YH51_SCHPO
ID YH51_SCHPO Reviewed; 834 AA.
AC O43048;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 4.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=TBC domain-containing protein C215.01;
GN ORFNames=SPBC215.01, SPBC3B9.20;
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 GTPase-activating protein for Rab family
CC protein(s). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Note=Localizes also to the barrier septum.
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DR EMBL; CU329671; CAA17800.2; -; Genomic_DNA.
DR RefSeq; NP_596678.2; NM_001022600.3.
DR AlphaFoldDB; O43048; -.
DR SMR; O43048; -.
DR BioGRID; 277062; 32.
DR STRING; 4896.SPBC215.01.1; -.
DR iPTMnet; O43048; -.
DR MaxQB; O43048; -.
DR PaxDb; O43048; -.
DR PRIDE; O43048; -.
DR EnsemblFungi; SPBC215.01.1; SPBC215.01.1:pep; SPBC215.01.
DR GeneID; 2540535; -.
DR KEGG; spo:SPBC215.01; -.
DR PomBase; SPBC215.01; -.
DR VEuPathDB; FungiDB:SPBC215.01; -.
DR eggNOG; KOG4347; Eukaryota.
DR HOGENOM; CLU_003538_1_0_1; -.
DR InParanoid; O43048; -.
DR OMA; ICEDYIP; -.
DR PhylomeDB; O43048; -.
DR PRO; PR:O43048; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005509; F:calcium ion binding; ISM:PomBase.
DR GO; GO:0005096; F:GTPase activator activity; ISM:PomBase.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; NAS:PomBase.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 3: Inferred from homology;
KW Calcium; Cytoplasm; GTPase activation; Metal-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..834
FT /note="TBC domain-containing protein C215.01"
FT /id="PRO_0000353839"
FT DOMAIN 220..408
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 576..611
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 612..647
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 766..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 589
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 591
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 593
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 595
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 625
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 627
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 629
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 636
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 834 AA; 95006 MW; 27A05A66CAB3293C CRC64;
MSSLASLIKT KLKLPDSSKN LNKLRWKFRL LESQFALYSL PCQLRFVHYN NLEDPNSFNG
LLYLFTDYIA FQGDDESNQF CMPYTIIRKV SRVKSNDLEQ LLSVSTSNGY EYRISLQVSE
TTAAHFCQLL REELVSHKAD MQRSSEFSKQ FFSERLCKPN VPEPETKDSY GFGARYGYPT
DPRISRERAK LRMWKEYFLL YGANLSLIRV SLFSKLVRIE LPNKLRGEIW ELTSGSMYFR
LENSDEYDHL LKVYSGQTSF SLEEIEKDLG RSLPEYPAYQ NEEGINALRN VLVAFSWKNQ
EVGYCQAMNI VAAALLIHCT EEQTFFLMHK ICEDYIPGYY SKTMYGTLID QQVYESLVQR
SMPNLHAHFV SKDIQLSIIS LPWFLSLFLC TMPLPYAFRL LDFFFLEGPR VLFQIGMAIL
YDNEAEIMKA TEDTMLISIL KNYFSSLGDK AYKDATDKRV ASITKFQLLL VTAFKKFSHI
THSLIEDERK KHYEGVMNSI ESFAKRTQIR SLQNYGTLTR TDLSNIYDRY HEVLSSKHRV
GLGSSTDTRL EFDEFCIFLA GVTEWAKGLD AAAINNSSSF LRHLFLRFDK SMTGSLSLQD
LVSGIAELKF RDVMRNISFI FELYDFNGDG FMDKPDVLKV SEAILWLTRF MGDEYLSAVS
EFIQRCFHFA DEASPDGHSD TLIDISDHMS STGSENRSVG ANSDIKVSLP TFRMVVLSIG
LLEQLFSGGL ADSIVLAPVQ EKSSTTGGLR GLLDSLVIDT NRIGKTFRGH KPASRPSTAN
GTSNQNTTSE ITTSETTATE KTPSNSSDTE DDVGDVVEND KDLLQFDPYK KNDA
