(data stored in ACNUC6288 zone)

SWISSPROT: 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   08-MAY-2019, entry version 90.
DE   RecName: Full=Protein transport protein SEC61 subunit alpha;
GN   Name=SEC61; OrderedLocusNames=DEHA2F01144g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   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
CC       secretory and membrane polypeptides into the ER. It is required
CC       for assembly of membrane and secretory proteins and is essential
CC       for cell growth. It interacts with other membrane proteins
CC       required for protein translocation. Upon binding to SEC62/63
CC       complex, secretory precursor polypeptides may engage SEC61 to
CC       begin membrane penetration event. A cycle of assembly and
CC       disassembly of SEC62/63 from SEC61 may govern the activity of the
CC       translocase (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterotrimeric complex composed of SEC61-alpha, SEC61-
CC       beta and 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}.
DR   EMBL; CR382138; CAG88716.1; -; Genomic_DNA.
DR   RefSeq; XP_460412.1; XM_460412.1.
DR   STRING; 4959.XP_460412.1; -.
DR   EnsemblFungi; CAG88716; CAG88716; DEHA2F01144g.
DR   GeneID; 2903812; -.
DR   KEGG; dha:DEHA2F01144g; -.
DR   HOGENOM; HOG000231249; -.
DR   InParanoid; Q6BN08; -.
DR   KO; K10956; -.
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;
DR   PRODOM; Q6BN08.
DR   SWISS-2DPAGE; Q6BN08.
KW   Complete proteome; Endoplasmic reticulum; Membrane; Protein transport;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    479       Protein transport protein SEC61 subunit
FT                                alpha.
FT                                /FTId=PRO_0000131783.
FT   TOPO_DOM      1     33       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     34     54       Helical. {ECO:0000255}.
FT   TOPO_DOM     55     76       Lumenal. {ECO:0000255}.
FT   TRANSMEM     77     97       Helical. {ECO:0000255}.
FT   TOPO_DOM     98    119       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    120    140       Helical. {ECO:0000255}.
FT   TOPO_DOM    141    146       Lumenal. {ECO:0000255}.
FT   TRANSMEM    147    167       Helical. {ECO:0000255}.
FT   TOPO_DOM    168    246       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    247    267       Helical. {ECO:0000255}.
FT   TOPO_DOM    268    361       Lumenal. {ECO:0000255}.
FT   TRANSMEM    362    382       Helical. {ECO:0000255}.
FT   TOPO_DOM    383    415       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    416    434       Helical. {ECO:0000255}.
FT   TOPO_DOM    435    440       Lumenal. {ECO:0000255}.
FT   TRANSMEM    441    458       Helical. {ECO:0000255}.
FT   TOPO_DOM    459    479       Cytoplasmic. {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
//

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