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   02-JUN-2021, entry version 133.
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   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; IDFRGEG; -.
DR   PhylomeDB; O74752; -.
DR   Reactome; R-SPO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
DR   PRO; PR:O74752; -.
DR   Proteomes; UP000002485; Chromosome II.
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: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:0006457; P:protein folding; IEA:InterPro.
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          129..131
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          209..210
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          241..243
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   REGION          375..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           137
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250"
FT   METAL           140
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250"
FT   METAL           153
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000250"
FT   METAL           156
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000250"
FT   METAL           179
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000250"
FT   METAL           182
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000250"
FT   METAL           195
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250"
FT   METAL           198
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /note="Substrate; via amide nitrogen"
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
//