GYP3_SCHPO
ID GYP3_SCHPO Reviewed; 635 AA.
AC P87234;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=GTPase-activating protein gyp3;
GN Name=gyp3 {ECO:0000312|EMBL:CAB09776.1}; ORFNames=SPCC4G3.09c;
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:CAB09776.1}
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND THR-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Regulates exocytosis by functioning as a GAP for ypt2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Membrane
CC {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
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DR EMBL; CU329672; CAB09776.1; -; Genomic_DNA.
DR PIR; T41367; T41367.
DR RefSeq; NP_587829.1; NM_001022822.2.
DR AlphaFoldDB; P87234; -.
DR SMR; P87234; -.
DR STRING; 4896.SPCC4G3.09c.1; -.
DR iPTMnet; P87234; -.
DR MaxQB; P87234; -.
DR PaxDb; P87234; -.
DR PRIDE; P87234; -.
DR EnsemblFungi; SPCC4G3.09c.1; SPCC4G3.09c.1:pep; SPCC4G3.09c.
DR GeneID; 2539298; -.
DR KEGG; spo:SPCC4G3.09c; -.
DR PomBase; SPCC4G3.09c; gyp3.
DR VEuPathDB; FungiDB:SPCC4G3.09c; -.
DR eggNOG; KOG2058; Eukaryota.
DR HOGENOM; CLU_005350_12_3_1; -.
DR InParanoid; P87234; -.
DR OMA; VFQVIQD; -.
DR PhylomeDB; P87234; -.
DR PRO; PR:P87234; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; ISM:PomBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:PomBase.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; ISO:PomBase.
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; SSF47923; SSF47923; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTPase activation; Membrane; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..635
FT /note="GTPase-activating protein gyp3"
FT /id="PRO_0000312837"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 300..520
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 361..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 635 AA; 72790 MW; 1B1E619846E1EAFD CRC64;
MAGITEHSTI MNDANFKEEN AHLSDASIHF GSSEQDKTPS DYELDDVLDL YNDTTEDDAD
DADDVNNYIM SPSSSLSSES EHALDALVYP IYSHHNILEH ENNSDYASIT PSNHPAFTSC
AYLQNPVVDS NNEYESKFRL SLEIPPTDFL STSTELSKRE SCLSTETSSS KFSAVTAATI
TNETQSEKRS SQTDPSLPFK TNSLNCDVTY EEGPLTKKLR GPKKYKPSHS SWDIYGFKKA
NQFYTVDQYN TWYGPYSRYL ERREQRWKLF LQENGIDYIH QSPSIFPSRS AKTQRFIRKG
IPPEYRGNAW FYYSGGYELL QRNPKLYETL WRCACIKKPS DSDLIERDLY RTFPDNVHFR
HKSKHSRNSS DASEHSSEEP DVPMISKLRR VLMTFATYLP ENGYCQSLNF LAGFFLLFMS
EEKAFWMLVI TCRKYLPKMH DANLEGANID QSVLMASVRE SLPAVWSRIS LNFDGIPVND
IVAKLPPITL VTAAWFMSAF VGILPTETAL RVWDCFFYEG SKVLFMTALC ILRLGEDDIK
SKSEQTEVFQ VIQDLPKSLL DANAFLSLCF RRNFRRTPSQ KDIERRREKV AKKRNSSASK
LEMSDSSKHH LSRSSSRFSK SHIISQLHNH LKKST
