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Protein

Rho guanine nucleotide exchange factor scd1

Gene

scd1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • Rho guanyl-nucleotide exchange factor activity Source: PomBase

GO - Biological processi

  • barrier septum assembly Source: UniProtKB-KW
  • Cdc42 protein signal transduction Source: PomBase
  • conjugation with cellular fusion Source: PomBase
  • positive regulation of conjugation with cellular fusion Source: PomBase
  • regulation of barrier septum assembly Source: PomBase
  • regulation of endocytosis Source: PomBase
  • regulation of establishment or maintenance of cell polarity regulating cell shape Source: PomBase
  • regulation of GTPase activity Source: PomBase
  • regulation of Rho protein signal transduction Source: InterPro
  • regulation of spindle elongation Source: PomBase
  • signal transduction involved in conjugation with cellular fusion Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Cell cycle, Cell division, Septation

Enzyme and pathway databases

ReactomeiR-SPO-194840. Rho GTPase cycle.
R-SPO-416482. G alpha (12/13) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho guanine nucleotide exchange factor scd1
Gene namesi
Name:scd1
Synonyms:ral1
ORF Names:SPAC16E8.09
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC16E8.09.
PomBaseiSPAC16E8.09. scd1.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Located at the growing cell ends and tips of conjugation tubes.

GO - Cellular componenti

  • Cdc42 GTPase complex Source: PomBase
  • cell cortex of cell tip Source: PomBase
  • cell cortex of growing cell tip Source: PomBase
  • cell division site Source: PomBase
  • cell tip Source: PomBase
  • cytosol Source: PomBase
  • intracellular Source: PomBase
  • mating projection tip Source: PomBase
  • mitotic spindle Source: PomBase
  • nucleus Source: PomBase
  • site of polarized growth Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 872872Rho guanine nucleotide exchange factor scd1PRO_0000080973Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei583 – 5831Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP40995.

PTM databases

iPTMnetiP40995.

Interactioni

Subunit structurei

Scd1, scd2, cdc42, and ras1, in its GTP-bound state, act cooperatively to form a protein complex. Interacts with moe1 and cdc42.2 Publications

Protein-protein interaction databases

BioGridi278803. 25 interactions.
DIPiDIP-44893N.
MINTiMINT-111336.

Structurei

3D structure databases

ProteinModelPortaliP40995.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini228 – 402175DHPROSITE-ProRule annotationAdd
BLAST
Domaini426 – 547122PHPROSITE-ProRule annotationAdd
BLAST
Domaini772 – 85988PB1PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi559 – 667109Ser/Thr-richAdd
BLAST

Sequence similaritiesi

Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PB1 domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiP40995.
KOiK11236.
OMAiFIVACRN.
OrthoDBiEOG77DJF5.
PhylomeDBiP40995.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR033511. Cdc24/Scd1.
IPR010481. Cdc24/Scd1_N.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR000270. PB1_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR22826:SF133. PTHR22826:SF133. 2 hits.
PfamiPF06395. CDC24. 1 hit.
PF00564. PB1. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00666. PB1. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS51745. PB1. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40995-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYFQDRKTS SRSLPSYINH STQNLVGPRK DETNLSEYMK LRLLQSPSQV
60 70 80 90 100
IYNLENTVSL YRRCLNLRKR LMDISELAAF FDSIHREALN SSFKILEFKD
110 120 130 140 150
IEFDDPVTEI WLFCRLGYPL CALFNCLPVK QKLEVNSSVS LENTNVCKAS
160 170 180 190 200
LYRFMLMCKN ELGLTDAALF SISEIYKPST APLVRALQTI ELLLKKYEVS
210 220 230 240 250
NTTKSSSTPS PSTDDNVPTG TLNSLIASGR RVTAELYETE LKYIQDLEYL
260 270 280 290 300
SNYMVILQQK QILSQDTILS IFTNLNEILD FQRRFLVGLE MNLSLPVEEQ
310 320 330 340 350
RLGALFIALE EGFSVYQVFC TNFPNAQQLI IDNQNQLLKV ANLLEPSYEL
360 370 380 390 400
PALLIKPIQR ICKYPLLLNQ LLKGTPSGYQ YEEELKQGMA CVVRVANQVN
410 420 430 440 450
ETRRIHENRN AIIELEQRVI DWKGYSLQYF GQLLVWDVVN VCKADIEREY
460 470 480 490 500
HVYLFEKILL CCKEMSTLKR QARSISMNKK TKRLDSLQLK GRILTSNITT
510 520 530 540 550
VVPNHHMGSY AIQIFWRGDP QHESFILKLR NEESHKLWMS VLNRLLWKNE
560 570 580 590 600
HGSPKDIRSA ASTPANPVYN RSSSQTSKGY NSSDYDLLRT HSLDENVNSP
610 620 630 640 650
TSISSPSSKS SPFTKTTSKD TKSATTTDER PSDFIRLNSE ESVGTSSLRT
660 670 680 690 700
SQTTSTIVSN DSSSTASIPS QISRISQVNS LLNDYNYNRQ SHITRVYSGT
710 720 730 740 750
DDGSSVSIFE DTSSSTKQKI FDQPTTNDCD VMRPRQYSYS AGMKSDGSLL
760 770 780 790 800
PSTKHTSLSS SSTSTSLSVR NTTNVKIRLR LHEVSLVLVV AHDITFDELL
810 820 830 840 850
AKVEHKIKLC GILKQAVPFR VRLKYVDEDG DFITITSDED VLMAFETCTF
860 870
ELMDPVHNKG MDTVSLHVVV YF
Length:872
Mass (Da):99,102
Last modified:December 15, 1998 - v2
Checksum:i726FAE33B519D69D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12538 Genomic DNA. Translation: AAA50556.2.
CU329670 Genomic DNA. Translation: CAB11037.1.
PIRiT37789.
RefSeqiNP_594221.1. NM_001019644.2.

