ID   GLO3_SCHPO              Reviewed;         483 AA.
AC   Q10367;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=ADP-ribosylation factor GTPase-activating protein glo3;
DE            Short=ARF GAP glo3;
GN   Name=glo3; ORFNames=SPAC22E12.17c;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
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 for the ADP ribosylation factor
CC       (ARF) family. Involved in retrograde vesicular transport from the Golgi
CC       to the endoplasmic reticulum (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:16823372}.
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DR   EMBL; CU329670; CAA93904.2; -; Genomic_DNA.
DR   PIR; T38174; T38174.
DR   RefSeq; NP_594843.2; NM_001020272.2.
DR   AlphaFoldDB; Q10367; -.
DR   SMR; Q10367; -.
DR   BioGRID; 278316; 1.
DR   STRING; 4896.SPAC22E12.17c.1; -.
DR   iPTMnet; Q10367; -.
DR   MaxQB; Q10367; -.
DR   PaxDb; Q10367; -.
DR   PRIDE; Q10367; -.
DR   EnsemblFungi; SPAC22E12.17c.1; SPAC22E12.17c.1:pep; SPAC22E12.17c.
DR   GeneID; 2541825; -.
DR   KEGG; spo:SPAC22E12.17c; -.
DR   PomBase; SPAC22E12.17c; glo3.
DR   VEuPathDB; FungiDB:SPAC22E12.17c; -.
DR   eggNOG; KOG0706; Eukaryota.
DR   HOGENOM; CLU_023062_7_0_1; -.
DR   InParanoid; Q10367; -.
DR   OMA; QNVGESI; -.
DR   Reactome; R-SPO-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-SPO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   PRO; PR:Q10367; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0030126; C:COPI vesicle coat; ISO:PomBase.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:PomBase.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR   GO; GO:0000139; C:Golgi membrane; IEA:GOC.
DR   GO; GO:0005096; F:GTPase activator activity; ISO:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048205; P:COPI coating of Golgi vesicle; ISO:PomBase.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:PomBase.
DR   GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; ISO:PomBase.
DR   Gene3D; 1.10.220.150; -; 1.
DR   InterPro; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; SSF57863; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   3: Inferred from homology;
KW   Golgi apparatus; GTPase activation; Metal-binding; Reference proteome;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..483
FT                   /note="ADP-ribosylation factor GTPase-activating protein
FT                   glo3"
FT                   /id="PRO_0000074229"
FT   DOMAIN          9..128
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   ZN_FING         24..47
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT   REGION          169..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   483 AA;  52584 MW;  A3DF7C335C0A70D8 CRC64;
     MTATKEESQK LLTSLRSQRD NKVCFDCGAK NPTWSSTTFG IYLCLDCSAA HRNMGVHISF
     VRSTVLDSWT YAQLRVMRVG GNENARNYFK RHGGVSLLNS KDCRLKYSSK TAKQYLEKLK
     SLAVEDEANY PDILDMDFLS NTHEGSSAAD TTNEDDDFFS AWDKASVKKS DDNLDDKTDL
     ASTSSSVVVE SGEKDEPVVV TEEKTMVSPP SRPDSTSTTK SKTSSISSAR ARPIRASSRP
     TASKLGASRP QKLGIKKANA DIDFDEFEKA VLSSESAPTK KPAAVASKES TVDTLVDNGV
     EEVKESTSTT VQGKPVKPVL KSAASAKSTK SDDSNLNANF ARLGFGQFAA ASNARAKAAA
     KARELKKNEV NAPTYARDHF ASQKSISSDQ YFGRGSFDPE AAAEAQERLS SFRDATAISS
     KSYFGEEEDE NEEGESSHRP DSAYLRDIAE TATEDIEAIK VAIHQGAEKL SDFIQKVGAR
     YNF