BUD2_CANAL
ID BUD2_CANAL Reviewed; 1237 AA.
AC Q5A506; A0A1D8PMX4;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=GTPase activating protein BUD2;
DE AltName: Full=Bud site selection protein 2;
GN Name=BUD2; OrderedLocusNames=CAALFM_C500490CA;
GN ORFNames=CaO19.8555, CaO19.940;
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 INDUCTION.
RX PubMed=15387822; DOI=10.1111/j.1365-2958.2004.04214.x;
RA Lan C.Y., Rodarte G., Murillo L.A., Jones T., Davis R.W., Dungan J.,
RA Newport G., Agabian N.;
RT "Regulatory networks affected by iron availability in Candida albicans.";
RL Mol. Microbiol. 53:1451-1469(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16002653; DOI=10.1128/ec.4.7.1273-1286.2005;
RA Hausauer D.L., Gerami-Nejad M., Kistler-Anderson C., Gale C.A.;
RT "Hyphal guidance and invasive growth in Candida albicans require the Ras-
RT like GTPase Rsr1p and its GTPase-activating protein Bud2p.";
RL Eukaryot. Cell 4:1273-1286(2005).
RN [6]
RP FUNCTION.
RX PubMed=21407800; DOI=10.1371/journal.pone.0017046;
RA Wachtler B., Wilson D., Haedicke K., Dalle F., Hube B.;
RT "From attachment to damage: defined genes of Candida albicans mediate
RT adhesion, invasion and damage during interaction with oral epithelial
RT cells.";
RL PLoS ONE 6:E17046-E17046(2011).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23223038; DOI=10.1128/ec.00294-12;
RA Pulver R., Heisel T., Gonia S., Robins R., Norton J., Haynes P., Gale C.A.;
RT "Rsr1 focuses Cdc42 activity at hyphal tips and promotes maintenance of
RT hyphal development in Candida albicans.";
RL Eukaryot. Cell 12:482-495(2013).
CC -!- FUNCTION: GTPase activating protein (GAP) for RSR1 which is involved in
CC the polarization of yeast and hyphal cells. Directs the site of new
CC daughter cell growth in yeast and hyphal cells. Important for hyphae to
CC maintain linear growth and necessary for hyphal responses to
CC directional cues in the environment (tropisms). Required for correct
CC localization of the septin rings and stabilization of the polarisome at
CC hyphal tips. Involved in cell adhesion. {ECO:0000269|PubMed:16002653,
CC ECO:0000269|PubMed:21407800, ECO:0000269|PubMed:23223038}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cell tip. Cell septum.
CC Note=Enriched just behind the apices of hyphal tips, appearing as a
CC faint ring at the membrane with a relatively reduced intensity at the
CC extreme tip. Also enriched in the concave angle of some curved hyphae
CC and shows discrete localization to septa.
CC -!- INDUCTION: Expression is increased in low iron conditions.
CC {ECO:0000269|PubMed:15387822}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017627; AOW29493.1; -; Genomic_DNA.
DR RefSeq; XP_716779.1; XM_711686.1.
DR AlphaFoldDB; Q5A506; -.
DR STRING; 237561.Q5A506; -.
DR PRIDE; Q5A506; -.
DR GeneID; 3641541; -.
DR KEGG; cal:CAALFM_C500490CA; -.
DR CGD; CAL0000199838; BUD2.
DR VEuPathDB; FungiDB:C5_00490C_A; -.
DR eggNOG; KOG3508; Eukaryota.
DR HOGENOM; CLU_002973_1_0_1; -.
DR InParanoid; Q5A506; -.
DR OMA; WFVGLNY; -.
DR OrthoDB; 145372at2759; -.
DR PRO; PR:Q5A506; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0005935; C:cellular bud neck; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0001411; C:hyphal tip; IDA:CGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:CGD.
DR GO; GO:0005096; F:GTPase activator activity; IMP:CGD.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:CGD.
