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 12-APR-2017, entry version 113. 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; OC Schizosaccharomycetaceae; 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., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., 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 RT fission 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 CC organization. {ECO:0000250, ECO:0000269|PubMed:15797925}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. CC Nucleus {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 ProteinModelPortal; O74752; -. DR SMR; O74752; -. DR BioGrid; 276226; 6. DR IntAct; O74752; 1. DR MINT; MINT-4680451; -. DR MaxQB; O74752; -. DR PRIDE; O74752; -. DR EnsemblFungi; SPBC1734.11.1; SPBC1734.11.1:pep; SPBC1734.11. DR GeneID; 2539671; -. DR KEGG; spo:SPBC1734.11; -. DR EuPathDB; FungiDB:SPBC1734.11; -. DR PomBase; SPBC1734.11; mas5. DR HOGENOM; HOG000226718; -. DR InParanoid; O74752; -. DR KO; K09503; -. DR OMA; ETIRDED; -. DR OrthoDB; EOG092C1UGR; -. DR PhylomeDB; O74752; -. DR PRO; PR:O74752; -. DR Proteomes; UP000002485; Chromosome II. DR GO; GO:0005829; C:cytosol; IDA:PomBase. DR GO; GO:0005634; C:nucleus; 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:0000226; P:microtubule cytoskeleton organization; IMP:PomBase. DR GO; GO:1900035; P:negative regulation of cellular response to heat; IMP:PomBase. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0009408; P:response to heat; IEA:InterPro. DR CDD; cd06257; DnaJ; 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; IPR008971; HSP40/DnaJ_pept-bd. DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom. 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; 3. 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; Complete proteome; Cytoplasm; Lipoprotein; Metal-binding; KW Methylation; Nucleus; Prenylation; Protein transport; KW Reference proteome; Repeat; Transport; Zinc; Zinc-finger. FT CHAIN 1 404 Mitochondrial protein import protein FT mas5. FT /FTId=PRO_0000314107. FT PROPEP 405 407 Removed in mature form. {ECO:0000250}. FT /FTId=PRO_0000396683. FT DOMAIN 6 68 J. FT REPEAT 137 144 CXXCXGXG motif. FT REPEAT 153 160 CXXCXGXG motif. FT REPEAT 179 186 CXXCXGXG motif. FT REPEAT 195 202 CXXCXGXG motif. FT ZN_FING 124 207 CR-type. FT REGION 129 131 Substrate binding. {ECO:0000250}. FT REGION 209 210 Substrate binding. {ECO:0000250}. FT REGION 241 243 Substrate binding. {ECO:0000250}. FT COMPBIAS 68 107 Gly-rich. FT METAL 137 137 Zinc 1. {ECO:0000250}. FT METAL 140 140 Zinc 1. {ECO:0000250}. FT METAL 153 153 Zinc 2. {ECO:0000250}. FT METAL 156 156 Zinc 2. {ECO:0000250}. FT METAL 179 179 Zinc 2. {ECO:0000250}. FT METAL 182 182 Zinc 2. {ECO:0000250}. FT METAL 195 195 Zinc 1. {ECO:0000250}. FT METAL 198 198 Zinc 1. {ECO:0000250}. FT BINDING 110 110 Substrate; via amide nitrogen. FT {ECO:0000250}. FT SITE 329 329 Involved in dimerization. {ECO:0000250}. FT MOD_RES 404 404 Cysteine methyl ester. {ECO:0000250}. FT LIPID 404 404 S-farnesyl cysteine. {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 //