ID   SLA1_CANAL              Reviewed;        1257 AA.
AC   Q5ALV2; A0A1D8PGF4;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1;
GN   Name=SLA1; OrderedLocusNames=CAALFM_C201640WA;
GN   ORFNames=CaO19.1474, CaO19.9049;
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=11737641; DOI=10.1046/j.1365-2958.2001.02713.x;
RA   Murad A.M., d'Enfert C., Gaillardin C., Tournu H., Tekaia F., Talibi D.,
RA   Marechal D., Marchais V., Cottin J., Brown A.J.;
RT   "Transcript profiling in Candida albicans reveals new cellular functions
RT   for the transcriptional repressors CaTup1, CaMig1 and CaNrg1.";
RL   Mol. Microbiol. 42:981-993(2001).
RN   [5]
RP   SUBCELLULAR LOCATION, DOMAIN, AND FUNCTION.
RX   PubMed=20383711; DOI=10.1007/s00294-010-0301-7;
RA   Reijnst P., Jorde S., Wendland J.;
RT   "Candida albicans SH3-domain proteins involved in hyphal growth,
RT   cytokinesis, and vacuolar morphology.";
RL   Curr. Genet. 56:309-319(2010).
RN   [6]
RP   INTERACTION WITH CLN3 AND PAN1, PHOSPHORYLATION BY CDC28-CLN3 AND PRK1,
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=22787279; DOI=10.1091/mbc.e12-03-0231;
RA   Zeng G., Wang Y.M., Wang Y.;
RT   "Cdc28-Cln3 phosphorylation of Sla1 regulates actin patch dynamics in
RT   different modes of fungal growth.";
RL   Mol. Biol. Cell 23:3485-3497(2012).
CC   -!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory complex
CC       required for the internalization of endosomes during actin-coupled
CC       endocytosis. The complex links the site of endocytosis to the cell
CC       membrane-associated actin cytoskeleton. Required for assembly of the
CC       cortical actin cytoskeleton and for hyphal growth.
CC       {ECO:0000269|PubMed:20383711, ECO:0000269|PubMed:22787279}.
CC   -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex
CC       (By similarity). Interacts with PAN1 and CLN3. {ECO:0000250,
CC       ECO:0000269|PubMed:22787279}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cell membrane; Peripheral
CC       membrane protein; Cytoplasmic side. Endosome membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Cytoplasm, cytoskeleton, actin patch {ECO:0000250}. Cell
CC       tip. Note=Localizes in patches that are found concentrated at the
CC       hyphal tip.
CC   -!- INDUCTION: Expression is regulated by NRG1 and MIG1.
CC       {ECO:0000269|PubMed:11737641}.
CC   -!- DOMAIN: The N-terminal SH3 domains are important for actin cytoskeleton
CC       assembly but not for localization. {ECO:0000269|PubMed:20383711}.
CC   -!- PTM: Phosphorylated by the CDC28-CLN3 complex and by PRK1. CDC28-CLN3
CC       phosphorylation regulates cortical actin patch dynamics, as well as
CC       PRK1 phosphorylation and SLA1 association with PAN1. Rapidly
CC       dephosphorylated upon hyphal induction. {ECO:0000269|PubMed:22787279}.
CC   -!- SIMILARITY: Belongs to the SLA1 family. {ECO:0000305}.
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DR   EMBL; CP017624; AOW27210.1; -; Genomic_DNA.
DR   RefSeq; XP_722523.1; XM_717430.1.
DR   AlphaFoldDB; Q5ALV2; -.
DR   SMR; Q5ALV2; -.
DR   BioGRID; 1218833; 3.
DR   STRING; 237561.Q5ALV2; -.
DR   PRIDE; Q5ALV2; -.
DR   GeneID; 3635739; -.
DR   KEGG; cal:CAALFM_C201640WA; -.
DR   CGD; CAL0000198859; SLA1.
DR   VEuPathDB; FungiDB:C2_01640W_A; -.
DR   eggNOG; ENOG502QQC3; Eukaryota.
DR   HOGENOM; CLU_003674_0_0_1; -.
DR   InParanoid; Q5ALV2; -.
DR   OMA; PDWILVG; -.
DR   OrthoDB; 1483210at2759; -.
DR   PRO; PR:Q5ALV2; -.
DR   Proteomes; UP000000559; Chromosome 2.
DR   GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR   GO; GO:1990964; C:actin cytoskeleton-regulatory complex; IEA:EnsemblFungi.
DR   GO; GO:0051286; C:cell tip; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030427; C:site of polarized growth; IDA:CGD.
DR   GO; GO:0140224; C:SLAC complex; IEA:EnsemblFungi.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0140312; F:cargo adaptor activity; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
DR   GO; GO:0000147; P:actin cortical patch assembly; IMP:CGD.
