SC61A_DEBHA
ID SC61A_DEBHA Reviewed; 479 AA.
AC Q6BN08;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Protein transport protein SEC61 subunit alpha;
GN Name=SEC61; OrderedLocusNames=DEHA2F01144g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAG88716.1; -; Genomic_DNA.
DR RefSeq; XP_460412.1; XM_460412.1.
DR AlphaFoldDB; Q6BN08; -.
DR SMR; Q6BN08; -.
DR STRING; 4959.XP_460412.1; -.
DR EnsemblFungi; CAG88716; CAG88716; DEHA2F01144g.
DR GeneID; 2903812; -.
DR KEGG; dha:DEHA2F01144g; -.
DR VEuPathDB; FungiDB:DEHA2F01144g; -.
DR eggNOG; KOG1373; Eukaryota.
DR HOGENOM; CLU_031763_2_1_1; -.
DR InParanoid; Q6BN08; -.
DR OMA; KWGIGSG; -.
DR OrthoDB; 482911at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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_0000131783"
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..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 479 AA; 52518 MW; C17180AAEFB0E50C CRC64;
MSGFRVLDLV KPFTPFMPEV IAPERKVAFQ QRLMWTGVTL LIFLVMSEIP LYGIASSDGS
DPLYWLRMML ASNRGTLMEL GISPIVSAGM VFQLLQGTKL ITVDMSNKND RDQFQTAQKL
FAILLAVGQA TVYVLTGMYG PPSSLGTGVC LLLVLQLVFA GIVVILLDEL LQKGYGLGSG
ISLFTATNVC EQVFWKAFAP TTSNIGKGTE FEGAVVALFH LLGSRKDKKR ALLEAFYRSH
LPNMFQLIAT VFVFLLVVYL QGFRIELPIK STRQRGPYGL YPIRLFYTSN IPIMLQSALS
SNIFIISQML FVRWPNNIFV KILGSWDTRQ GAAQLYAVSG LAYYIQPPLS FTEALLDPIK
TIIYIIFVLG SCAVFSTTWI EISGASPRDV AKQFKEQGLV IAGHRDTSAY RELKKIIPTA
AAFGGATIGA LSVFCDLMGT LGSGTSILLS VTTIYGYYEL AMKEGGFGKS VVSSFSDGI
