RSP1_SCHPO
ID RSP1_SCHPO Reviewed; 494 AA.
AC O13601;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=DnaJ-related protein rsp1;
GN Name=rsp1; ORFNames=pi006, SPBC11B10.05c;
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=10620777;
RX DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT yeast chromosome II: sequence analysis and characterization of the genomic
RT DNA and cDNAs encoded on the segment.";
RL Yeast 16:71-80(2000).
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 FUNCTION, INTERACTION WITH SSA1, AND SUBCELLULAR LOCATION.
RX PubMed=15068790; DOI=10.1016/s1534-5807(04)00096-6;
RA Zimmerman S., Tran P.T., Daga R.R., Niwa O., Chang F.;
RT "Rsp1p, a J domain protein required for disassembly and assembly of
RT microtubule organizing centers during the fission yeast cell cycle.";
RL Dev. Cell 6:497-509(2004).
CC -!- FUNCTION: Has a role in the proper organization of the interphase
CC microtubule cytoskeleton. Required for equatorial microtubule
CC organizing center (eMTOC) disassembly into satellites, contributing to
CC the dynamic redistribution of MTOC components for organization of
CC interphase microtubules. {ECO:0000269|PubMed:15068790}.
CC -!- SUBUNIT: Interacts iwth ssa1. {ECO:0000269|PubMed:15068790}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15068790}. Nucleus {ECO:0000269|PubMed:15068790}.
CC Note=Associates with the microtubule bundles.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB004534; BAA21383.1; -; Genomic_DNA.
DR EMBL; CU329671; CAC37509.1; -; Genomic_DNA.
DR RefSeq; NP_595625.1; NM_001021519.2.
DR AlphaFoldDB; O13601; -.
DR BioGRID; 276495; 7.
DR STRING; 4896.SPBC11B10.05c.1; -.
DR iPTMnet; O13601; -.
DR MaxQB; O13601; -.
DR PaxDb; O13601; -.
DR EnsemblFungi; SPBC11B10.05c.1; SPBC11B10.05c.1:pep; SPBC11B10.05c.
DR GeneID; 2539951; -.
DR KEGG; spo:SPBC11B10.05c; -.
DR PomBase; SPBC11B10.05c; rsp1.
DR VEuPathDB; FungiDB:SPBC11B10.05c; -.
DR eggNOG; KOG0714; Eukaryota.
DR HOGENOM; CLU_570058_0_0_1; -.
DR InParanoid; O13601; -.
DR OMA; QDVIPHF; -.
DR PRO; PR:O13601; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:1904511; C:cytoplasmic microtubule plus-end; IDA:PomBase.
DR GO; GO:0000923; C:equatorial microtubule organizing center; IDA:PomBase.
DR GO; GO:0031021; C:interphase microtubule organizing center; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:PomBase.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; EXP:PomBase.
DR GO; GO:0031025; P:equatorial microtubule organizing center disassembly; IMP:PomBase.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0031024; P:interphase microtubule organizing center assembly; IMP:PomBase.
DR GO; GO:1902405; P:mitotic actomyosin contractile ring localization; IMP:PomBase.
DR GO; GO:0007097; P:nuclear migration; IMP:PomBase.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Cytoskeleton; Microtubule; Nucleus;
KW Reference proteome.
FT CHAIN 1..494
FT /note="DnaJ-related protein rsp1"
FT /id="PRO_0000071131"
FT DOMAIN 12..78
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 229..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 56289 MW; DF5082E0CA16D3EB CRC64;
MARTAFHDEF VDYYTILGAE STSSYVEIRQ QYLKLVLRYH PDRNPGREAE VLPQFQLIQK
AHEVLKDPKL RELFDQRRLL EAGRPDGVLR FRPKKSGPKN DISTKVASKV SVTMATKFAE
KKKKQDRENV DSKDNNITNF SLHRSFSASG KMEKNNSFKE VSTSKSYISS GYLHPKTSPI
FKKNGYATEN VVDPISSSPR FKGPNYNKFN AKLYLESLRE KRRTYTPLSE ISNGLNSNGV
ENSSITKSSP RSSSSSNNER FKDTSEESII FTSPNTPEHP SVYQTDITPE IKLEHSDNNS
PSKPEIPFRH PTSKPLPPKP LSRSKSSSLS RNQTRSQLND LSAENDSTSN STEYDDQLQS
ILRSLAIEGD DDEVAKVLPK PPSVPTIQAP IPPEAPRNLT NASVDSYLNS FEMYQRRWSS
YSIIYTQYAF QWQIFKNKCF QLDLMNTPGQ SRLIDNWKEG SQAIQLFYAY EQMHLRALEE
LQSLKESLFA SFGI
