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Rho guanine nucleotide exchange factor scd1

 SCD1_SCHPO              Reviewed;         872 AA.
P40995;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
15-DEC-1998, sequence version 2.
22-NOV-2017, entry version 143.
RecName: Full=Rho guanine nucleotide exchange factor scd1;
Name=scd1; Synonyms=ral1; ORFNames=SPAC16E8.09;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=SP870;
PubMed=7923372; DOI=10.1016/0092-8674(94)90406-5;
Chang E.C., Barr M., Wang Y., Jung V., Xu H.-P., Wigler M.H.;
"Cooperative interaction of S. pombe proteins required for mating and
morphogenesis.";
Cell 79:131-141(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
INTERACTION WITH MOE1, AND SUBCELLULAR LOCATION.
PubMed=9892665; DOI=10.1073/pnas.96.2.517;
Chen C.-R., Li Y.-C., Chen J., Hou M.-C., Papadaki P., Chang E.C.;
"Moe1, a conserved protein in Schizosaccharomyces pombe, interacts
with a Ras effector, Scd1, to affect proper spindle formation.";
Proc. Natl. Acad. Sci. U.S.A. 96:517-522(1999).
[4]
FUNCTION, INTERACTION WITH CDC42, AND SUBCELLULAR LOCATION.
PubMed=12972551; DOI=10.1091/mbc.E02-10-0665;
Hirota K., Tanaka K., Ohta K., Yamamoto M.;
"Gef1p and Scd1p, the Two GDP-GTP exchange factors for Cdc42p, form a
ring structure that shrinks during cytokinesis in Schizosaccharomyces
pombe.";
Mol. Biol. Cell 14:3617-3627(2003).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
-!- FUNCTION: Required for mating and morphogenesis. May contain a
cryptic binding site for cdc42 that is enhanced by binding Ras.
Interacts directly with scd2. Promotes the exchange of cdc42-bound
GDP by GTP. Involved in septation and stimulates the elongation of
conjugation tubes. {ECO:0000269|PubMed:12972551}.
-!- SUBUNIT: Scd1, scd2, cdc42, and ras1, in its GTP-bound state, act
cooperatively to form a protein complex. Interacts with moe1 and
cdc42. {ECO:0000269|PubMed:12972551, ECO:0000269|PubMed:9892665}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Located at the
growing cell ends and tips of conjugation tubes.
-----------------------------------------------------------------------
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EMBL; U12538; AAA50556.2; -; Genomic_DNA.
EMBL; CU329670; CAB11037.1; -; Genomic_DNA.
PIR; T37789; T37789.
RefSeq; NP_594221.1; NM_001019644.2.
ProteinModelPortal; P40995; -.
SMR; P40995; -.
BioGrid; 278803; 25.
DIP; DIP-44893N; -.
IntAct; P40995; 1.
MINT; MINT-111336; -.
STRING; 4896.SPAC16E8.09.1; -.
iPTMnet; P40995; -.
MaxQB; P40995; -.
PRIDE; P40995; -.
EnsemblFungi; SPAC16E8.09.1; SPAC16E8.09.1:pep; SPAC16E8.09.
GeneID; 2542337; -.
KEGG; spo:SPAC16E8.09; -.
EuPathDB; FungiDB:SPAC16E8.09; -.
PomBase; SPAC16E8.09; scd1.
InParanoid; P40995; -.
KO; K11236; -.
OMA; ANQVNEA; -.
OrthoDB; EOG092C2MTU; -.
PhylomeDB; P40995; -.
Reactome; R-SPO-194840; Rho GTPase cycle.
Reactome; R-SPO-416482; G alpha (12/13) signalling events.
PRO; PR:P40995; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0071521; C:Cdc42 GTPase complex; TAS:PomBase.
GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
GO; GO:1902716; C:cell cortex of growing cell tip; IDA:PomBase.
GO; GO:0032153; C:cell division site; IDA:PomBase.
GO; GO:0051286; C:cell tip; IDA:PomBase.
GO; GO:0032154; C:cleavage furrow; IDA:PomBase.
GO; GO:0090726; C:cortical dynamic polarity patch; IDA:PomBase.
GO; GO:0005829; C:cytosol; IDA:PomBase.
GO; GO:0000935; C:division septum; IDA:PomBase.
GO; GO:0043332; C:mating projection tip; IDA:PomBase.
GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
GO; GO:0005634; C:nucleus; IDA:PomBase.
GO; GO:0030427; C:site of polarized growth; IDA:PomBase.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:PomBase.
GO; GO:0032488; P:Cdc42 protein signal transduction; IC:PomBase.
GO; GO:0000747; P:conjugation with cellular fusion; IMP:PomBase.
GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
GO; GO:0031139; P:positive regulation of conjugation with cellular fusion; IMP:PomBase.
GO; GO:1902432; P:protein localization to division septum; IMP:PomBase.
GO; GO:1901891; P:regulation of cell septum assembly; IMP:PomBase.
GO; GO:0032955; P:regulation of division septum assembly; IGI:PomBase.
GO; GO:0030100; P:regulation of endocytosis; IMP:PomBase.
GO; GO:2000769; P:regulation of establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:PomBase.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
GO; GO:0032005; P:signal transduction involved in conjugation with cellular fusion; IMP:PomBase.
CDD; cd13246; PH_Scd1; 1.
CDD; cd00160; RhoGEF; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR010481; Cdc24/Scd1_N.
InterPro; IPR033511; Cdc24/Scd1_PH_dom.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR001331; GDS_CDC24_CS.
InterPro; IPR000270; PB1_dom.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
Pfam; PF06395; CDC24; 1.
Pfam; PF00564; PB1; 1.
Pfam; PF00621; RhoGEF; 1.
SMART; SM00666; PB1; 1.
SMART; SM00233; PH; 1.
SMART; SM00325; RhoGEF; 1.
SUPFAM; SSF48065; SSF48065; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50021; CH; 1.
PROSITE; PS00741; DH_1; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS51745; PB1; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Complete proteome; Cytoplasm;
Guanine-nucleotide releasing factor; Nucleus; Phosphoprotein;
Reference proteome; Septation.
CHAIN 1 872 Rho guanine nucleotide exchange factor
scd1.
/FTId=PRO_0000080973.
DOMAIN 82 198 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 228 402 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 426 547 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 772 859 PB1. {ECO:0000255|PROSITE-
ProRule:PRU01081}.
COMPBIAS 559 667 Ser/Thr-rich.
MOD_RES 583 583 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
SEQUENCE 872 AA; 99102 MW; 726FAE33B519D69D CRC64;
MAYFQDRKTS SRSLPSYINH STQNLVGPRK DETNLSEYMK LRLLQSPSQV IYNLENTVSL
YRRCLNLRKR LMDISELAAF FDSIHREALN SSFKILEFKD IEFDDPVTEI WLFCRLGYPL
CALFNCLPVK QKLEVNSSVS LENTNVCKAS LYRFMLMCKN ELGLTDAALF SISEIYKPST
APLVRALQTI ELLLKKYEVS NTTKSSSTPS PSTDDNVPTG TLNSLIASGR RVTAELYETE
LKYIQDLEYL SNYMVILQQK QILSQDTILS IFTNLNEILD FQRRFLVGLE MNLSLPVEEQ
RLGALFIALE EGFSVYQVFC TNFPNAQQLI IDNQNQLLKV ANLLEPSYEL PALLIKPIQR
ICKYPLLLNQ LLKGTPSGYQ YEEELKQGMA CVVRVANQVN ETRRIHENRN AIIELEQRVI
DWKGYSLQYF GQLLVWDVVN VCKADIEREY HVYLFEKILL CCKEMSTLKR QARSISMNKK
TKRLDSLQLK GRILTSNITT VVPNHHMGSY AIQIFWRGDP QHESFILKLR NEESHKLWMS
VLNRLLWKNE HGSPKDIRSA ASTPANPVYN RSSSQTSKGY NSSDYDLLRT HSLDENVNSP
TSISSPSSKS SPFTKTTSKD TKSATTTDER PSDFIRLNSE ESVGTSSLRT SQTTSTIVSN
DSSSTASIPS QISRISQVNS LLNDYNYNRQ SHITRVYSGT DDGSSVSIFE DTSSSTKQKI
FDQPTTNDCD VMRPRQYSYS AGMKSDGSLL PSTKHTSLSS SSTSTSLSVR NTTNVKIRLR
LHEVSLVLVV AHDITFDELL AKVEHKIKLC GILKQAVPFR VRLKYVDEDG DFITITSDED
VLMAFETCTF ELMDPVHNKG MDTVSLHVVV YF


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