Gaillardin C.,
RA Stirling C.J.;
RT "Cloning of SEC61 homologues from Schizosaccharomyces pombe and Yarrowia
RT lipolytica reveals the extent of functional conservation within this core
RT component of the ER translocation machinery.";
RL J. Cell Sci. 110:2715-2727(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; Y11322; CAA72175.1; -; Genomic_DNA.
DR EMBL; CR382131; CAG79843.1; -; Genomic_DNA.
DR PIR; T12065; T12065.
DR RefSeq; XP_504248.1; XM_504248.1.
DR AlphaFoldDB; P78979; -.
DR SMR; P78979; -.
DR STRING; 4952.CAG79843; -.
DR EnsemblFungi; CAG79843; CAG79843; YALI0_E21912g.
DR GeneID; 2911750; -.
DR KEGG; yli:YALI0E21912g; -.
DR VEuPathDB; FungiDB:YALI0_E21912g; -.
DR HOGENOM; CLU_031763_2_1_1; -.
DR InParanoid; P78979; -.
DR OMA; KWGIGSG; -.
DR Proteomes; UP000001300; Chromosome E.
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.
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..471
FT /note="Protein transport protein SEC61 subunit alpha"
FT /id="PRO_0000131788"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..76
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..146
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..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..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 461
FT /note="A -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="I -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 51687 MW; AB35A8C4B6565D9B CRC64;
MAGVRFLDLV KPFTPFLPEV QAPERKVPFN QKIMWTAVTL MIFLVMSEIP LYGINSSDKS
DALYWLRMML ASNRGSLMEL GITPIVSSGM VFQLLGGTQL IEVNMDLKSD RELYQTAQKL
FAIILSLGQA TVYVLTGMYG PPKDLGVGVC LLLIFQLVLA ALVVILLDEL LQKGYGLGSG
ISLFIATNIC EQIFWKAFAP TTVNKGRGYE FEGAIVAFVH LLFTRKDKKR AIIEAFTRQD
LPNMSQLVTT VAIFAAVIYL QGFRVDIPVK SSKQRGPYGV FPIKLFYTSN LPIMLQSALT
SNIFIISQML FKKFPTNVLV RLLGVWDGRE GMQQLFPVSG IAYYMQPPFN AKEALADPVK
TVIYIAFVLG VCAVFSATWI EISGSSPRDV AKQFKEQGLV IAGRRETSAY KELKRIIPTA
AAFGGATIGA LSVASDLLGA LSSGTGILMA VTTIYGYYEM AAKEGYVDAA I