DR   GO; GO:0044396; P:actin cortical patch organization; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:CGD.
DR   GO; GO:0071555; P:cell wall organization; IEA:EnsemblFungi.
DR   GO; GO:0006897; P:endocytosis; IMP:CGD.
DR   GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR   GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR   GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IEA:EnsemblFungi.
DR   CDD; cd11773; SH3_Sla1p_1; 1.
DR   CDD; cd11775; SH3_Sla1p_3; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR007131; SHD1.
DR   InterPro; IPR029922; Sla1.
DR   InterPro; IPR035800; Sla1_SH3_1.
DR   InterPro; IPR035821; Sla1_SH3_3.
DR   PANTHER; PTHR11216:SF134; PTHR11216:SF134; 2.
DR   Pfam; PF00018; SH3_1; 2.
DR   Pfam; PF14604; SH3_9; 1.
DR   Pfam; PF03983; SHD1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF50044; SSF50044; 3.
DR   PROSITE; PS50002; SH3; 3.
PE   1: Evidence at protein level;
KW   Actin-binding; Cell membrane; Cytoplasm; Cytoskeleton; Endocytosis;
KW   Endosome; Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   SH3 domain.
FT   CHAIN           1..1257
FT                   /note="Actin cytoskeleton-regulatory complex protein SLA1"
FT                   /id="PRO_0000424376"
FT   DOMAIN          4..74
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          75..134
FT                   /note="SH3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          396..458
FT                   /note="SH3 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          133..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          464..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1057..1168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1207..1257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..182
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..515
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..832
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..867
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1207..1247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1257 AA;  138870 MW;  981BF1339AA506BA CRC64;
     MSSIYIGVYK ALYDYAAQAE EELNIKQNDL LYLLEKSDID DWWKVKKRVV ATGEEIVDEP
     SGLVPSTYIE EAPVIKTATA LYDYDKQTEE ELSFNENDKF NVFDLNDPDW ILVGDLAKEK
     FGFVPSNYIQ LDSTAEPAQH QQQQPQQVFQ PPPQQQQAIP QQQTQIPINN FPPPPTHKDR
     TPDFPAPPAH RDRSPEHPPP TPEKDYPRMF EQEPRSLGSR YDRQPEGREE EEDEAPPPMP
     SRPTGSNIVA PEPVVGRSNT YEQEENVEHS EHSYDGEFFT WYIDEVDGRK KRAIKLSIGQ
     GLVIIKPNTT NPKKLRMRSS SSLDNQWRIK DLITFNNEKK HVFLEFKNPA ASLELHAGSK
     DVAEAIMAIL GDLKGAEAAH GLREVAKASK ASANERNRKI GRLLYDFEVQ GDDELDCKEG
     DEVYIIDQKK SKDWWMVENI ATRRQGVVPS TYIEIISTSN LDKLTDGPLR RKSTKSKGRV
     VETKDKRSSH HRTREERDRI REKDRAQRDK APTSQTEQDK SMPNFHRVRT WIDSSGTFKV
     EAEFLGCVEG KIHLHKTNGV KIAVAADKLS VEDLEYVERV TGTSLEQYKE QVMKQQAKRA
     KSKSKSGATA TPSSTNETKY ASSATAAIND IAPPKPTRPQ TTTQVSNNGA PLYDWFDFFL
     ECGVDIGNCQ RYTLNFEREQ MDENILEDIS PSLLRTLGLR EGDIIRVMKY LDAKFDRKKT
     PEAPQQNGGL FIDKNGNLKN NSSSTEISKV SADALPSPVK TQVTSFTPVN ESTQNNNKIE
     DDAWAMKPAA RSSEDLLKPS PQPQTPQYTG ALSDLVNIKP VGTSNENKAK TEQIPVEPSA
     PALQPMKTSN TAATSSIPPQ GPGVTPQRTG TLVPVQKTGG LVPVQRTGAG LVPVQTGGYL
     PAQPTGFVPI TAQPTGFIPI QATGILQPQL TFGIVPLQTG TSTFNANNKT APPRPDTAPP
     PITTFGQQPT FQPAFVPLQT GVITMPQTTF GGQSQQLPTQ ITGGAPPQTS FNQPALVPTQ
     RTGGQITGGF VPQSNFGKQI TGGFMDTNTL SFGQQITGNA QQQPPPSTSF GQQITGGLPA
     TSFGQQITGG FPQTSFGQQM TGGAPQTSFG QHITGGNMPN TSFGQPFSQQ ATSNPFPQMA
     NQFTQQQQYQ QQQPVMNQFQ QQPQQQQQPF YNQFQSQPNL NQMTNMFQNT SISSPATFNQ
     QIPTTTFGQQ PQFEGFGSQP LQSQPTGMGF GNAPLQSQPT GKRANLQAAT PDNPFGF