SHS1_CANAL
ID SHS1_CANAL Reviewed; 670 AA.
AC Q59VX8; A0A1D8PCP5;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Septation protein 7;
DE AltName: Full=Seventh homolog of septin 1;
GN Name=SEP7; Synonyms=SHS1; OrderedLocusNames=CAALFM_C102230WA;
GN ORFNames=CaO19.11164, CaO19.3680;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP IDENTIFICATION.
RX PubMed=12181342; DOI=10.1091/mbc.e02-01-0013;
RA Warenda A.J., Konopka J.B.;
RT "Septin function in Candida albicans morphogenesis.";
RL Mol. Biol. Cell 13:2732-2746(2002).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=12819094; DOI=10.1128/iai.71.7.4045-4051.2003;
RA Warenda A.J., Kauffman S., Sherrill T.P., Becker J.M., Konopka J.B.;
RT "Candida albicans septin mutants are defective for invasive growth and
RT virulence.";
RL Infect. Immun. 71:4045-4051(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SEPTIN
RP COMPLEX.
RX PubMed=15449307; DOI=10.1002/yea.1147;
RA Kaneko A., Umeyama T., Hanaoka N., Monk B.C., Uehara Y., Niimi M.;
RT "Tandem affinity purification of the Candida albicans septin protein
RT complex.";
RL Yeast 21:1025-1033(2004).
RN [7]
RP SUBCELLULAR LOCATION, FUNCTION, AND PHOSPHORYLATION.
RX PubMed=18234840; DOI=10.1091/mbc.e07-09-0876;
RA Gonzalez-Novo A., Correa-Bordes J., Labrador L., Sanchez M.,
RA Vazquez de Aldana C.R., Jimenez J.;
RT "Sep7 is essential to modify septin ring dynamics and inhibit cell
RT separation during Candida albicans hyphal growth.";
RL Mol. Biol. Cell 19:1509-1518(2008).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=22687514; DOI=10.1128/aac.00112-12;
RA Badrane H., Nguyen M.H., Blankenship J.R., Cheng S., Hao B., Mitchell A.P.,
RA Clancy C.J.;
RT "Rapid redistribution of phosphatidylinositol-(4,5)-bisphosphate and
RT septins during the Candida albicans response to caspofungin.";
RL Antimicrob. Agents Chemother. 56:4614-4624(2012).
RN [9]
RP INTERACTION WITH GIN4, AND PHOSPHORYLATION.
RX PubMed=22366454; DOI=10.1242/jcs.104497;
RA Li C.R., Yong J.Y., Wang Y.M., Wang Y.;
RT "CDK regulates septin organization through cell-cycle-dependent
RT phosphorylation of the Nim1-related kinase Gin4.";
RL J. Cell Sci. 125:2533-2543(2012).
CC -!- FUNCTION: Septins are GTPases involved in cytokinesis that assemble
CC early in the cell cycle as a patch at the incipient bud site and form a
CC ring before bud emergence, which transforms into an hour-glass shaped
CC collar of cortical filaments that spans both sides of the mother-bud
CC neck. This collar persists until just before cytokinesis, when it
CC splits into two rings that occupy opposite sides of the neck. The
CC septins at the bud neck serve as a structural scaffold that recruits
CC different components involved in diverse processes at specific stages
CC during the cell cycle. Many proteins bind asymmetrically to the septin
CC collar. The septin assembly is regulated by protein kinase GIN4.
CC Septins are also involved in cell morphogenesis, chlamydospores
CC morphogenesis, bud site selection, chitin deposition, cell cycle
CC regulation, cell compartmentalization and spore wall formation. SEP7 is
CC required to convert hyphal septin rings into the hyphal-specific state
CC and is necessary for CDC10 turnover during hyphal growth.
CC {ECO:0000269|PubMed:18234840}.
CC -!- SUBUNIT: Component of the septin complex which consists of CDC3, CDC10,
CC CDC11, CDC12 and probably SEP7. The purified septin complex appeared to
CC have a stoichiometry of 2 CDC3, 1 to 2 CDC10, 1 CDC11, 2 CDC12, and 1
CC or none SEP7 subunit. Induction of hyphal growth brings about important
CC modifications in septin ring dynamics, because the rings were found in
CC a different state from those of yeast cells. This hyphal-specific state
CC contains a core of stable septins (SEP7, CDC3, and CDC12), and it shows
CC a high CDC10 turnover between the ring and the cytoplasm. Interacts
CC with GIN4. {ECO:0000269|PubMed:15449307, ECO:0000269|PubMed:22366454}.
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:18234840,
CC ECO:0000269|PubMed:22687514}. Note=Present at the bud neck during cell
CC division.
CC -!- PTM: Phosphorylated by GIN4 which stabilizes the GIN4-SEP7 interaction.
CC {ECO:0000269|PubMed:18234840, ECO:0000269|PubMed:22366454}.
CC -!- DISRUPTION PHENOTYPE: Leads to a minor reduction in agar invasion
CC ability. {ECO:0000269|PubMed:12819094}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
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DR EMBL; CP017623; AOW25908.1; -; Genomic_DNA.
DR RefSeq; XP_713774.1; XM_708681.2.
DR AlphaFoldDB; Q59VX8; -.
DR SMR; Q59VX8; -.
DR BioGRID; 1227690; 7.
DR STRING; 237561.Q59VX8; -.
DR PRIDE; Q59VX8; -.
DR GeneID; 3644596; -.
DR KEGG; cal:CAALFM_C102230WA; -.
DR CGD; CAL0000186883; SEP7.
DR VEuPathDB; FungiDB:C1_02230W_A; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_7_4_1; -.
DR InParanoid; Q59VX8; -.
DR OrthoDB; 845354at2759; -.
DR PRO; PR:Q59VX8; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0030428; C:cell septum; IDA:CGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:CGD.
DR GO; GO:1990317; C:Gin4 complex; IEA:EnsemblFungi.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0031105; C:septin complex; IBA:GO_Central.
DR GO; GO:0005940; C:septin ring; IDA:CGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:EnsemblFungi.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IBA:GO_Central.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IBA:GO_Central.
DR GO; GO:0061163; P:endoplasmic reticulum polarization; IEA:EnsemblFungi.
DR GO; GO:0010458; P:exit from mitosis; IEA:EnsemblFungi.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR GO; GO:0000280; P:nuclear division; IGI:CGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:EnsemblFungi.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0097271; P:protein localization to bud neck; IBA:GO_Central.
DR GO; GO:0000921; P:septin ring assembly; IEA:EnsemblFungi.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR Pfam; PF00735; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; GTP-binding; Hydrolase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..670
FT /note="Septation protein 7"
FT /id="PRO_0000424366"
FT DOMAIN 33..357
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 43..50
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 134..137
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 216..219
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 383..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 472..606
FT /evidence="ECO:0000255"
FT COMPBIAS 384..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 217..225
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ 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
