SEC8_SCHPO
ID SEC8_SCHPO Reviewed; 1073 AA.
AC O74562;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Exocyst complex component sec8;
GN Name=sec8; ORFNames=SPCC970.09;
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, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION IN THE EXOCYST COMPLEX.
RX PubMed=11854409; DOI=10.1091/mbc.01-11-0542;
RA Wang H., Tang X., Liu J., Trautmann S., Balasundaram D., McCollum D.,
RA Balasubramanian M.K.;
RT "The multiprotein exocyst complex is essential for cell separation in
RT Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 13:515-529(2002).
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [4]
RP FUNCTION.
RX PubMed=12930742; DOI=10.1093/genetics/164.4.1323;
RA Wang H., Tang X., Balasubramanian M.K.;
RT "Rho3p regulates cell separation by modulating exocyst function in
RT Schizosaccharomyces pombe.";
RL Genetics 164:1323-1331(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16141239; DOI=10.1242/jcs.02530;
RA Gachet Y., Hyams J.S.;
RT "Endocytosis in fission yeast is spatially associated with the actin
RT cytoskeleton during polarised cell growth and cytokinesis.";
RL J. Cell Sci. 118:4231-4242(2005).
RN [6]
RP FUNCTION.
RX PubMed=16079182; DOI=10.1091/mbc.e04-12-1114;
RA Martin-Cuadrado A.B., Morrell J.L., Konomi M., An H., Petit C.S., Osumi M.,
RA Balasubramanian M., Gould K.L., Del Rey F., Vazquez de Aldana C.R.;
RT "Role of septins and the exocyst complex in the function of hydrolytic
RT enzymes responsible for fission yeast cell separation.";
RL Mol. Biol. Cell 16:4867-4881(2005).
RN [7]
RP FUNCTION.
RX PubMed=16415366; DOI=10.1534/genetics.105.050955;
RA Jin Q.W., Zhou M., Bimbo A., Balasubramanian M.K., McCollum D.;
RT "A role for the septation initiation network in septum assembly revealed by
RT genetic analysis of sid2-250 suppressors.";
RL Genetics 172:2101-2112(2006).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-449 AND SER-450, 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 [10]
RP SUBCELLULAR LOCATION, AND FUNCTION OF THE EXOCYST COMPLEX.
RX PubMed=21148300; DOI=10.1091/mbc.e10-08-0720;
RA Bendezu F.O., Martin S.G.;
RT "Actin cables and the exocyst form two independent morphogenesis pathways
RT in the fission yeast.";
RL Mol. Biol. Cell 22:44-53(2011).
CC -!- FUNCTION: Component of the exocyst complex involved in the delivery of
CC secretory vesicles to the plasma membrane. Also required for polarized
CC cell growth and division septum assembly. The exocyst complex plays an
CC important role in the targeting of rho3, as well as the two main
CC hydrolases required for cell separation, eng1 and agn1, to the cell
CC wall surrounding the septum before cell separation begins.
CC {ECO:0000269|PubMed:11854409, ECO:0000269|PubMed:12930742,
CC ECO:0000269|PubMed:16079182, ECO:0000269|PubMed:16415366,
CC ECO:0000269|PubMed:21148300}.
CC -!- SUBUNIT: Component of the exocyst complex composed of sec3, sec5, sec6,
CC sec8, sec10, sec15 and exo70. {ECO:0000269|PubMed:11854409}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16141239,
CC ECO:0000269|PubMed:16823372}. Cell tip {ECO:0000269|PubMed:11854409}.
CC Cell septum {ECO:0000269|PubMed:11854409, ECO:0000269|PubMed:16823372}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:16141239}. Note=Associated with
CC the actinomyosin ring at the division site and at the cell tips.
CC {ECO:0000269|PubMed:11854409}.
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DR EMBL; CU329672; CAA20702.2; -; Genomic_DNA.
DR PIR; T41671; T41671.
DR RefSeq; NP_587846.2; NM_001022839.2.
DR AlphaFoldDB; O74562; -.
DR SMR; O74562; -.
DR BioGRID; 275972; 17.
