ID YB35_SCHPO Reviewed; 1310 AA.
AC O14340;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 27-MAR-2024, entry version 151.
DE RecName: Full=Oxysterol-binding protein homolog C2F12.05c;
GN ORFNames=SPBC2F12.05c;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384 AND SER-394, 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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH DIL1.
RX PubMed=20404563; DOI=10.4161/cc.9.9.11526;
RA Rumpf C., Cipak L., Novatchkova M., Li Z., Polakova S., Dudas A.,
RA Kovacikova I., Miadokova E., Ammerer G., Gregan J.;
RT "High-throughput knockout screen in Schizosaccharomyces pombe identifies a
RT novel gene required for efficient homolog disjunction during meiosis I.";
RL Cell Cycle 9:1802-1808(2010).
CC -!- SUBUNIT: Interacts with dil1. {ECO:0000269|PubMed:20404563}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
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DR EMBL; CU329671; CAB10154.2; -; Genomic_DNA.
DR PIR; T40135; T40135.
DR RefSeq; NP_595710.1; NM_001021607.2.
DR AlphaFoldDB; O14340; -.
DR SMR; O14340; -.
DR BioGRID; 276886; 23.
DR IntAct; O14340; 1.
DR STRING; 284812.O14340; -.
DR iPTMnet; O14340; -.
DR MaxQB; O14340; -.
DR PaxDb; 4896-SPBC2F12-05c-1; -.
DR EnsemblFungi; SPBC2F12.05c.1; SPBC2F12.05c.1:pep; SPBC2F12.05c.
DR GeneID; 2540357; -.
DR KEGG; spo:SPBC2F12.05c; -.
DR PomBase; SPBC2F12.05c; -.
DR VEuPathDB; FungiDB:SPBC2F12.05c; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1737; Eukaryota.
DR HOGENOM; CLU_001040_1_1_1; -.
DR InParanoid; O14340; -.
DR OMA; SIRQMWE; -.
DR PhylomeDB; O14340; -.
DR Reactome; R-SPO-192105; Synthesis of bile acids and bile salts.
DR PRO; PR:O14340; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; ISO:PomBase.
DR GO; GO:0008142; F:oxysterol binding; ISO:PomBase.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0120015; F:sterol transfer activity; ISO:PomBase.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0030011; P:maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0015918; P:sterol transport; ISO:PomBase.
DR CDD; cd13292; PH_Osh1p_Osh2p_yeast; 1.
DR Gene3D; 2.40.160.120; -; 1.
DR Gene3D; 3.30.70.3490; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972:SF205; OXYSTEROL-BINDING PROTEIN; 1.
DR PANTHER; PTHR10972; OXYSTEROL-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF144000; Oxysterol-binding protein-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Lipid transport; Lipid-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..1310
FT /note="Oxysterol-binding protein homolog C2F12.05c"
FT /id="PRO_0000100394"
FT REPEAT 54..84
FT /note="ANK 1"
FT REPEAT 88..118
FT /note="ANK 2"
FT REPEAT 188..217
FT /note="ANK 3"
FT DOMAIN 254..349
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1310 AA; 148475 MW; E6F284F09C073262 CRC64;
MEHPSPDSVS STSSSDHKKA ELSDSLKQLQ LLQAFQAGDI KQVDNLLHNK SKDECTHALF
ISIQCANVQM VKHILSVFDV DVNAYDKNKN TPLHLAAMAG RQDIVEALLL HPDINYNLVN
ANNKKAYQVA TSPQLMDFMK GFYVTYTKET AREFKKAFKE RNLESMDYLM RHNEFNDAID
LNEVDIKTGQ TYLHVATKAK DAELVKWLLD NGADPYRRDK FGKLPTDYTK DENMRSLLRS
YSGNRDSSSA PAVPQHMSGY LKKWTNYKSG YKLRWFTLNN GVLSYYKNQD DASSACRGSI
NLKLARLVHD PKQPTVFQVI GKGSVRYSVK ANSPVEAKKW IAAISSAIEN DEEANKPNVT
ADNASFGTHD LAPAAHKFTQ SNASGNSGWD DNESDIDRAQ LPSRENFEFN VNIAKLQVET
LHKLIDSAMQ TEKVKKDPSL SQVFDGISNS FNTLHKTVLE MLDLQRQAEH YYKRKLDNAK
AINALWAENL KTVVEEQDQI EERYHRSEAH RRRTKRAFRR LAASLKKRPS DKDNKLHIHY
DDGAMSSTSY STDFTDDEEE TNTKDEFFDV DAHDNNHANK AEPSQTANNV HEIREPSFSS
EHKPQPSLKT TTDVSSPETK QNIADIRKTT LTDQTEEFTE RRDNNGSIPS KQPSDEQHLG
KESLPSQQST VSNHHRKESI PSKQPTEGQH ARQESLPSQQ TTETKHLRKE STPSKQPTEG
QHTRQESLPS QQTTETKHLR KESIPSKQPT EGQHARQESL PSQQTTETKH LRKESIPSKQ
PSGGQQLRQE SLPSQQSSES KQSTQHQQPV EVQKSIQSDV SAPKAKEVSE KPVSHQAKPS
NASQLSRNTD DTQAKEAPKE ASIPDNASTA STKVSNDSHL KPDADKKSVS SELTHASKPS
LDEKTMQLAK QIAVSFHGYE APTRENLDVN DDRPKISLWG ILKGMIGKDM TKMTLPVSFN
EPTSLLQRVA EDMEYTELLD QASHNKDPYQ RILYVAAFAA SEYASTLNRV AKPFNPLLGE
TYEFCHPQRG FRFIVEQVSH HPPVGAAYSE SANWKYYGES SVKSKFYGKS FDISPLGTWF
LELRHPSGEV ELYTWKKVTS SVVGIILGSP SVDNYGQMHI VNHSSGINCV LDFKPRGWRG
TNAHEVKGSV QSTDDTPKWM VNGHWNDKIF GQQPNGNKIL LWQNHERPPR PFNLTPFAIS
LNALTPQLKP WLPPTDTRLR PDQRAMENGQ YDLAASEKNR LEEKQRKKRR MREQGEMPPW
SPRWFSAAKH PVTGEDYWQF NNEYWKIREE AGEAHLAGKE FEWPNVDDIF
//
