BUD4_CANAL
ID BUD4_CANAL Reviewed; 1709 AA.
AC P53705; A0A1D8PNF4; Q5AGC3; Q5AGQ9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Bud site selection protein BUD4;
DE AltName: Full=Alpha-INT1;
DE AltName: Full=Integrin alpha chain-like protein;
GN Name=BUD4; Synonyms=INT1; OrderedLocusNames=CAALFM_C502470WA;
GN ORFNames=CaO19.11733, CaO19.4257;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-1709, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061;
RX PubMed=8552638; DOI=10.1073/pnas.93.1.357;
RA Gale C.A., Finkel D., Tao N., Meinke M., McClellan M., Olson J.,
RA Kendrick K., Hostetter M.K.;
RT "Cloning and expression of a gene encoding an integrin-like protein in
RT Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:357-361(1996).
RN [5]
RP FUNCTION IN CELL ADHESION, AND SUBCELLULAR LOCATION.
RX PubMed=9478896; DOI=10.1126/science.279.5355.1355;
RA Gale C.A., Bendel C.M., McClellan M., Hauser M., Becker J.M., Berman J.,
RA Hostetter M.K.;
RT "Linkage of adhesion, filamentous growth, and virulence in Candida albicans
RT to a single gene, INT1.";
RL Science 279:1355-1358(1998).
RN [6]
RP FUNCTION.
RX PubMed=10444345; DOI=10.1006/mgme.1999.2875;
RA Bendel C.M., Kinneberg K.M., Jechorek R.P., Gale C.A., Erlandsen S.L.,
RA Hostetter M.K., Wells C.L.;
RT "Systemic infection following intravenous inoculation of mice with Candida
RT albicans int1 mutant strains.";
RL Mol. Genet. Metab. 67:343-351(1999).
RN [7]
RP FUNCTION.
RX PubMed=10847632; DOI=10.1097/00024382-200006000-00006;
RA Bendel C.M., Kinneberg K.M., Jechorek R.P., Erlandsen S.L., Sahar D.E.,
RA Wells C.L.;
RT "The Candida albicans INT1 gene facilitates cecal colonization in
RT endotoxin-treated mice.";
RL Shock 13:453-458(2000).
RN [8]
RP FUNCTION IN BUD SITE SELECTION, AND SUBCELLULAR LOCATION.
RX PubMed=11694587; DOI=10.1091/mbc.12.11.3538;
RA Gale C.A., Gerami-Nejad M., McClellan M., Vandoninck S., Longtine M.S.,
RA Berman J.;
RT "Candida albicans Int1p interacts with the septin ring in yeast and hyphal
RT cells.";
RL Mol. Biol. Cell 12:3538-3549(2001).
RN [9]
RP FUNCTION IN CELL ADHESION.
RX PubMed=11990933; DOI=10.1097/00003246-200203000-00030;
RA Wiesner S.M., Bendel C.M., Hess D.J., Erlandsen S.L., Wells C.L.;
RT "Adherence of yeast and filamentous forms of Candida albicans to cultured
RT enterocytes.";
RL Crit. Care Med. 30:677-683(2002).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=16178371; DOI=10.1080/13693780400013340;
RA Lee S.A., Khalique Z., Gale C.A., Wong B.;
RT "Intracellular trafficking of fluorescently tagged proteins associated with
RT pathogenesis in Candida albicans.";
RL Med. Mycol. 43:423-430(2005).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=16858141; DOI=10.1111/j.1348-0421.2006.tb03820.x;
RA Gonzalez-Novo A., Labrador L., Jimenez A., Sanchez-Perez M., Jimenez J.;
RT "Role of the septin Cdc10 in the virulence of Candida albicans.";
RL Microbiol. Immunol. 50:499-511(2006).
RN [12]
RP IDENTIFICATION OF INTRON.
RX PubMed=17351132; DOI=10.1101/gr.6111907;
RA Mitrovich Q.M., Tuch B.B., Guthrie C., Johnson A.D.;
RT "Computational and experimental approaches double the number of known
RT introns in the pathogenic yeast Candida albicans.";
RL Genome Res. 17:492-502(2007).
CC -!- FUNCTION: Required for establishment of the axial budding pattern in
CC yeast cells. May be involved in the selection of future sites of
CC septation in hyphal cells. Contributes to morphogenesis and is
CC important for induction of hyphal growth. Also plays a role in
CC epithelial adherence, and is involved in intestinal colonization and
CC systemic infection. The role in adhesion is probably minor compared
CC with its role in morphogenesis. {ECO:0000269|PubMed:10444345,
CC ECO:0000269|PubMed:10847632, ECO:0000269|PubMed:11694587,
CC ECO:0000269|PubMed:11990933, ECO:0000269|PubMed:9478896}.
CC -!- SUBCELLULAR LOCATION: Cell surface. Bud neck. Spore, perispore.
CC Note=Localizes to a ring at the mother-bud neck of yeast and
CC pseudohyphal cells. Localizes to single or double rings distal to the
CC junction of the mother cell and germ tube in hyphal cells. Requires
CC septins for proper localization. Also found at the cell-surface of
CC blastospores.
CC -!- SIMILARITY: Belongs to the BUD4 family. {ECO:0000305}.
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DR EMBL; CP017627; AOW29672.1; -; Genomic_DNA.
DR EMBL; U35070; AAA96019.1; -; Genomic_DNA.
DR PIR; T18216; T18216.
DR RefSeq; XP_019330964.1; XM_019475419.1.
DR AlphaFoldDB; P53705; -.
DR BioGRID; 1220689; 2.
DR STRING; 237561.P53705; -.
DR PRIDE; P53705; -.