DR STRING; 4896.SPCC970.09.1; -.
DR iPTMnet; O74562; -.
DR MaxQB; O74562; -.
DR PaxDb; O74562; -.
DR PRIDE; O74562; -.
DR EnsemblFungi; SPCC970.09.1; SPCC970.09.1:pep; SPCC970.09.
DR PomBase; SPCC970.09; sec8.
DR VEuPathDB; FungiDB:SPCC970.09; -.
DR eggNOG; KOG3691; Eukaryota.
DR HOGENOM; CLU_288715_0_0_1; -.
DR InParanoid; O74562; -.
DR OMA; SLPNWTD; -.
DR PRO; PR:O74562; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0090619; C:meiotic spindle pole; IDA:PomBase.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:PomBase.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IMP:PomBase.
DR GO; GO:0006887; P:exocytosis; IMP:PomBase.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:PomBase.
DR InterPro; IPR039682; Sec8/EXOC4.
DR InterPro; IPR007191; Sec8_exocyst_N.
DR PANTHER; PTHR14146; PTHR14146; 1.
DR Pfam; PF04048; Sec8_exocyst; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoplasmic vesicle; Exocytosis;
KW Phosphoprotein; Protein transport; Reference proteome; Septation;
KW Transport.
FT CHAIN 1..1073
FT /note="Exocyst complex component sec8"
FT /id="PRO_0000118941"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 449
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1073 AA; 122975 MW; F3476EBDBEF9A2CD CRC64;
MDTRGYSETK KGRYPVGKKS LESPNGYSNY GTSMDNELSS EYASRGMHIG DLENLVNEIE
DEWKDLGRED YQPISTALEL LDDSSFGRDY KSFLNVYDRI SAALQTIAHT HKDDFTRGIS
AYGEIMEGIQ KCNSRIIALK QSLEASQECI GNTNSKELQQ TLARSSQYKK VISVLKELNE
ANQLFDNFHT LVDSKQYYHA SDLIRRVWDE LSRSDFDGIL VVEQFKSRMT GLLSHLEDIL
SEELVSITFL KDAVAYPIVS YCSPNPLRET SNPYFLRDFL KNNANTSTLG QSEQLRYLEE
ALSLKLSDCL KMDYGRDSLR DIRIVLESLN LLGKLPNAIS SLKSRTSAEM FTTVDSTSRA
IVNKYSLGNN VSTVNPFSKS LYDIGLHAET DREHTMISEF LTNLFTKLRC VLMHYRGISE
FMTKLETKTP KHASSSHKSS IMSVNSDPTS PKVSKFDTSD STFPFDTLLQ AFESEIRLML
KDYLISKEEY IENSGNFVVG TEMSIYNLPG ENEEDKLFDV TNEIAVENKS NAFYARINEL
VNEKAPELIL NKSNASVSTI ELFSGSSKEI VRLAGHVVFV GPSVFHASSV LPQTVFFLED
SVSILKNPNI PPQFAVNFMK EFLRGSYIPQ LYKFMSSHFD TIMKDVGAFQ LHRDWKIYSK
IPIFKCHVAI VQYFHDLQDY LPIVALNLVE FYELLHTLLV RFRNHCSDYL SDLCRTAVLK
EYKHVNEDTE DVDDTVRVKL LHDDVTYPQF IKFLKQKNPS LEGLNELCRM ENKRLLQYED
RAITSEVKLP VSVLSKDSDL VNSVSYLHNS MEWFLQRCFS RFMNGSRRMN VLQQNQANFG
GDFLPIDNLL GNNSDLMKGA YKEVFDSLQR LQFDALLLIR MEVRLQYIHS INQSVNLPDY
VVEYRGRPDA SIMALNSTIV TTNLKLETCL NEWERRFVFQ GLSELVDSSL YSIFYKIESM
NRGSCLQMLK NMSAMIQILK TVKEIHGDVE FPKSSRVFGI YQNGAKKIIE HFIAAPKKEL
LPDVKQMVRI YYQRLMKDAK RNGRDDLYRQ YQKKIGSVLT QFDNTVGGAR KNP
