SEC62_SCHPO
ID SEC62_SCHPO Reviewed; 273 AA.
AC O13787;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Translocation protein sec62;
GN Name=sec62; ORFNames=SPAC17G6.09;
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).
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. In an initial
CC step, the signal sequence seems to bind simultaneously to sec61 and
CC sec62. sec62 and sec63 are required for interactions between sec61 and
CC translocating polypeptides. sec62 may affect sec61-polypeptide
CC interactions by increasing the affinity of targeting pathways for sec61
CC and/or by modifying sec61 to allow more efficient polypeptide
CC interaction. A cycle of assembly and disassembly of Sec62/63 complex
CC from sec61 may govern the activity of the translocon (By similarity).
CC {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 Multi-pass membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SEC62 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16220.1; -; Genomic_DNA.
DR PIR; T37841; T37841.
DR RefSeq; NP_594256.1; NM_001019679.2.
DR AlphaFoldDB; O13787; -.
DR SMR; O13787; -.
DR BioGRID; 278860; 7.
DR IntAct; O13787; 2.
DR STRING; 4896.SPAC17G6.09.1; -.
DR iPTMnet; O13787; -.
DR MaxQB; O13787; -.
DR PaxDb; O13787; -.
DR PRIDE; O13787; -.
DR EnsemblFungi; SPAC17G6.09.1; SPAC17G6.09.1:pep; SPAC17G6.09.
DR GeneID; 2542396; -.
DR KEGG; spo:SPAC17G6.09; -.
DR PomBase; SPAC17G6.09; sec62.
DR VEuPathDB; FungiDB:SPAC17G6.09; -.
DR eggNOG; KOG2927; Eukaryota.
DR HOGENOM; CLU_040936_1_0_1; -.
DR InParanoid; O13787; -.
DR OMA; GLWLYPN; -.
DR PhylomeDB; O13787; -.
DR PRO; PR:O13787; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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; IPR004728; Sec62.
DR InterPro; IPR011553; Sec62_asco.
DR PANTHER; PTHR12443; PTHR12443; 1.
DR Pfam; PF03839; Sec62; 1.
DR TIGRFAMs; TIGR00869; sec62; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..273
FT /note="Translocation protein sec62"
FT /id="PRO_0000206625"
FT TOPO_DOM 1..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..167
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 225..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 273 AA; 31586 MW; EE7A6369530799B3 CRC64;
MDSSNVPVLK DEDKCKFSMR FTNFLKSRPE LKTKPAILNG KRVYYFRVKR VLRFLTSEAY
TPKKYKGFPE ISSREEAIEV LKLLIMNSML VRVDKLPPKQ RKQKLVELQI NRNQDFQDDM
HYVWLYEPLP KRVMALAVLF ALVVLALVLF PLWPMFMRKG AWYLSMGGLG VIGLFFVLVI
LRFFLFCITA VIVRPGIWLF PNLLADVGFC DSFKPLWSWH NSKSEVKKTR KSKKLSKKAT
SPAASATPEK SSTSTTSLKN LRHRNPTVEE VSE
