GYP2_SCHPO
ID GYP2_SCHPO Reviewed; 720 AA.
AC O94711;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=GTPase-activating protein gyp2;
GN Name=gyp2 {ECO:0000312|EMBL:CAA22549.1}; ORFNames=SPCC1259.11c;
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] {ECO:0000312|EMBL:CAA22549.1}
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] {ECO:0000305}
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: Stimulates specifically the GTPase activity of ypt2 and ryh1.
CC Inactivates ryh1 during recycling between the endosome and the Golgi
CC compartments (By similarity). {ECO:0000250|UniProtKB:P53258}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329672; CAA22549.1; -; Genomic_DNA.
DR PIR; T40900; T40900.
DR RefSeq; NP_588067.1; NM_001023059.2.
DR AlphaFoldDB; O94711; -.
DR SMR; O94711; -.
DR BioGRID; 275712; 4.
DR STRING; 4896.SPCC1259.11c.1; -.
DR MaxQB; O94711; -.
DR PaxDb; O94711; -.
DR EnsemblFungi; SPCC1259.11c.1; SPCC1259.11c.1:pep; SPCC1259.11c.
DR GeneID; 2539140; -.
DR KEGG; spo:SPCC1259.11c; -.
DR PomBase; SPCC1259.11c; gyp2.
DR VEuPathDB; FungiDB:SPCC1259.11c; -.
DR eggNOG; KOG4347; Eukaryota.
DR HOGENOM; CLU_003538_0_1_1; -.
DR InParanoid; O94711; -.
DR OMA; QAYFLFS; -.
DR PhylomeDB; O94711; -.
DR PRO; PR:O94711; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA: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 Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTPase activation; Nucleus; Reference proteome.
FT CHAIN 1..720
FT /note="GTPase-activating protein gyp2"
FT /id="PRO_0000312836"
FT DOMAIN 20..85
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 216..404
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
SQ SEQUENCE 720 AA; 82749 MW; 7CFF5D45AB1E3BE4 CRC64;
MNLLKHIFLE DDYDAYEGTL DPASFFRINK QEEIIASTVC EIGWEYSKSF GNAYICTSFL
CFHSDDFKTR FTFPLAAVRK LERENSDNDT FTFDLSNFHS QIIHLRFKGT RQQSEFFCDR
LVRQLHASLE DASSVGLFLL SLASERVCFS ESANSQEIES IDLGLGSQFG YPIASSNTNG
LINENNSKSW IQYLKKNGAN FNLIQTPNFQ KLVQSGIPNN LRADIWETCS GSLFPRWKSK
GFYAKNIDSV INNRCEYSEE IEKDLTRSLP DYPAYQSPTG INTLRRILLF YSETNKEVGY
CQAMNIVLAA LLVYCTEEQA YFLFSQLCEF YIPGYYAKII HGLLLDLTVF EYVLEHTLPH
LYQKIIELDM DLKLITINWF FSLFIKDFRL DYAFRILDCL FVNGPRVLFQ VALALFKVNA
QGILNATDDS SVMKVFRQCF DHINQGTAAD EKMAALGSRS SMCTLPQLFA VAFEYFDFIT
DSFVSAKRKE FKSSVLYSLR CFTKRSHLRS VYQTTLLSNT DLDLVYDAFI NAIGENNICH
GDVLEQKIDF NGFERLVDCA APPLSVIREP LHYQRSKRKL FTRLYIWMKD GDSTETSLTF
KRIIHGLERL KADIALHSEI LCFQLYDLKR DGTLRTEEVV ELSESLILLC CYEGDEKDEE
RLTVISEFLK SCFSGCQDRR SFQITMEDFQ AIVDTTGLHA TLEFFLKKLI DGLLGKLNAS