EPT1_SCHPO
ID EPT1_SCHPO Reviewed; 547 AA.
AC O13747;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=RING finger protein ETP1 homolog;
DE AltName: Full=BRAP2 homolog;
GN ORFNames=SPAC16E8.13;
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).
CC -!- FUNCTION: May act as a cytoplasmic retention protein with a role in
CC regulating nuclear transport. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAB11041.1; -; Genomic_DNA.
DR PIR; T37793; T37793.
DR RefSeq; NP_594226.1; NM_001019649.2.
DR AlphaFoldDB; O13747; -.
DR SMR; O13747; -.
DR BioGRID; 278799; 1.
DR STRING; 4896.SPAC16E8.13.1; -.
DR iPTMnet; O13747; -.
DR MaxQB; O13747; -.
DR PaxDb; O13747; -.
DR PRIDE; O13747; -.
DR EnsemblFungi; SPAC16E8.13.1; SPAC16E8.13.1:pep; SPAC16E8.13.
DR GeneID; 2542333; -.
DR KEGG; spo:SPAC16E8.13; -.
DR PomBase; SPAC16E8.13; -.
DR VEuPathDB; FungiDB:SPAC16E8.13; -.
DR eggNOG; KOG0804; Eukaryota.
DR HOGENOM; CLU_009969_0_1_1; -.
DR InParanoid; O13747; -.
DR OMA; GIIHLYK; -.
DR PhylomeDB; O13747; -.
DR PRO; PR:O13747; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISM:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0023051; P:regulation of signaling; ISS:PomBase.
DR CDD; cd12717; RRM_ETP1; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR011422; BRAP2.
DR InterPro; IPR034931; ETP1_RRM.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF07576; BRAP2; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..547
FT /note="RING finger protein ETP1 homolog"
FT /id="PRO_0000056332"
FT ZN_FING 208..248
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 245..338
FT /note="UBP-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 514..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
SQ SEQUENCE 547 AA; 61825 MW; 2C3FDB4FD7CF70E1 CRC64;
MYYYLEIECE SPVKDIFTCN KRRASKVVGN SFGGDHFNFR LGEIKLLSMD FPSSKVPEVE
ETSLGHGVVH LYRVFPSESH EFDAPGLILA ILAIPLYMSP SDVLGFLGEK HCKSIQHIRL
LKTKDPNRIM ALLKFKDQAS VIRFYTEFNG KAFSQIDPET CHVLHIDKVN IKYPMESSDS
SSTEQQLVGP SSKPFASTTP ALIELPTCVV CLERMDSSIT GLITIVCQHT FHCPCLQKWG
NSSCPVCRYT QKVQSSEFQS KCTVCCYDKD LWICLICGNI GCGRYHDAHA KQHYVDTAHC
YAMELETQRV WDYAGDNYVH RLLQSETDGK LVELSTDGKS SGWTGSSATE SKLRDKMGLE
YTQILVSQLE SQRLYYESHL SNMSQKLSRV NEELVLKTKI ATASSNANTD LRSRVDISES
KLKKRDDKLK RVSSQLEHLK HNYEEEKSMN ENLLVRIQTL EKQNTTKSDQ IVSMQFQIND
LNEQLRDLMF TISASQEIQK MGQSEELQNG TIVLPNNSTV RSNSVKSKKK KKKKPVVPSS
SGSLGTD
