SC61A_CANAL
ID SC61A_CANAL Reviewed; 479 AA.
AC Q9P8E3; A0A1D8PKY6; Q59MJ6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protein transport protein SEC61 subunit alpha;
GN Name=SEC61; OrderedLocusNames=CAALFM_C307810CA; ORFNames=CaO19.6176;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15341916; DOI=10.1016/j.fgb.2004.07.004;
RA de la Rosa J.M., Ruiz T., Fonzi W.A., Rodriguez L.;
RT "Analysis of heterologous expression of Candida albicans SEC61 gene reveals
RT differences in Sec61p homologues related to species-specific
RT functionality.";
RL Fungal Genet. Biol. 41:941-953(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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
CC {ECO:0000269|PubMed:15341916}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15341916}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; AJ238713; CAB90210.1; -; Genomic_DNA.
DR EMBL; CP017625; AOW28779.1; -; Genomic_DNA.
DR RefSeq; XP_710932.1; XM_705840.1.
DR AlphaFoldDB; Q9P8E3; -.
DR SMR; Q9P8E3; -.
DR STRING; 237561.Q9P8E3; -.
DR PRIDE; Q9P8E3; -.
DR GeneID; 3647462; -.
DR KEGG; cal:CAALFM_C307810CA; -.
DR CGD; CAL0000178942; SEC61.
DR VEuPathDB; FungiDB:C3_07810C_A; -.
DR eggNOG; KOG1373; Eukaryota.
DR HOGENOM; CLU_031763_2_1_1; -.
DR InParanoid; Q9P8E3; -.
DR OMA; KWGIGSG; -.
DR OrthoDB; 482911at2759; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
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:0005886; C:plasma membrane; IDA:CGD.
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:0015031; P:protein transport; IMP:CGD.
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..479
FT /note="Protein transport protein SEC61 subunit alpha"
FT /id="PRO_0000131781"
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"
FT CONFLICT 418
FT /note="P -> H (in Ref. 1; CAB90210)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 52520 MW; A688F501CF59C9F9 CRC64;
MSGFRVLDLV KPFSPFLPEV IAPERKVQFQ QRVMWTIITL LIFLVMSEIP LYGIASSDSS
DPLFWLRMML ASNRGTLMEL GISPIVSSGM LFQLLQGTKI IHVDMQNKND RETFQTAQKL
LAILLAVGQA TVYVLTGMYG PPSSLGVGVC SLLILQLVFA STIVILLDEL LQKGYGLGSG
VSLFTATNTC EQVFWKAFAP TTSTSAKGTE FDGAVVAMFH LLGSRKDKKR ALIESFYRPN
LPNMFQLLAT LLVFFAVVYL QGFRIELPMK STRQRGPYGS YPIRLFYTSN IPIMLESALA
SNIFIISQLL FMRWPNNLFV KLLGTWDARA GSSQLYANGG LAYYIQPPFN FTDALLDPIK
TTIYIAFVLG SCAVFSTTWI EISGTSPRDV AKQFKEQGLV IAGHRDTSAY KELKKIIPIA
AAFGGATIGA LSVVCDLMGT LGSGTSILLA VTTIYGYYEL AVKEGGFNKS IVSGFSDGI
