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Septation protein 7 (Seventh homolog of septin 1)

 SHS1_CANAL              Reviewed;         670 AA.
Q59VX8; A0A1D8PCP5;
13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
22-NOV-2017, entry version 84.
RecName: Full=Septation protein 7;
AltName: Full=Seventh homolog of septin 1;
Name=SEP7; Synonyms=SHS1; OrderedLocusNames=CAALFM_C102230WA;
ORFNames=CaO19.11164, CaO19.3680;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[2]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[4]
IDENTIFICATION.
PubMed=12181342; DOI=10.1091/mbc.E02-01-0013;
Warenda A.J., Konopka J.B.;
"Septin function in Candida albicans morphogenesis.";
Mol. Biol. Cell 13:2732-2746(2002).
[5]
DISRUPTION PHENOTYPE.
PubMed=12819094; DOI=10.1128/IAI.71.7.4045-4051.2003;
Warenda A.J., Kauffman S., Sherrill T.P., Becker J.M., Konopka J.B.;
"Candida albicans septin mutants are defective for invasive growth and
virulence.";
Infect. Immun. 71:4045-4051(2003).
[6]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SEPTIN
COMPLEX.
PubMed=15449307; DOI=10.1002/yea.1147;
Kaneko A., Umeyama T., Hanaoka N., Monk B.C., Uehara Y., Niimi M.;
"Tandem affinity purification of the Candida albicans septin protein
complex.";
Yeast 21:1025-1033(2004).
[7]
SUBCELLULAR LOCATION, FUNCTION, AND PHOSPHORYLATION.
PubMed=18234840; DOI=10.1091/mbc.E07-09-0876;
Gonzalez-Novo A., Correa-Bordes J., Labrador L., Sanchez M.,
Vazquez de Aldana C.R., Jimenez J.;
"Sep7 is essential to modify septin ring dynamics and inhibit cell
separation during Candida albicans hyphal growth.";
Mol. Biol. Cell 19:1509-1518(2008).
[8]
SUBCELLULAR LOCATION.
PubMed=22687514; DOI=10.1128/AAC.00112-12;
Badrane H., Nguyen M.H., Blankenship J.R., Cheng S., Hao B.,
Mitchell A.P., Clancy C.J.;
"Rapid redistribution of phosphatidylinositol-(4,5)-bisphosphate and
septins during the Candida albicans response to caspofungin.";
Antimicrob. Agents Chemother. 56:4614-4624(2012).
[9]
INTERACTION WITH GIN4, AND PHOSPHORYLATION.
PubMed=22366454; DOI=10.1242/jcs.104497;
Li C.R., Yong J.Y., Wang Y.M., Wang Y.;
"CDK regulates septin organization through cell-cycle-dependent
phosphorylation of the Nim1-related kinase Gin4.";
J. Cell Sci. 125:2533-2543(2012).
-!- FUNCTION: Septins are GTPases involved in cytokinesis that
assemble early in the cell cycle as a patch at the incipient bud
site and form a ring before bud emergence, which transforms into
an hour-glass shaped collar of cortical filaments that spans both
sides of the mother-bud neck. This collar persists until just
before cytokinesis, when it splits into two rings that occupy
opposite sides of the neck. The septins at the bud neck serve as a
structural scaffold that recruits different components involved in
diverse processes at specific stages during the cell cycle. Many
proteins bind asymmetrically to the septin collar. The septin
assembly is regulated by protein kinase GIN4. Septins are also
involved in cell morphogenesis, chlamydospores morphogenesis, bud
site selection, chitin deposition, cell cycle regulation, cell
compartmentalization and spore wall formation. SEP7 is required to
convert hyphal septin rings into the hyphal-specific state and is
necessary for CDC10 turnover during hyphal growth.
{ECO:0000269|PubMed:18234840}.
-!- SUBUNIT: Component of the septin complex which consists of CDC3,
CDC10, CDC11, CDC12 and probably SEP7. The purified septin complex
appeared to have a stoichiometry of 2 CDC3, 1 to 2 CDC10, 1 CDC11,
2 CDC12, and 1 or none SEP7 subunit. Induction of hyphal growth
brings about important modifications in septin ring dynamics,
because the rings were found in a different state from those of
yeast cells. This hyphal-specific state contains a core of stable
septins (SEP7, CDC3, and CDC12), and it shows a high CDC10
turnover between the ring and the cytoplasm. Interacts with GIN4.
