SLA1_YARLI
ID SLA1_YARLI Reviewed; 1136 AA.
AC Q6CHN0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1;
GN Name=SLA1; OrderedLocusNames=YALI0A07018g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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. Mediates uptake of external
CC molecules and vacuolar degradation of plasma membrane proteins. Plays a
CC role in the proper organization of the cell membrane-associated actin
CC cytoskeleton and promotes its destabilization (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250}. Note=Cytoplasmic and cortical actin patches.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLA1 family. {ECO:0000305}.
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DR EMBL; CR382127; CAG83757.1; -; Genomic_DNA.
DR RefSeq; XP_499831.1; XM_499831.1.
DR AlphaFoldDB; Q6CHN0; -.
DR SMR; Q6CHN0; -.
DR STRING; 4952.CAG83757; -.
DR PRIDE; Q6CHN0; -.
DR EnsemblFungi; CAG83757; CAG83757; YALI0_A07018g.
DR GeneID; 2905766; -.
DR KEGG; yli:YALI0A07018g; -.
DR VEuPathDB; FungiDB:YALI0_A07018g; -.
DR HOGENOM; CLU_003674_0_0_1; -.
DR InParanoid; Q6CHN0; -.
DR OMA; PDWILVG; -.
DR Proteomes; UP000001300; Chromosome A.
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: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: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; IBA:GO_Central.
DR GO; GO:0044396; P:actin cortical patch organization; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:EnsemblFungi.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
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; 1.
DR Pfam; PF00018; SH3_1; 3.
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 3: Inferred from homology;
KW Actin-binding; Cell membrane; Cytoplasm; Cytoskeleton; Endocytosis;
KW Endosome; Membrane; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1136
FT /note="Actin cytoskeleton-regulatory complex protein SLA1"
FT /id="PRO_0000349492"
FT DOMAIN 4..66
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 68..128
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 356..417
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 143..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 122856 MW; FFB8D70B6AA60568 CRC64;
MPSLFHGVYQ ALYDYEARTE DELTFSENSL LYLLEKSSTD EWLKAKKAGP AGTNEIGLVP
LTYIEPAPAK RQAYALYDYD KQTEEELTFK EGDALTVYDD SDSEWLLVCR GGDEYGFVPA
NYTGDAPPSA APAPVAAIPT PVAAIPTPAG QPTTPITKDS PLPPLPKDAF PPPPQAYRPP
ASTTHASTEP VYANGRDEES PPPMPARPGG SGNGSGRPSS GAGDSRSRGS SVSRSRNASS
ANDKPSSSSA NFFTWPVQEV DGRKKRKATL AIGNGMIMFS PERSSGQPQQ WPVKDLVNYN
SEKKHVFLDF KHPTVSFDLH LGSKDTADEV IYALGELAGA YNSSGLTEVM MAANSAGQKL
GKVLYKFDAQ GRDEVSVEEG ENVFIIDDTK SRDWWMVKNS SGVAGVVPSS YIEIAPSEKT
LKKVVDQQRK ASGSSRDKSR DRSRDDRSRD RADKRSSRSS RDAPKSKPDP RKVRTWTDRS
GAFKVDAALL GCVDGKIHLH KVNGVKIAVA CSKMAIEDLE YVEDVTGVDL EEDKPLSRDR
GGSSRDRRRS TSRSDRRKSS SGAASSANAP KPTPESDYDW FGFFLDCGVD VHACQRYATS
FTRDQMDESI LPEVTPSTLR SLGLKEGDIL RVTKKLDEKY GRSGTGTSAS TPVGGNPSGG
LFSDTTGALK NNTSKTLTKA DDTDPWSSLD KQQAPPQQQA PPVQQQPPVQ QQPIQAQPTA
PIQQQPIQAQ PTAPIQPVRT GSINDLMNIK PLQPTPTSSN LQTQATGGIM QPIQQQYTQQ
PMSQSTSALP QQSMNTGILP QTTGPLQQSL TGSAPVQNPF LTGGPNTLLS QQTGGLVGVP
TGGLVGVPTG GLQGVPTGYT AQNVLGMNQP ANTGGYSMNA ITNALAGASL NKQQQQQQPM
VQQLTGGSMF GQQPMQQQLT GSSIFQQQPM QQQFTQQQPM QQQFTQQQPM SQQLTGGSIF
NSQPQQPFQQ QPMQPQQTSF QQQQPFSTGA SASPFGSQPT TPFGQPQQSA GLSYFNNIQP
LQQQQAFGQQ MQPQQTFQPQ QPFQQPFQQP FQQQQQQPFQ QQQQQPFQQQ QQPFGGLQSQ
PTGFGFGNSS SPFGGMQSQQ TGAPSTSFGQ QPLQPTATGR QRANLASATP NNPFGF
