POB1_SCHPO
ID POB1_SCHPO Reviewed; 871 AA.
AC O74653;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein pob1;
DE AltName: Full=BOI protein homolog;
GN Name=pob1; ORFNames=SPBC1289.04c;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10436025; DOI=10.1091/mbc.10.8.2745;
RA Toya M., Iino Y., Yamamoto M.;
RT "Fission yeast Pob1p, which is homologous to budding yeast boi proteins and
RT exhibits subcellular localization close to actin patches, is essential for
RT cell elongation and separation.";
RL Mol. Biol. Cell 10:2745-2757(1999).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-225; TYR-229;
RP SER-241; SER-433; SER-439; SER-440; THR-442; SER-444 AND SER-549, 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: Has a role in cell elongation and separation.
CC {ECO:0000269|PubMed:10436025}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10436025}. Membrane
CC {ECO:0000269|PubMed:10436025}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10436025}. Note=Membrane-associated at the cell
CC tips during interphase.
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DR EMBL; AB018044; BAA33490.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB38684.1; -; Genomic_DNA.
DR PIR; T43427; T43427.
DR RefSeq; NP_596828.1; NM_001023849.2.
DR AlphaFoldDB; O74653; -.
DR SMR; O74653; -.
DR BioGRID; 276536; 16.
DR STRING; 4896.SPBC1289.04c.1; -.
DR iPTMnet; O74653; -.
DR MaxQB; O74653; -.
DR PaxDb; O74653; -.
DR PRIDE; O74653; -.
DR EnsemblFungi; SPBC1289.04c.1; SPBC1289.04c.1:pep; SPBC1289.04c.
DR GeneID; 2539992; -.
DR KEGG; spo:SPBC1289.04c; -.
DR PomBase; SPBC1289.04c; pob1.
DR VEuPathDB; FungiDB:SPBC1289.04c; -.
DR eggNOG; ENOG502QPMX; Eukaryota.
DR HOGENOM; CLU_306775_0_0_1; -.
DR InParanoid; O74653; -.
DR OMA; HYFQVDN; -.
DR PhylomeDB; O74653; -.
DR PRO; PR:O74653; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; ISM:PomBase.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IGI:PomBase.
DR GO; GO:0001881; P:receptor recycling; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR045188; Boi1/Boi2-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR22902; PTHR22902; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..871
FT /note="Protein pob1"
FT /id="PRO_0000058504"
FT DOMAIN 2..65
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 250..313
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 698..808
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 42..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 229
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 442
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 871 AA; 93773 MW; 28F2F12D5F814BF9 CRC64;
MASQRFVIAL HSFPGKSSDE LPLVEGRKYL LIKMDEEFGD GWWEGEDEQG NRGIFPASHV
ELISDERSDS SDSRRGKEDF SISTAEVTRS SLSSSRSTSS RSDKDSEKLY SNNSLSSSHS
SILNGPLDSL SKPSVPSNFN SMFPSSKQEG PSPLLDNQPS SDLSNFNTID ADYNNASAST
SAPATSASLK KVLSAEDSVR ETITDIETAL QNMSTSASRT PNDSSPLPYI ENRPASSLAV
SEKIQNVPNW STEEVVEWLM NAGLGSVAPN FAENEITGEI LLGLDSNVLK ELNITSFGKR
FEVLRKIQQL KDSYEQSLYE EYPQFAEPIS VSQSSDSSSS IPKKSNDEAG GSPSKSSPTR
PGFNDYVNRP TSVMPSLSNM IVSPDLDSSP STDWNQYVIP PLATPSSRNS KSTQSAVPEN
VSRFDSNEPS ATSPILKRSS PTDSISQNSG LPSRLTEPIS SPSTSSIDVD KEGTSFPGLP
YHSSKGNLYA PQPSSNVPTK FTGGASESSS VPPRPIPSAM KGKAPASAIS IEALEELDPP
KITTIDGESP SSISSRLPSS NLEQGSSSSV TKSPESMPDP SAKASSPVTS KGVSINEKSA
VNNYATPLSK PQPKDTKGSK LGNTFVAPSP AASLPASPPV GTELKTRPTL RSVASSPLNK
EPIGKRKSKR DIFGRQKVLP TGISEGLSNI PAKEAIKTAD CHGWMRKRSD RYGVWKSRYF
VLKGTRLSYY HSLNDASEKG LIDMTSHRVT KTDDIVLSGG KTAIKLIPPA PGAAKAAVMF
TPPKVHYFTC ENNEELHRWS SAFLKATVER DMSVPVLTTS RMPTISLSKA KELRTRPPSL
LIDDENEANL TSSIGLKKNA KQKNKKSSKQ K