DR GO; GO:0007015; P:actin filament organization; IMP:CGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0000282; P:cellular bud site selection; IMP:CGD.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IMP:CGD.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR GO; GO:0030011; P:maintenance of cell polarity; IMP:CGD.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IMP:CGD.
DR GO; GO:0009652; P:thigmotropism; IMP:CGD.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194; PTHR10194; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00616; RasGAP; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Coiled coil; Cytoplasm; GTPase activation;
KW Reference proteome; Virulence.
FT CHAIN 1..1237
FT /note="GTPase activating protein BUD2"
FT /id="PRO_0000422801"
FT DOMAIN 381..503
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 592..872
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT REGION 79..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1065..1093
FT /evidence="ECO:0000255"
FT COMPBIAS 79..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..752
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1237 AA; 142287 MW; 80812A1981DE6240 CRC64;
MPPAYQSAFH KIISRDKGVF EGHNFLVSVD TINWIHVNTL TITEQGQLFS SDSKDNHYLL
LQSLQSCFIQ IYPDSNISGS GKSSISQPPP TTSTRRNLLR KSSNLNSSDQ SHSKSSEDNE
HQPPAILIKT FDNDKLYIRI PSKANFGNLL SCLMVWQNLK PQGLAKKWYC ENKVIEGFNP
NAPIYELLVC RFKIYGPLPN KYKNLNIVPG PKAPVYQQKM DDFKANFDNS YIITPQISSD
NHNSINEGWF YAMGALNSHG ILNFISELDG TLLYSIDIKQ ILSSEIREMH NSIFNSSNIL
FIGQLKELRY NNVIRTLSTL TPDQLLTPFL TRDGKIIPNN QRILIEFPLH IDLEDWFVGL
NYFAKREYIG SFDNESKLIH NVEHPQLYDF SKANFRVSKK MSIDIIEAKF ENTETNKSGK
IYAEVRMWGF PWSRTAIVNH TNNPFWKEEF STDLPISTQM VHILIKKCSF NDSSYSTGDK
LIGTVYVTPD ILTKQIKTTS TIMTSSESSQ AIQMNTVPLS SMASNSNAGL DIVRLTINDP
NNIPIGKLLL EVHLQEYHIL SPSVFKPLEK MLVNAPMKDL IKFCNENVPS SDFERVSLVL
LDIFQSLEVE DDWFKSLMEV ELVNVDIMTR KNYHQRNSQD QAVSNSKTQQ QSSHNNVFNT
LFRGSSIFSK SLEKYNLRIG QEYLEKVFGD FFAKISNEKK NCEVDPRYVR IQERALRKGK
SIHEATGLEN GQNEDVSDDD DDDDDNSSDD DADYNAEKER ERNERIKQMV EENFQNLYGY
VEEIWYKIYI TSNDLPDQIK LQLKNFRTKV ELVCDPEDKV TSLNCLSAFI FLRFFCPAIL
NPKLFYLAKN HQTGSTQRTL TLIAKILLNF ANRQEFSPHK EPHLVRMNVF LRKHTPEIYD
YFDKLTGRKN DFNEKILDLS HEVKRFDLGL DKTSNELPTT PYLIDKYLRL TEIVHLLDYS
KYVKNIGNNN NGSMSNLGTP VNSPSRDMER EQDRSRSRSQ SGTPDLDPIL NLSDLKLNYE
NKYQIGSLEF EKSEFLELTG DNETEGFIKS LCKGNEEIFS FINSNITLKD IQKQSTKIMN
KIQELEIYLE NYEFPNNYKD QIIWDSFTDD IMNKCWLDTS RNCLIYSDHV PSSNNQYKKL
VDHAFSGLKL KFNDHQKLNG NSTMNSLINN GGMGNRNGHD VNGHNNNNNN NNNNTGDGYN
ETDRNQRLSS TFSTISIGSA IKPNTSKNPF KKWLRKN