Genome annotation databases

EnsemblFungiiSPAC16E8.09.1; SPAC16E8.09.1:pep; SPAC16E8.09.
GeneIDi2542337.
KEGGispo:SPAC16E8.09.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12538 Genomic DNA. Translation: AAA50556.2.
CU329670 Genomic DNA. Translation: CAB11037.1.
PIRiT37789.
RefSeqiNP_594221.1. NM_001019644.2.

3D structure databases

ProteinModelPortaliP40995.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278803. 25 interactions.
DIPiDIP-44893N.
MINTiMINT-111336.

PTM databases

iPTMnetiP40995.

Proteomic databases

MaxQBiP40995.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC16E8.09.1; SPAC16E8.09.1:pep; SPAC16E8.09.
GeneIDi2542337.
KEGGispo:SPAC16E8.09.

Organism-specific databases

EuPathDBiFungiDB:SPAC16E8.09.
PomBaseiSPAC16E8.09. scd1.

Phylogenomic databases

InParanoidiP40995.
KOiK11236.
OMAiFIVACRN.
OrthoDBiEOG77DJF5.
PhylomeDBiP40995.

Enzyme and pathway databases

ReactomeiR-SPO-194840. Rho GTPase cycle.
R-SPO-416482. G alpha (12/13) signalling events.

Miscellaneous databases

PROiP40995.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR033511. Cdc24/Scd1.
IPR010481. Cdc24/Scd1_N.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR000270. PB1_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR22826:SF133. PTHR22826:SF133. 2 hits.
PfamiPF06395. CDC24. 1 hit.
PF00564. PB1. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTiSM00666. PB1. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50729. SSF50729. 1 hit.
PROSITEiPS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS51745. PB1. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cooperative interaction of S. pombe proteins required for mating and morphogenesis."
    Chang E.C., Barr M., Wang Y., Jung V., Xu H.-P., Wigler M.H.
    Cell 79:131-141(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SP870.
  2. "The genome sequence of Schizosaccharomyces pombe."
    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.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Moe1, a conserved protein in Schizosaccharomyces pombe, interacts with a Ras effector, Scd1, to affect proper spindle formation."
    Chen C.-R., Li Y.-C., Chen J., Hou M.-C., Papadaki P., Chang E.C.
    Proc. Natl. Acad. Sci. U.S.A. 96:517-522(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MOE1, SUBCELLULAR LOCATION.
  4. "Gef1p and Scd1p, the Two GDP-GTP exchange factors for Cdc42p, form a ring structure that shrinks during cytokinesis in Schizosaccharomyces pombe."
    Hirota K., Tanaka K., Ohta K., Yamamoto M.
    Mol. Biol. Cell 14:3617-3627(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDC42, SUBCELLULAR LOCATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSCD1_SCHPO
AccessioniPrimary (citable) accession number: P40995
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: December 15, 1998
Last modified: July 6, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.