SUR7_CANAL
ID SUR7_CANAL Reviewed; 270 AA.
AC Q5A4M8; A0A1D8PPP2; O94006;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Protein SUR7;
DE Flags: Precursor;
GN Name=SUR7; OrderedLocusNames=CAALFM_C601720CA;
GN ORFNames=CaO19.10917, CaO19.3414;
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 SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18799621; DOI=10.1091/mbc.e08-05-0479;
RA Alvarez F.J., Douglas L.M., Rosebrock A., Konopka J.B.;
RT "The Sur7 protein regulates plasma membrane organization and prevents
RT intracellular cell wall growth in Candida albicans.";
RL Mol. Biol. Cell 19:5214-5225(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19824013; DOI=10.1002/pmic.200800988;
RA Cabezon V., Llama-Palacios A., Nombela C., Monteoliva L., Gil C.;
RT "Analysis of Candida albicans plasma membrane proteome.";
RL Proteomics 9:4770-4786(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20433738; DOI=10.1186/1471-2180-10-133;
RA Bernardo S.M., Lee S.A.;
RT "Candida albicans SUR7 contributes to secretion, biofilm formation, and
RT macrophage killing.";
RL BMC Microbiol. 10:133-133(2010).
RN [7]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=21115741; DOI=10.1128/ec.00167-10;
RA Wang H.X., Douglas L.M., Aimanianda V., Latge J.P., Konopka J.B.;
RT "The Candida albicans Sur7 protein is needed for proper synthesis of the
RT fibrillar component of the cell wall that confers strength.";
RL Eukaryot. Cell 10:72-80(2011).
RN [8]
RP INDUCTION.
RX PubMed=21622905; DOI=10.1128/ec.05011-11;
RA Sorgo A.G., Heilmann C.J., Dekker H.L., Bekker M., Brul S., de Koster C.G.,
RA de Koning L.J., Klis F.M.;
RT "Effects of fluconazole on the secretome, the wall proteome, and wall
RT integrity of the clinical fungus Candida albicans.";
RL Eukaryot. Cell 10:1071-1081(2011).
RN [9]
RP FUNCTION.
RX PubMed=22202230; DOI=10.1128/mbio.00254-11;
RA Douglas L.M., Wang H.X., Keppler-Ross S., Dean N., Konopka J.B.;
RT "Sur7 promotes plasma membrane organization and is needed for resistance to
RT stressful conditions and to the invasive growth and virulence of Candida
RT albicans.";
RL MBio 3:135-150(2012).
RN [10]
RP INDUCTION.
RX PubMed=23490206; DOI=10.1111/cmi.12135;
RA She X., Zhang L., Chen H., Calderone R., Li D.;
RT "Cell surface changes in the Candida albicans mitochondrial mutant
RT goa1Delta are associated with reduced recognition by innate immune cells.";
RL Cell. Microbiol. 15:1572-1584(2013).
CC -!- FUNCTION: Involved in cell wall, plasma membrane, and cytoskeletal
CC organization. Plays a role in endocytosis and hyphal morphogenesis.
CC Required to restrict septin proteins to the bud neck and prevents
CC intracellular growth of cell wall. Contributes to secretion, biofilm
CC formation, and macrophage killing. Essential for resistance to
CC stressful conditions and for invasive growth and virulence.
CC {ECO:0000269|PubMed:18799621, ECO:0000269|PubMed:20433738,
CC ECO:0000269|PubMed:21115741, ECO:0000269|PubMed:22202230}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18799621,
CC ECO:0000269|PubMed:19824013, ECO:0000269|PubMed:21115741}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:18799621,
CC ECO:0000269|PubMed:19824013, ECO:0000269|PubMed:21115741}.
CC Note=Localizes at eisosomes, structures which colocalize with sites of
CC protein and lipid endocytosis.
CC -!- INDUCTION: Induced by fluconazole and down-regulated in absence of
CC GOA1. {ECO:0000269|PubMed:21622905, ECO:0000269|PubMed:23490206}.
CC -!- DISRUPTION PHENOTYPE: Leads to defective tolerance to cell wall stress
CC and antifungal agents targeting cell wall components, defective plasma
CC membrane structure, defective endocytosis, impaired lipase secretion,
CC SAP2 over-production, increased adherence, aberrant biofilm formation,
CC defective macrophage killing, and decreased virulence in a mouse
CC infection model. {ECO:0000269|PubMed:20433738}.
CC -!- SIMILARITY: Belongs to the SUR7 family. {ECO:0000305}.
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DR EMBL; CP017628; AOW30109.1; -; Genomic_DNA.
DR RefSeq; XP_716723.1; XM_711630.1.
DR AlphaFoldDB; Q5A4M8; -.
DR STRING; 237561.Q5A4M8; -.
DR TCDB; 1.H.1.7.2; the claudin tight junction (claudin1) family.
DR PRIDE; Q5A4M8; -.
DR GeneID; 3641610; -.
DR KEGG; cal:CAALFM_C601720CA; -.
DR CGD; CAL0000180156; SUR7.
DR VEuPathDB; FungiDB:C6_01720C_A; -.
DR HOGENOM; CLU_059603_1_0_1; -.
DR InParanoid; Q5A4M8; -.
DR OMA; PLNKFYW; -.
DR OrthoDB; 1348547at2759; -.
DR PHI-base; PHI:2337; -.
DR PRO; PR:Q5A4M8; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0032126; C:eisosome; IDA:CGD.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0016021; C:integral component of membrane; ISM:CGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:CGD.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0044853; C:plasma membrane raft; IDA:CGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:CGD.
DR GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:CGD.
DR GO; GO:0006897; P:endocytosis; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036171; P:filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0032185; P:septin cytoskeleton organization; IMP:CGD.
DR GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
DR InterPro; IPR009571; SUR7/Rim9-like_fungi.
DR Pfam; PF06687; SUR7; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Endocytosis; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Stress response;
KW Transmembrane; Transmembrane helix; Virulence.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..270
FT /note="Protein SUR7"
FT /id="PRO_0000424631"
FT TOPO_DOM 28..107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 220..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 270 AA; 29916 MW; 46940D75D487460D CRC64;
MKVVFTFFNL FFLAGTVLLL IFTVLSGSSK HFPLNKFYWL EADTSGIKNA PANRSAWTFW
GVCDKADYSN CLLGPAYPIS PEDNFGTTAD IPKDFVDNEN TYYYLSRFAF AFCLIALAFS
GLAFIIDILG FCFEIIDKVV IFLITIGLLF LAGFASLQTA VVVLAKNAFK NDGRYAHIGA
KSMGIMWAAF ACLLICWLLI FAGTISNSYK KHIARVKAEQ GQYSQPTHGP AGDESSFTRA
APPTKDEENT GGIRFFKIKR NQKVSDDESV
