SC61A_SCHPO
ID SC61A_SCHPO Reviewed; 479 AA.
AC P79088; Q9UU67;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein transport protein sec61 subunit alpha;
GN Name=sec61; ORFNames=SPBC354.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
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=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 121-179, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
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:10759889}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10759889}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; Y11376; CAA72200.1; -; mRNA.
DR EMBL; Y11375; CAA72199.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA17802.1; -; Genomic_DNA.
DR EMBL; AB027782; BAA87086.1; -; Genomic_DNA.
DR PIR; T40282; T40282.
DR RefSeq; NP_595226.1; NM_001021132.2.
DR AlphaFoldDB; P79088; -.
DR SMR; P79088; -.
DR BioGRID; 277552; 3.
DR STRING; 4896.SPBC354.02c.1; -.
DR iPTMnet; P79088; -.
DR SwissPalm; P79088; -.
DR MaxQB; P79088; -.
DR PaxDb; P79088; -.
DR PRIDE; P79088; -.
DR EnsemblFungi; SPBC354.02c.1; SPBC354.02c.1:pep; SPBC354.02c.
DR GeneID; 2541037; -.
DR KEGG; spo:SPBC354.02c; -.
DR PomBase; SPBC354.02c; sec61.
DR VEuPathDB; FungiDB:SPBC354.02c; -.
DR eggNOG; KOG1373; Eukaryota.
DR HOGENOM; CLU_031763_2_1_1; -.
DR InParanoid; P79088; -.
DR OMA; KWGIGSG; -.
DR PhylomeDB; P79088; -.
DR PRO; PR:P79088; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:PomBase.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005784; C:Sec61 translocon complex; ISO:PomBase.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IBA:GO_Central.
DR GO; GO:0045048; P:protein insertion into ER membrane; IC:PomBase.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; ISO:PomBase.
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 2: Evidence at transcript level;
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_0000131787"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..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..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..354
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..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; 53254 MW; 36E3F08E2CFD9868 CRC64;
MSDLRFLDLV KPFAPFLPEI AAPERKVPFK QKMLWTGVTL LIFLVMSQVP LYGIVSSDSS
DPLLWLRMIL AANRGTLMEL GISPIVTSSM LVQLLVGSQL IEVNMELKSD REMYQLVQKF
LAIIIAFGQA TAYVLTGMYG RPQDLGAGIC LLLILQLAAA SLIVLLLDEL LQKGYGLGSG
ISLFIATINC ENIFWKAFSP TTYHIANGVQ FEGAVINFVY VMFTWDNKAA ALYQAFFRSG
LTSSQIQLPN LWNFFATLLV FGVVIYLQDF RVEIPIRSQK FRGYRSTFPV KLLYTSNTPI
MLQSALTSNL FFASRLLFNR FSSNFLVRFL GVWEQTATSG LSYYLSPPAS FQDALIDPIH
TLVYVFFTMF ACALFSKLWI EVSGASPRDV AKQLKSQQLV MAGHREGSMY KELKRIIPTA
AWLSGAVVGA LAVASDLLGA LGSGTAVLLC TTTIYGYYEQ LQKEIKGDQY GLPVTPMMQ
