SEC72_SCHPO
ID SEC72_SCHPO Reviewed; 192 AA.
AC O14085;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Translocation protein sec72;
GN Name=sec72; ORFNames=SPAC2F3.02;
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 non-essential component of the Sec62/63 complex which
CC is involved in SRP-independent post-translational translocation across
CC the 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. sec72 may be involved in signal peptide
CC recognition for a defined subset of leader peptides, or may increase
CC the efficiency of unusual or 'difficult' secretory precursors to the
CC translocation pore, it may be that this protein binds charged leader
CC peptides to the membrane until they engage the translocation apparatus
CC (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: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAB16260.1; -; Genomic_DNA.
DR PIR; T38535; T38535.
DR RefSeq; NP_594381.1; NM_001019802.2.
DR AlphaFoldDB; O14085; -.
DR SMR; O14085; -.
DR BioGRID; 277965; 7.
DR STRING; 4896.SPAC2F3.02.1; -.
DR MaxQB; O14085; -.
DR PaxDb; O14085; -.
DR EnsemblFungi; SPAC2F3.02.1; SPAC2F3.02.1:pep; SPAC2F3.02.
DR GeneID; 2541463; -.
DR KEGG; spo:SPAC2F3.02; -.
DR PomBase; SPAC2F3.02; -.
DR VEuPathDB; FungiDB:SPAC2F3.02; -.
DR eggNOG; ENOG502S1IJ; Eukaryota.
DR HOGENOM; CLU_090376_2_0_1; -.
DR OMA; MLCNRAA; -.
DR PhylomeDB; O14085; -.
DR PRO; PR:O14085; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0031207; C:Sec62/Sec63 complex; ISO:PomBase.
DR GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus; Protein transport; Reference proteome; Repeat;
KW TPR repeat; Transport.
FT CHAIN 1..192
FT /note="Translocation protein sec72"
FT /id="PRO_0000311764"
FT REPEAT 62..95
FT /note="TPR 1"
FT REPEAT 136..169
FT /note="TPR 2"
SQ SEQUENCE 192 AA; 21657 MW; 6B9DB8FC35F75D25 CRC64;
MVAKQESVVA PQVDVSKWSG KELELGKKVN EYAKSLATFK YPFFIPPPYP PAKPNMALST
QVNKMKQTAN EAFKRKKYEE AKKLYGLALQ LALNRCTWEP SILTREEASV MLCNRAAAEI
ALSQFPEALA DANAALKIRN NYGKCYYRKA KALEAMHRIE EAKQVVRDGL ILAEPVTRNE
LVALWASYTE KD
