HOB3_SCHPO
ID HOB3_SCHPO Reviewed; 264 AA.
AC Q9UUM7; P78850;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein hob3;
DE AltName: Full=Homolog of Bin3;
GN Name=hob3; ORFNames=SPBC725.09c;
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 [MRNA], AND FUNCTION.
RX PubMed=11274158; DOI=10.1074/jbc.m101096200;
RA Routhier E.L., Burn T.C., Abbaszade I., Summers M., Albright C.F.,
RA Prendergast G.C.;
RT "Human BIN3 complements the F-actin localization defects caused by loss of
RT Hob3p, the fission yeast homolog of Rvs161p.";
RL J. Biol. Chem. 276:21670-21677(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
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).
CC -!- FUNCTION: Involved in cytokinesis and septation where it has a role in
CC the localization of F-actin. {ECO:0000269|PubMed:11274158}.
CC -!- INTERACTION:
CC Q9UUM7; Q01112: cdc42; NbExp=2; IntAct=EBI-1556284, EBI-767502;
CC Q9UUM7; Q09763: gef1; NbExp=5; IntAct=EBI-1556284, EBI-1556299;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13861.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF275638; AAF86459.1; -; mRNA.
DR EMBL; D89200; BAA13861.1; ALT_INIT; mRNA.
DR EMBL; CU329671; CAA22181.1; -; Genomic_DNA.
DR PIR; T40661; T40661.
DR PIR; T43000; T43000.
DR RefSeq; NP_595489.1; NM_001021400.2.
DR AlphaFoldDB; Q9UUM7; -.
DR SMR; Q9UUM7; -.
DR BioGRID; 277675; 77.
DR IntAct; Q9UUM7; 2.
DR MINT; Q9UUM7; -.
DR STRING; 4896.SPBC725.09c.1; -.
DR iPTMnet; Q9UUM7; -.
DR MaxQB; Q9UUM7; -.
DR PaxDb; Q9UUM7; -.
DR PRIDE; Q9UUM7; -.
DR EnsemblFungi; SPBC725.09c.1; SPBC725.09c.1:pep; SPBC725.09c.
DR GeneID; 2541160; -.
DR KEGG; spo:SPBC725.09c; -.
DR PomBase; SPBC725.09c; hob3.
DR VEuPathDB; FungiDB:SPBC725.09c; -.
DR eggNOG; KOG3771; Eukaryota.
DR HOGENOM; CLU_072096_0_0_1; -.
DR InParanoid; Q9UUM7; -.
DR OMA; TRFCAYF; -.
DR PhylomeDB; Q9UUM7; -.
DR PRO; PR:Q9UUM7; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030479; C:actin cortical patch; ISO:PomBase.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IBA:GO_Central.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:1990528; C:Rvs161p-Rvs167p complex; IBA:GO_Central.
DR GO; GO:0106006; F:cytoskeletal protein-membrane anchor activity; ISM:PomBase.
DR GO; GO:0008289; F:lipid binding; ISM:PomBase.
DR GO; GO:0051666; P:actin cortical patch localization; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:PomBase.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:0097320; P:plasma membrane tubulation; IBA:GO_Central.
DR CDD; cd07591; BAR_Rvs161p; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR003005; Amphiphysin.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR037429; Rvs161/Hob3_BAR.
DR Pfam; PF03114; BAR; 1.
DR PRINTS; PR01251; AMPHIPHYSIN.
DR SMART; SM00721; BAR; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51021; BAR; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Reference proteome; Septation.
FT CHAIN 1..264
FT /note="Protein hob3"
FT /id="PRO_0000192959"
FT DOMAIN 17..237
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT COILED 25..65
FT /evidence="ECO:0000255"
FT COILED 165..187
FT /evidence="ECO:0000255"
FT CONFLICT 93
FT /note="Q -> L (in Ref. 2; BAA13861)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="E -> K (in Ref. 2; BAA13861)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 30094 MW; 845388582305AD4D CRC64;
MSWHGFKKAV NRAGTSVMMK TGHVERTVDR EFETEERRYR TMESAAKKLQ KEAKGYLDAL
RAMTASQTRI ANTIDAFYGD AGSKDGVSAY YRQVVEDLDA DTVKELDGPF RTTVLDPISR
FCSYFPDINA AITKRNHKLL DHDAMRAKVQ KLVDKPSNDT TKLPRTEKEA AMAKEVYETL
NNQLVSELPQ LIALRVPYLD PSFEALVKIQ LRFCREGYEK MAQVQQYFDN SVREDYSNGL
LDDKVEQVLQ SMRDLSIAGL NNSQ
