RNG3_SCHPO
ID RNG3_SCHPO Reviewed; 746 AA.
AC O74994;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Ring assembly protein 3;
GN Name=rng3; ORFNames=SPCC613.04c;
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.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10852821; DOI=10.1242/jcs.113.13.2421;
RA Wong K.C.Y., Naqvi N.I., Iino Y., Yamamoto M., Balasubramanian M.K.;
RT "Fission yeast Rng3p: an UCS-domain protein that mediates myosin II
RT assembly during cytokinesis.";
RL J. Cell Sci. 113:2421-2432(2000).
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).
CC -!- FUNCTION: Essential for actinomyosin ring assembly during cytokinesis.
CC Has a role, in conjunction with F-actin, in assembling myosin II-
CC containing proteins, such as myo2, at the division site.
CC {ECO:0000269|PubMed:10852821}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10852821}.
CC Note=Associated with the actinomyosin ring.
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DR EMBL; AJ011773; CAA09767.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA21056.1; -; Genomic_DNA.
DR PIR; T43648; T43648.
DR RefSeq; NP_587692.1; NM_001022687.2.
DR AlphaFoldDB; O74994; -.
DR SMR; O74994; -.
DR BioGRID; 275926; 20.
DR STRING; 4896.SPCC613.04c.1; -.
DR SwissPalm; O74994; -.
DR MaxQB; O74994; -.
DR PaxDb; O74994; -.
DR EnsemblFungi; SPCC613.04c.1; SPCC613.04c.1:pep; SPCC613.04c.
DR GeneID; 2539360; -.
DR KEGG; spo:SPCC613.04c; -.
DR PomBase; SPCC613.04c; rng3.
DR VEuPathDB; FungiDB:SPCC613.04c; -.
DR eggNOG; KOG4151; Eukaryota.
DR HOGENOM; CLU_381374_0_0_1; -.
DR InParanoid; O74994; -.
DR OMA; IHKECSE; -.
DR PhylomeDB; O74994; -.
DR PRO; PR:O74994; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0005844; C:polysome; IDA:PomBase.
DR GO; GO:0051879; F:Hsp90 protein binding; IBA:GO_Central.
DR GO; GO:0017022; F:myosin binding; ISO:PomBase.
DR GO; GO:0044183; F:protein folding chaperone; EXP:PomBase.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; EXP:PomBase.
DR GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; IMP:PomBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 4: Predicted;
KW Cell cycle; Cell division; Cytoplasm; Reference proteome; Septation.
FT CHAIN 1..746
FT /note="Ring assembly protein 3"
FT /id="PRO_0000097380"
SQ SEQUENCE 746 AA; 84472 MW; A0158CEDB110D71E CRC64;
MTHELSSTPQ IDLLNDILKN SVESNVFSDY QKKQIVTLIL KSKISTAIVL LSPKSTAASE
WNYLCNLQDL HECVLCVDTI LPANLQTIAK RIFSLVLLPP LNDWCKQLRD AFLRFVSQPS
ICPTDFPLKL FFLSTVGIEL LIVNEKIIPQ KTQKYLLYEL FSSPSSITAN EIARLCQEAN
NRNYLLQSLT SATDARRAFL NNPNYRLLSA IIFQDGPSNL AFVLAKDCVL LARQPETIPV
SFERMSSLLL MCLPSHPDFI SPEFCHEWTE LAERNGLQEE WLNILNTACN FKECRAIIHK
ECSEFIKDNH TSRVAILISM KLAFQYQLSQ VIPTLKLLLQ SKVYDSVLLE ALRQSSTLGP
VKQLIADDSC LLNNLSKLLL DTNISPLDAS SIATIIYNMC KFKITKSEHE RELNQLRNMA
EASKTIDYKE DETAPTERRI QKILEYDILS KLFSAAKHYN SLNGLLAMIL VHMANYKLAR
RKLVQIGALK FLTRQCFIQT QDSNAAFALA KILISVAPHS IFTKAFPSNR AIHPMSKLLS
TNSADTEYPI LLGKFEVLLA LTNLASHDEE SRQAIVQECW RELDELIIET NPLIQRATTE
LINNLSLSPY CLIKFIGDKD SDFENTRLHI VLALSDTEDT PTRLAACGIL VQITSVDEGC
KKILSLQNDF NYIVRMLTDQ DEGIQHRGLV CICNIVYSKD QEIFNKFIKT PKAVETLRTY
ITKQAALKEL QHEALVMIDS RLQGSK
