MAS5_SCHPO
ID MAS5_SCHPO Reviewed; 407 AA.
AC O74752;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Mitochondrial protein import protein mas5;
DE Flags: Precursor;
GN Name=mas5; ORFNames=SPBC1734.11;
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 FUNCTION.
RX PubMed=15797925; DOI=10.1242/jcs.02305;
RA Pardo M., Nurse P.;
RT "The nuclear rim protein Amo1 is required for proper microtubule
RT cytoskeleton organisation in fission yeast.";
RL J. Cell Sci. 118:1705-1714(2005).
RN [3]
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: Probably involved in mitochondrial protein import (By
CC similarity). Plays a role in microtubule cytoskeleton organization.
CC {ECO:0000250, ECO:0000269|PubMed:15797925}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329671; CAA21305.1; -; Genomic_DNA.
DR PIR; T39658; T39658.
DR RefSeq; NP_595428.1; NM_001021336.2.
DR AlphaFoldDB; O74752; -.
DR SMR; O74752; -.
DR BioGRID; 276226; 12.
DR IntAct; O74752; 1.
DR STRING; 4896.SPBC1734.11.1; -.
DR iPTMnet; O74752; -.
DR MaxQB; O74752; -.
DR PaxDb; O74752; -.
DR PRIDE; O74752; -.
DR EnsemblFungi; SPBC1734.11.1; SPBC1734.11.1:pep; SPBC1734.11.
DR GeneID; 2539671; -.
DR KEGG; spo:SPBC1734.11; -.
DR PomBase; SPBC1734.11; mas5.
DR VEuPathDB; FungiDB:SPBC1734.11; -.
DR eggNOG; KOG0712; Eukaryota.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; O74752; -.
DR OMA; RVCPTCV; -.
DR PhylomeDB; O74752; -.
DR Reactome; R-SPO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR PRO; PR:O74752; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0140453; C:protein aggregate center; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0030544; F:Hsp70 protein binding; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140311; F:protein sequestering activity; EXP:PomBase.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0034605; P:cellular response to heat; IMP:PomBase.
DR GO; GO:0140455; P:cytoplasm protein quality control; IMP:PomBase.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
DR GO; GO:0140454; P:protein aggregate center assembly; IMP:PomBase.
DR GO; GO:0042026; P:protein refolding; IMP:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR044713; DNJA1/2-like.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR43888; PTHR43888; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR SUPFAM; SSF57938; SSF57938; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Lipoprotein; Metal-binding; Methylation; Nucleus;
KW Prenylation; Protein transport; Reference proteome; Repeat; Transport;
KW Zinc; Zinc-finger.
FT CHAIN 1..404
FT /note="Mitochondrial protein import protein mas5"
FT /id="PRO_0000314107"
FT PROPEP 405..407
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396683"
FT DOMAIN 6..68
FT /note="J"
FT REPEAT 137..144
FT /note="CXXCXGXG motif"
FT REPEAT 153..160
FT /note="CXXCXGXG motif"
FT REPEAT 179..186
FT /note="CXXCXGXG motif"
FT REPEAT 195..202
FT /note="CXXCXGXG motif"
FT ZN_FING 124..207
FT /note="CR-type"
FT REGION 375..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129..131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 209..210
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241..243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 329
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250"
FT MOD_RES 404
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 404
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 407 AA; 44821 MW; 3A76A614B7369426 CRC64;
MVKETKLYEV LNVDVTASQA ELKKAYRKLA LKYHPDKNPN AGDKFKEISR AYEILADEEK
RATYDRFGEE GLQGGGADGG MSADDLFASF FGGGMFGGGM PRGPRKGKDL VHTIKVTLED
LYRGKTTKLA LQKKVICPKC SGRGGKEGSV KSCASCNGSG VKFITRAMGP MIQRMQMTCP
DCNGAGETIR DEDRCKECDG AKVISQRKIL TVHVEKGMHN GQKIVFKEEG EQAPGIIPGD
VIFVIDQKEH PRFKRSGDHL FYEAHVDLLT ALAGGQIVVE HLDDRWLTIP IIPGECIRPN
ELKVLPGQGM LSQRHHQPGN LYIRFHVDFP EPNFATPEQL ALLEKALPPR KIESAPKNAH
TEECVLATVD PTEKVRIDNN VDPTTATSMD EDEDEEGGHP GVQCAQQ
