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 24-JUL-2024, entry version 145. 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}. 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; 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; 18. DR IntAct; O74752; 1. DR STRING; 284812.O74752; -. DR iPTMnet; O74752; -. DR PaxDb; 4896-SPBC1734-11-1; -. 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: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:0051087; F:protein-folding chaperone binding; IBA:GO_Central. 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: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 GO; GO:0031048; P:regulatory ncRNA-mediated heterochromatin formation; IMP:PomBase. DR CDD; cd06257; DnaJ; 1. DR CDD; cd10747; DnaJ_C; 1. DR CDD; cd10719; DnaJ_zf; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1. DR Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2. 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:SF10; DNAJ-LIKE-2, ISOFORM A; 1. DR PANTHER; PTHR43888; DNAJ-LIKE-2, ISOFORM A-RELATED; 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; Chaperone J-domain; 1. DR SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1. DR SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2. 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 //