DR GeneID; 3637761; -.
DR KEGG; cal:CAALFM_C502470WA; -.
DR CGD; CAL0000198939; INT1.
DR VEuPathDB; FungiDB:C5_02470W_A; -.
DR eggNOG; ENOG502REBM; Eukaryota.
DR HOGENOM; CLU_240532_0_0_1; -.
DR InParanoid; P53705; -.
DR OrthoDB; 181602at2759; -.
DR PHI-base; PHI:124; -.
DR PRO; PR:P53705; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0000142; C:cellular bud neck contractile ring; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0007120; P:axial cellular bud site selection; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0097271; P:protein localization to bud neck; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell cycle; Cell division; Reference proteome.
FT CHAIN 1..1709
FT /note="Bud site selection protein BUD4"
FT /id="PRO_0000174218"
FT DOMAIN 1575..1684
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1282..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1326..1343
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 158
FT /note="P -> S (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="I -> V (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="A -> V (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="S -> L (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="H -> R (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="D -> N (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="T -> V (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="N -> H (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 523..525
FT /note="KQI -> RQT (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="F -> L (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 723
FT /note="S -> L (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 845
FT /note="S -> F (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 1148
FT /note="T -> A (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 1340
FT /note="H -> HHH (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 1509
FT /note="L -> S (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
FT CONFLICT 1705
FT /note="Q -> QQQQ (in Ref. 4; AAA96019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1709 AA; 192915 MW; 3D56249F8ADFB3D3 CRC64;
MQTSISTTTI EDHLHHYSPE ESQKLLSRES SINTDLFKHE NESVDLLLKE MNSTPSKLLP
IDKHSHLQLQ PQSSSASIFN SPTKPLNFPR TNSKPSLDPN SSSDTYTSEQ DQEKGKEEKK
DTAFQTSFDR NFDLDNSIDI QQTIQHQQQQ PQQQQQLPQT DNNLIDEFSF QTPMTSTLDL
TKQNPTVDKI NENHAPTYIN TSPNKSIMKK ATPKASPKKV AFTATNPEIH HYPDNRVEEE
DQSQQKEDSV EPPSIQHQWK DPSQFNYSDE DTNASVPPTP PLHTTKPTFA QLLNKNNEVN
SEPEALTDMK LKHENFSNLS LDEKVNLYLS PTNNNNSKNV SDMDSHLQNL QDASKNKTNE
NIHNLSFALK APKNDIENPL NSLTNADISL RSSGSSQSSL QSLRDDNRVL ESTPGSPKKV
NPGLSLNDGI KGFSDEVVES LLPRDLSRDK LETTKENDAP EHNNENFIDA KSTNTNKGQL
LVSSDDHLDS FDRSYNHTEQ SILNLLNSAS QSQISLNALE KQKQIQEQEQ TQAAEPEEET
SFSDNIKVKQ EPKSNLEFVK VTIKKEPVSA TEIKAPKREF SSRILRIKNE DEIAEPADIH
PKKENEANSH VEDTDALLKK ALNDDEESDT TQNSTKMSIR FHIDSDWKLE DSNDGDREDN
DDISRFEKSD ILNDVSQTSD IIGDKYGNSS SEITTKTLAP PRSDNNDKEN SKSFEDPANN
ESSQQQLEVP HTKEDDSILA NSSNIAPPEE LTLPVVEAND YSSFNDVTKT FDAYSSFEES
LSREHETDSK PINFISIWHK QEKQKKHQIH KVPTKQIIAS YQQYKNEQES RVTSDKVKIP
NAIQSKKFKE VNVMSRRVVS PDMDDLNVSQ FLPELSEDSG FKDLNFANYS NNTNRPRSFT
PLSTKNVLSN IDNDPNVVEP PEPKSYAEIR NARRLSANKA APNQAPPLPP QRQPSSTRSN
SNKRVSRFRV PTFEIRRTSS ALAPCDMYND IFDDFGAGSK PTIKAEGMKT LPSMDKDDVK
RILNAKKGVT QDEYINAKLV DQKPKKNSIV TDPEDRYEEL QQTASIHNAT IDSSIYGRPD
SISTDMLPYL SDELKKPPTA LLSADRLFME QEVHPLRSNS VLVHPGAGAA TNSSMLPEPD
FELINSPTRN VSNNSDNVAI SGNASTISFN QLDMNFDDQA TIGQKIQEQP ASKSANTVRG
DDDGLASAPE TPRTPTKKES ISSKPAKLSS ASPRKSPIKI GSPVRVIKKN GSIAGIEPIP
KATHKPKKSF QGNEISNHKV RDGGISPSSG SEHQQHNPSM VSVPSQYTDA TSTVPDENKD
VQHKPREKQK QKHHHRHHHH KQKTDIPGVV DDEIPDVGLQ ERGKLFFRVL GIKNINLPDI
NTHKGRFTLT LDNGVHCVTT PEYNMDDHNV AIGKEFELTV ADSLEFILTL KASYEKPRGT
LVEVTEKKVV KSRNRLSRLF GSKDIITTTK FVPTEVKDTW ANKFAPDGSF ARCYIDLQQF
EDQITGKALQ FDLNCFNEWE TMSNGNQPMK RGKPYKIAQL EVKMLYVPRS DPREILPTSI
RSAYESINEL NNEQNNYFEG YLHQEGGDCP IFKKRFFKLM GTSLLAHSEI SHKTRAKINL
SKVVDLIYVD KENIDRSNHR NFSDVLLLDH AFKIKFANGE LIDFCAPNKH EMKIWIQNLQ
EIIYRNRFRR QPWVNLMLQQ QQQQQSSQQ
