SEC66_SCHPO
ID SEC66_SCHPO Reviewed; 192 AA.
AC Q9UUA4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Translocation protein sec66;
GN Name=sec66; ORFNames=SPBC409.21;
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 [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 [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Acts as component of the Sec62/63 complex which is involved
CC in SRP-independent post-translational translocation across the
CC endoplasmic reticulum (ER) and functions together with the Sec61
CC complex and bip1 in a channel-forming translocon complex. A cycle of
CC assembly and disassembly of Sec62/63 complex from sec61 may govern the
CC activity of the translocon. sec66 is required to attach or retain sec72
CC in the sec63 complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the heterotetrameric Sec62/63complex composed of
CC sec62, sec63, sec66 and sec72. The Sec62/63 complex associates with the
CC Sec61 complex to form the Sec complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type II membrane protein {ECO:0000305}.
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DR EMBL; CU329671; CAB52623.1; -; Genomic_DNA.
DR PIR; T40448; T40448.
DR RefSeq; NP_595471.1; NM_001021381.2.
DR AlphaFoldDB; Q9UUA4; -.
DR SMR; Q9UUA4; -.
DR BioGRID; 277558; 2.
DR STRING; 4896.SPBC409.21.1; -.
DR iPTMnet; Q9UUA4; -.
DR MaxQB; Q9UUA4; -.
DR PaxDb; Q9UUA4; -.
DR PRIDE; Q9UUA4; -.
DR EnsemblFungi; SPBC409.21.1; SPBC409.21.1:pep; SPBC409.21.
DR GeneID; 2541043; -.
DR KEGG; spo:SPBC409.21; -.
DR PomBase; SPBC409.21; sec66.
DR VEuPathDB; FungiDB:SPBC409.21; -.
DR eggNOG; KOG4699; Eukaryota.
DR HOGENOM; CLU_066294_1_1_1; -.
DR InParanoid; Q9UUA4; -.
DR OMA; WQRYQNE; -.
DR PhylomeDB; Q9UUA4; -.
DR PRO; PR:Q9UUA4; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031207; C:Sec62/Sec63 complex; ISO:PomBase.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IBA:GO_Central.
DR InterPro; IPR018624; Sec66.
DR PANTHER; PTHR28229; PTHR28229; 1.
DR Pfam; PF09802; Sec66; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..192
FT /note="Translocation protein sec66"
FT /id="PRO_0000311763"
FT TOPO_DOM 1..3
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 4..21
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 192 AA; 22136 MW; E3CE117767792C10 CRC64;
MVSIYVPLIY ITILMGSMYG VSRFVRKSKN QESKPVSEEW FGENYSRNIF FSLLQQNPPA
EDTLLKAALV LRATEGLRRL MKLKVSRMAL NNLLNRGGVG DELIRKFGRL EKETELELMD
IAKTANSLQP GWNQFIFQTC NEIIENEKIH SIIDNIPKDI DSISQRWQTE KILYEAADEE
LRIQAQKELG VL
