CSX2_SCHPO
ID CSX2_SCHPO Reviewed; 870 AA.
AC Q9UUE2; Q09425;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Protein csx2;
GN Name=csx2; ORFNames=SPBC17G9.08c;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 158-345.
RA Saitoh S., Takahashi K., Nabeshima K., Yamashita Y., Nakaseko Y.,
RA Hirata A., Yanagida M.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625; SER-653 AND SER-655, 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).
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DR EMBL; CU329671; CAB52806.1; -; Genomic_DNA.
DR EMBL; D83419; BAA11920.1; -; Genomic_DNA.
DR PIR; T39731; T39731.
DR RefSeq; NP_595897.1; NM_001021804.2.
DR AlphaFoldDB; Q9UUE2; -.
DR SMR; Q9UUE2; -.
DR BioGRID; 276412; 5.
DR STRING; 4896.SPBC17G9.08c.1; -.
DR iPTMnet; Q9UUE2; -.
DR MaxQB; Q9UUE2; -.
DR PaxDb; Q9UUE2; -.
DR PRIDE; Q9UUE2; -.
DR EnsemblFungi; SPBC17G9.08c.1; SPBC17G9.08c.1:pep; SPBC17G9.08c.
DR GeneID; 2539865; -.
DR KEGG; spo:SPBC17G9.08c; -.
DR PomBase; SPBC17G9.08c; -.
DR VEuPathDB; FungiDB:SPBC17G9.08c; -.
DR eggNOG; KOG0521; Eukaryota.
DR HOGENOM; CLU_002728_0_0_1; -.
DR InParanoid; Q9UUE2; -.
DR OMA; QATYFQQ; -.
DR PhylomeDB; Q9UUE2; -.
DR PRO; PR:Q9UUE2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0005096; F:GTPase activator activity; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IDA:PomBase.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR045258; ACAP1/2/3-like.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR23180; PTHR23180; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW GTPase activation; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..870
FT /note="Protein csx2"
FT /id="PRO_0000074223"
FT DOMAIN 510..614
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 670..791
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT ZN_FING 686..710
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 212..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 158..166
FT /note="NGGSPIYLC -> VVQFVLNMQ (in Ref. 2; BAA11920)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="E -> G (in Ref. 2; BAA11920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 870 AA; 99082 MW; 4B3ED6F6162E80C6 CRC64;
MTGHVDPVHF ERLKIQSVTF GSANDNASLQ VHNVSKSPEY SKYSYSRKNN EPIEFIQLRE
EEGPIVKVEE EDGLTLRFQL EFHAQEGKRD VTNLTCVYGT SPQQLDRLIT REFSSDANFQ
NNHQVFLIGN IEFHSNENSK KIEWTWSNQS LHTLYFRNGG SPIYLCFAEY DKRLNCLVPL
KTFQFYVTES DQDSTPATPF PMPMHLAEET ATSPEISDAP PLSGNVDPLP INSPPLTNPV
ARDIDQTEPE DGPLFRATIL NYERTTHDMR MVLKKLIKRI EHVAHSHGLL YMSYKELMSA
FERVATINPP AFKPFLDHYY AAAAQSFDSF NIDRARLLRN FLIEPLRKIY DTDIKNVSTK
KKDFEETSRD YYTSLSRYLS KSEKETSSDK TKESKFAAKK RDFELSRFDY YSYMQDINGG
RKGQEVLSVL TSFAANDYNL IHSSLTDIDA LRPSIIQLQD IVTEANKEFQ LLRAEREERR
RYIETSSREL EDKDAEIAAQ AYKAKVDQDT SAKQGLLLAF SKSTSDLQVV GKSGWHKYWV
VLDHGKICEY ANWKQSLELH TEPIDLLMAT VRPAQSVSRK FCFEVITPQT KRTYQATSKA
EMHSWIEAIQ YSISESIVQK GKGTSMNSEE TSVKHGPTST IGKALQRVAS VTSPSRHNSD
SKEKKQTKSP SLVKTLKEMH SSDQSCADCN TTARVEWCAI NFPVVLCIDC SGIHRSLGTH
ITKIRSLTLD KFNPETVDLL YATGNSFVNE IYEGGITDWK IKNFENQERR VQFVKDKYLY
KRFIKSSFSH DPNTGLLESI EHSNLKEAVL CLALGADVNY QRAVVKALLK NNYLIAELLT
LNGASLNVDE VTMETLSARA QAFVMNRATP
