SEC63_SCHPO
ID SEC63_SCHPO Reviewed; 611 AA.
AC Q9HGN7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Translocation protein sec63;
GN Name=sec63; ORFNames=SPBC36B7.03;
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-566 AND SER-572, AND
RP IDENTIFICATION BY 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. sec63 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. May also be involved in SRP-dependent cotranslational
CC translocation (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. May physically associate with
CC bip1 in the endoplasmic reticulum and this interaction may be regulated
CC by ATP hydrolysis (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}. Nucleus membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Nucleus inner
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
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DR EMBL; CU329671; CAC05724.1; -; Genomic_DNA.
DR RefSeq; NP_595985.1; NM_001021892.2.
DR AlphaFoldDB; Q9HGN7; -.
DR SMR; Q9HGN7; -.
DR BioGRID; 277477; 25.
DR STRING; 4896.SPBC36B7.03.1; -.
DR iPTMnet; Q9HGN7; -.
DR MaxQB; Q9HGN7; -.
DR PaxDb; Q9HGN7; -.
DR PRIDE; Q9HGN7; -.
DR EnsemblFungi; SPBC36B7.03.1; SPBC36B7.03.1:pep; SPBC36B7.03.
DR GeneID; 2540961; -.
DR KEGG; spo:SPBC36B7.03; -.
DR PomBase; SPBC36B7.03; sec63.
DR VEuPathDB; FungiDB:SPBC36B7.03; -.
DR eggNOG; KOG0721; Eukaryota.
DR HOGENOM; CLU_014210_0_0_1; -.
DR InParanoid; Q9HGN7; -.
DR OMA; RAILHAH; -.
DR PhylomeDB; Q9HGN7; -.
DR PRO; PR:Q9HGN7; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005938; C:cell cortex; IDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:PomBase.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031207; C:Sec62/Sec63 complex; ISO:PomBase.
DR GO; GO:0030544; F:Hsp70 protein binding; ISM:PomBase.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; ISO:PomBase.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR027137; Sec63.
DR InterPro; IPR004179; Sec63-dom.
DR PANTHER; PTHR24075:SF0; PTHR24075:SF0; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF02889; Sec63; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00973; Sec63; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..611
FT /note="Translocation protein sec63"
FT /id="PRO_0000311762"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..191
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..611
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 98..168
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 200..503
FT /note="SEC63"
FT REGION 563..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..611
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 611 AA; 69726 MW; DA4BC288F13514D3 CRC64;
MSSEYKYDEQ GIFFPVFLLV GTSCCVLPLT YSTILGPSAS KEKKNVRDPF QKYRPKDLKV
QRKSIFRLRY IFLILGWLAI GFLSYKIANS RLKLNIWDPY EILGIAKGTS VDDVRRHYKR
LSIKFHPDKV RNMVNTTREE VEKHYIEITN AYRALTDDKT RENYALYGTP DVPQHISVGI
ALPKWISESE NSIYILGFYG LVFGIVLPYA VGKWWYGSRT YTRDHVHVDT VDEWFPKMET
SLTLDELLSL FASSKELTSL VPNEKNPKEY ILKLLFDHLN RKKTNNFNTH QILSQSDVVL
NALLSVATAF GFANPVDNVL KLWQHIVQAI PLDAPFPLLQ LPHLLMEDVK NLSIRNISSI
PQFLSLSEEQ TKDYLPNYSK NQLKEMREIA NGIPRISVVA AKVLVDDDEY ITVGAIANLI
LDLKCSYGTE VVPEVSTDGT ETATKKDEED AEKYHQSKDV VLGDVETLPY AWAPYFTQHH
KTAWWIYVVD PRQNRVIVPP FSITDIPKTL RTFRIPFQVP PVAGTFSFQL HIMSNSYVGE
DVISNLTMIV KDTSVLQEQL QEEAVSDLED NSDIDESANA GKDFSDDENI GSDEEDESEY
DPMDTDTSDG E
