SCD1_SCHPO
ID SCD1_SCHPO Reviewed; 872 AA.
AC P40995;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Rho guanine nucleotide exchange factor scd1;
GN Name=scd1; Synonyms=ral1; ORFNames=SPAC16E8.09;
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].
RC STRAIN=SP870;
RX PubMed=7923372; DOI=10.1016/0092-8674(94)90406-5;
RA Chang E.C., Barr M., Wang Y., Jung V., Xu H.-P., Wigler M.H.;
RT "Cooperative interaction of S. pombe proteins required for mating and
RT morphogenesis.";
RL Cell 79:131-141(1994).
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 INTERACTION WITH MOE1, AND SUBCELLULAR LOCATION.
RX PubMed=9892665; DOI=10.1073/pnas.96.2.517;
RA Chen C.-R., Li Y.-C., Chen J., Hou M.-C., Papadaki P., Chang E.C.;
RT "Moe1, a conserved protein in Schizosaccharomyces pombe, interacts with a
RT Ras effector, Scd1, to affect proper spindle formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:517-522(1999).
RN [4]
RP FUNCTION, INTERACTION WITH CDC42, AND SUBCELLULAR LOCATION.
RX PubMed=12972551; DOI=10.1091/mbc.e02-10-0665;
RA Hirota K., Tanaka K., Ohta K., Yamamoto M.;
RT "Gef1p and Scd1p, the Two GDP-GTP exchange factors for Cdc42p, form a ring
RT structure that shrinks during cytokinesis in Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 14:3617-3627(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND IDENTIFICATION BY
RP 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: Required for mating and morphogenesis. May contain a cryptic
CC binding site for cdc42 that is enhanced by binding Ras. Interacts
CC directly with scd2. Promotes the exchange of cdc42-bound GDP by GTP.
CC Involved in septation and stimulates the elongation of conjugation
CC tubes. {ECO:0000269|PubMed:12972551}.
CC -!- SUBUNIT: Scd1, scd2, cdc42, and ras1, in its GTP-bound state, act
CC cooperatively to form a protein complex. Interacts with moe1 and cdc42.
CC {ECO:0000269|PubMed:12972551, ECO:0000269|PubMed:9892665}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Located at the growing
CC cell ends and tips of conjugation tubes.
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DR EMBL; U12538; AAA50556.2; -; Genomic_DNA.
DR EMBL; CU329670; CAB11037.1; -; Genomic_DNA.
DR PIR; T37789; T37789.
DR RefSeq; NP_594221.1; NM_001019644.2.
DR AlphaFoldDB; P40995; -.
DR SMR; P40995; -.
DR BioGRID; 278803; 27.
DR DIP; DIP-44893N; -.
DR IntAct; P40995; 1.
DR STRING; 4896.SPAC16E8.09.1; -.
DR iPTMnet; P40995; -.
DR MaxQB; P40995; -.
DR PaxDb; P40995; -.
DR PRIDE; P40995; -.
DR EnsemblFungi; SPAC16E8.09.1; SPAC16E8.09.1:pep; SPAC16E8.09.
DR GeneID; 2542337; -.
DR KEGG; spo:SPAC16E8.09; -.
DR PomBase; SPAC16E8.09; scd1.
DR VEuPathDB; FungiDB:SPAC16E8.09; -.
DR eggNOG; KOG3519; Eukaryota.
DR HOGENOM; CLU_007879_0_0_1; -.
DR InParanoid; P40995; -.
DR OMA; LMAFETC; -.
DR PhylomeDB; P40995; -.
DR PRO; PR:P40995; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0071521; C:Cdc42 GTPase complex; TAS:PomBase.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:1902716; C:cell cortex of growing 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:0032154; C:cleavage furrow; IDA:PomBase.
DR GO; GO:0090726; C:cortical dynamic polarity patch; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0043332; C:mating projection tip; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0031520; C:plasma membrane of cell tip; EXP:PomBase.
DR GO; GO:0030427; C:site of polarized growth; IDA:PomBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:PomBase.
DR GO; GO:0008289; F:lipid binding; ISM:PomBase.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0030010; P:establishment of cell polarity; IBA:GO_Central.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:1902917; P:positive regulation of mating projection assembly; IMP:PomBase.
DR GO; GO:0140281; P:positive regulation of mitotic division septum assembly; IMP:PomBase.
DR GO; GO:0031137; P:regulation of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0032955; P:regulation of division septum assembly; IGI:PomBase.
DR GO; GO:0030100; P:regulation of endocytosis; IMP:PomBase.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:PomBase.
DR GO; GO:0031106; P:septin ring organization; IBA:GO_Central.
DR CDD; cd13246; PH_Scd1; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010481; Cdc24/Scd1_N.
DR InterPro; IPR033511; Cdc24/Scd1_PH_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR000270; PB1_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF06395; CDC24; 1.
DR Pfam; PF00564; PB1; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00666; PB1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS51745; PB1; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Guanine-nucleotide releasing factor;
KW Nucleus; Phosphoprotein; Reference proteome; Septation.
FT CHAIN 1..872
FT /note="Rho guanine nucleotide exchange factor scd1"
FT /id="PRO_0000080973"
FT DOMAIN 82..198
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 228..402
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 426..547
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 772..859
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ 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
