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FT105_SCHPO
ID   FT105_SCHPO             Reviewed;         925 AA.
AC   O13776;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Ubp5-interacting protein ftp105;
DE   AltName: Full=Down-regulated in multiple cancers 1 homolog 3;
DE   AltName: Full=Hid-1 family protein ftp105;
GN   Name=ftp105; ORFNames=SPAC17A5.16;
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   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).
RN   [3]
RP   FUNCTION.
RX   PubMed=18684775; DOI=10.1093/toxsci/kfn153;
RA   Kennedy P.J., Vashisht A.A., Hoe K.L., Kim D.U., Park H.O., Hayles J.,
RA   Russell P.;
RT   "A genome-wide screen of genes involved in cadmium tolerance in
RT   Schizosaccharomyces pombe.";
RL   Toxicol. Sci. 106:124-139(2008).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH UBP5, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=20838651; DOI=10.1371/journal.pbio.1000471;
RA   Kouranti I., McLean J.R., Feoktistova A., Liang P., Johnson A.E.,
RA   Roberts-Galbraith R.H., Gould K.L.;
RT   "A global census of fission yeast deubiquitinating enzyme localization and
RT   interaction networks reveals distinct compartmentalization profiles and
RT   overlapping functions in endocytosis and polarity.";
RL   PLoS Biol. 8:708-716(2010).
CC   -!- FUNCTION: Required for the localization of ubp5 to the Golgi apparatus.
CC       Involved in detoxification of cadmium ion.
CC       {ECO:0000269|PubMed:18684775, ECO:0000269|PubMed:20838651}.
CC   -!- SUBUNIT: Interacts with ubp5. {ECO:0000269|PubMed:20838651}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Golgi
CC       apparatus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:20838651}.
CC   -!- SIMILARITY: Belongs to the hid-1 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB11516.1; -; Genomic_DNA.
DR   PIR; T37831; T37831.
DR   RefSeq; NP_593484.1; NM_001018917.2.
DR   AlphaFoldDB; O13776; -.
DR   BioGRID; 278643; 91.
DR   STRING; 4896.SPAC17A5.16.1; -.
DR   iPTMnet; O13776; -.
DR   MaxQB; O13776; -.
DR   PaxDb; O13776; -.
DR   PRIDE; O13776; -.
DR   EnsemblFungi; SPAC17A5.16.1; SPAC17A5.16.1:pep; SPAC17A5.16.
DR   GeneID; 2542168; -.
DR   KEGG; spo:SPAC17A5.16; -.
DR   PomBase; SPAC17A5.16; ftp105.
DR   VEuPathDB; FungiDB:SPAC17A5.16; -.
DR   eggNOG; KOG2226; Eukaryota.
DR   HOGENOM; CLU_007392_0_0_1; -.
DR   InParanoid; O13776; -.
DR   OMA; VCPRPVC; -.
DR   PhylomeDB; O13776; -.
DR   PRO; PR:O13776; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0005797; C:Golgi medial cisterna; IBA:GO_Central.
DR   GO; GO:0000138; C:Golgi trans cisterna; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   InterPro; IPR026705; Hid-1/Ecm30.
DR   PANTHER; PTHR21575; PTHR21575; 1.
DR   Pfam; PF12722; Hid1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Golgi apparatus; Reference proteome.
FT   CHAIN           1..925
FT                   /note="Ubp5-interacting protein ftp105"
FT                   /id="PRO_0000116710"
FT   REGION          650..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   925 AA;  104836 MW;  432E7B468699246F CRC64;
     MGGQESKLAF QRGIARLASQ PDIPLDDEVW VSLWSVPESC PEVYDFFPPG LIREMRDHAF
     VNLEKLLLVL TSRLFALKND KKFPNPETAP ASEALNCIRL LTRIIPFLNE KLDLEEWHQK
     FWWSLRKKRN LPKENSELDL SNFQDDLDFE NSISQKNEFS QKSPSVPLSP VSTFPASSIS
     LDASSDVSAA DVSVGGSSTI KEIGSIEETF THEKTLMEEL LDTVFRLLFC RGFTLPLSSP
     EQYAYIIWEN GIGTTETQEK TTKELAFNRI EVLRLLLVLI SKRLYRSSEV ASHTLTYLTC
     VANKQLILVF LYSLINTTLR LRPDSWKASY STLVPYNDSS IALSKLTSQI LLLFLDHTPH
     ETTVEYFRQR LNLSPGAAIE NQYRLYFSRL QLQADYEFLV NELYRLLNAP VSAISAYISI
     VQKPNIAFPE IILFLWQAIL YNKRFRAFLI TSPYATEFLT SIQFYALRYR EDNEHSGLVR
     ICLFIVHYLS CEKVLCEKLN RNCMNAQSLM SSLGFSVPPM SYAEFLIISS FHISAVKRSP
     FSSLSPVILL TICNIAPFVE NLSFVTCAKL MQLCSSLSSP RFLFRNPRNH LLLEYLLQAI
     SSIVENKFSQ NPNLSYSIIR LQQVFLNLNS MKLPAVAQTK SQPLVALNSE GSSDFESKSS
     DNTSLDGTPL QNTDFKKVAT VEDDSPFDEL DKFSSPFSSS SSRGGLSHIS SRNVSISVPT
     VLQDVFSDSP LVLSRKLRGK IPENVSSSEL IKKCASNPFG KDLEIDSNLF APSNSWFNSW
     HSRLELDSIL AIISQFSLPV YKKMNEELST TDEAVKLLAN SVLNDVHPRV PNFRYFIWSV
     PMNNWFQSLV WLYTLSFDEK GLMATPSLFT TSKVYKQHGN IMKVASPENS SNSMENATKS
     ILDKLDLLYL QLPSSVNHDS SLRNK
 
 
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