{ECO:0000269|PubMed:15449307, ECO:0000269|PubMed:22366454}.
-!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:18234840,
ECO:0000269|PubMed:22687514}. Note=Present at the bud neck during
cell division.
-!- PTM: Phosphorylated by GIN4 which stabilizes the GIN4-SEP7
interaction. {ECO:0000269|PubMed:18234840,
ECO:0000269|PubMed:22366454}.
-!- DISRUPTION PHENOTYPE: Leads to a minor reduction in agar invasion
ability. {ECO:0000269|PubMed:12819094}.
-!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-
like GTPase superfamily. Septin GTPase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP017623; AOW25908.1; -; Genomic_DNA.
RefSeq; XP_713774.1; XM_708681.2.
ProteinModelPortal; Q59VX8; -.
SMR; Q59VX8; -.
BioGrid; 1227690; 1.
PRIDE; Q59VX8; -.
EnsemblFungi; AOW25908; AOW25908; CAALFM_C102230WA.
GeneID; 3644596; -.
KEGG; cal:CAALFM_C102230WA; -.
CGD; CAL0000186883; SEP7.
InParanoid; Q59VX8; -.
KO; K16946; -.
OrthoDB; EOG092C3HL6; -.
PRO; PR:Q59VX8; -.
Proteomes; UP000000559; Chromosome 1.
GO; GO:0030428; C:cell septum; IDA:CGD.
GO; GO:0005935; C:cellular bud neck; IDA:CGD.
GO; GO:0005940; C:septin ring; IDA:CGD.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0030448; P:hyphal growth; IMP:CGD.
CDD; cd01850; CDC_Septin; 1.
InterPro; IPR030379; G_SEPTIN_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR016491; Septin.
InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
Pfam; PF00735; Septin; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51719; G_SEPTIN; 1.
PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Coiled coil; Complete proteome;
GTP-binding; Hydrolase; Nucleotide-binding; Phosphoprotein;
Reference proteome.
CHAIN 1 670 Septation protein 7.
/FTId=PRO_0000424366.
DOMAIN 33 357 Septin-type G.
NP_BIND 43 50 GTP. {ECO:0000250}.
NP_BIND 217 225 GTP. {ECO:0000250}.
COILED 472 606 {ECO:0000255}.
COMPBIAS 395 404 Poly-Asn.
COMPBIAS 494 500 Poly-Asn.
COMPBIAS 612 619 Poly-Asn.
BINDING 137 137 GTP; via amide nitrogen. {ECO:0000250}.
BINDING 306 306 GTP. {ECO:0000250}.
SEQUENCE 670 AA; 75795 MW; 4BE314EF04244B25 CRC64;
MSRFDYRNTS KNTSVVDPDH SSPIINYRKD AKKGIKFTFM VVGESGTGKT TFINSLLNKK
VLNHRYEKLS PTVGDTKTLM FTSAKSVALP NTSILTKNEF NPRTINEEPG IALTETHIEI
IDDDNQKLLL NIIDTPGFGE NLNNELCFIE IENYLKQQFD LVLAEETRIK RNPRFVDTRV
HVMLYFITPT GHGLREIDIQ CMKRLSKYVN IIPVIGKADS FTLNELQHFK QQIRIDIQKF
NVPTFQFDNS LNDYDEDEDY DLIQECKFLT NLQPFAVVTS EDVFEVREST TSTKGNNDKP
KIIRARKYPW GLVDINDTRY SDFPILKSVL LGSHLQDLKD LTHDFLYETY RTERLTKVTG
NGQAFDDEEN EDAEFHDTVE HQLNDSNRGV GGDDNNNNNN NNNNASTIPS MSNLAQLTTS
TNEHDASHID NNSITSTSSS IKKSTSMLID DHPSSSPKLK NISSFTSSTS TVSLEGGEKE
GGHHDRGANS TSTNNNNNNN AFKRLSIGPQ RNQLRQISET VPYVLRHERI LERQQKLEEM
EQASARELAN RAALLEKKAA QLKAKEKALR QLELNRQKQE ESATSSLHRK DSDISGSVQS
GGVDDGKSES TNNNNNNRNG YGYGHGHGHG QSHEYDNSEY HHDDSTPNYE TSRLQKDETL
TDLHSIVSNH


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