GYP51_SCHPO
ID GYP51_SCHPO Reviewed; 1031 AA.
AC Q10496;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=GTPase activating protein Gyp51;
GN Name=gyp51; ORFNames=SPAC26F1.09;
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: GTPase-activating protein involved in ER to Golgi trafficking
CC and polarized exocytosis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the GYP5 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA97366.1; -; Genomic_DNA.
DR PIR; T38411; T38411.
DR RefSeq; NP_594886.1; NM_001020315.2.
DR AlphaFoldDB; Q10496; -.
DR SMR; Q10496; -.
DR BioGRID; 279133; 12.
DR STRING; 4896.SPAC26F1.09.1; -.
DR iPTMnet; Q10496; -.
DR MaxQB; Q10496; -.
DR PaxDb; Q10496; -.
DR PRIDE; Q10496; -.
DR EnsemblFungi; SPAC26F1.09.1; SPAC26F1.09.1:pep; SPAC26F1.09.
DR GeneID; 2542680; -.
DR KEGG; spo:SPAC26F1.09; -.
DR PomBase; SPAC26F1.09; gyp51.
DR VEuPathDB; FungiDB:SPAC26F1.09; -.
DR eggNOG; KOG1102; Eukaryota.
DR HOGENOM; CLU_302886_0_0_1; -.
DR InParanoid; Q10496; -.
DR OMA; NCETEAD; -.
DR PhylomeDB; Q10496; -.
DR Reactome; R-SPO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR PRO; PR:Q10496; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISO:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:PomBase.
DR GO; GO:0005096; F:GTPase activator activity; ISO:PomBase.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:PomBase.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0023052; P:signaling; IC: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 3: Inferred from homology;
KW Cytoplasm; ER-Golgi transport; Exocytosis; GTPase activation; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1031
FT /note="GTPase activating protein Gyp51"
FT /id="PRO_0000208061"
FT TRANSMEM 798..818
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 610..806
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT REGION 1..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1031 AA; 116290 MW; F2579A4C421D79EC CRC64;
MAFTEANERE VQSSYEKENV KIIREEEAKD QESTDDIAVE DGTGTSPDLN FFSTQNVMQM
NFEDEYSEFS NEDDEAEIDN SFADSIPNEP EIPDMQDEYS RDSHSQQSVE EQNNTTNTDE
DASVNEFSVA ADISDVNTLG KDNSESTEEP VNEVNETATL GNEDVGERSG FPSEGLDNEP
ESQRDLDETG NLAPEDLKDE VKSVHEFNEP NDLRQQEESY SDDDDTNVNE FEDVNEIENE
HQLSVADEDQ TSRLVKGKMI FVGKEDFGEE ADISNSVFIE QNGPNSDTVS GFKETSSIVN
SSSTTEKPGV ALDSQNDTSI FNEEQTNSLT ETFNDLTLDH LPENVESEPV AGKENETAKN
ESGASDNDHK ANVHVFVLKS SEDAITLNEE KIATQDDPLE APTPIVASSS TIFLNSNQRN
DELSASGSQE PHPKDGTNST SSLPLDTNNL SNSEPPSHVL DASSETIEVI QTIKKLQNQV
PETIKDEVGK KNTAFSPGTS LSTNHVKTKS RSAHNNSTSP FSTAVSSWLN PLRYPSDKSP
RVISSYLESV FISKPRSIGD AQKLEILEYL QSQSSTVSNQ VFTLLSNFIQ NPLFVLDECF
DEFRNLILMH NSHTVHTVVW KTISSWTSYD YEMQYSSLSI KNCDSDKAIR KDLDRTFAPE
ILSHFFSNRQ QLEPTDNIAE STANLHRVLR SLAIVLPQVG YTQGMSWIAG ALLMHLPAPQ
AFALLVFLFK NYHLQNIFSS EMRGLSRVLH QFTRLVEDYM PSLAIHFKRQ DIKTCSYASE
WFLTLFAYKF PLEVVAHLYD ILFLYGPGIL FNFGLALLSH SQESLLKLNM DRLISYLKED
IFLAFKETQE GENYDTSLFV KTAFSFEIQP DVLDRYGNEY DILLKSEHEL DSSLEEMRNR
HKSLNEHFIM LSDSMANLQV EHENMSALLL KEKMYLKNQT VEQASLKSEI ASLNSQLAKQ
KSEIEQAFQG DMEAIIAENL EIMVESQSLE DEIFRKEKQL AETKVNLAVL DEDHMMALQK
WSQLMNRIKT K
