ID T0KF06_COLGC Unreviewed; 1149 AA.
AC T0KF06;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
GN ORFNames=CGLO_09821 {ECO:0000313|EMBL:EQB50714.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB50714.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
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.
CC {ECO:0000256|ARBA:ARBA00025194}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton, actin patch {ECO:0000256|ARBA:ARBA00004134}. Endosome
CC membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the SLA1 family.
CC {ECO:0000256|ARBA:ARBA00007948}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQB50714.1}.
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DR EMBL; AMYD01001972; EQB50714.1; -; Genomic_DNA.
DR AlphaFoldDB; T0KF06; -.
DR STRING; 1237896.T0KF06; -.
DR eggNOG; ENOG502QQC3; Eukaryota.
DR HOGENOM; CLU_003674_0_0_1; -.
DR OMA; FMAQGED; -.
DR OrthoDB; 2906837at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd11773; SH3_Sla1p_1; 1.
DR CDD; cd11774; SH3_Sla1p_2; 1.
DR CDD; cd11775; SH3_Sla1p_3; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
DR Gene3D; 2.30.30.700; SLA1 homology domain 1; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR013182; DUF1720.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR007131; SHD1.
DR InterPro; IPR035800; Sla1_SH3_1.
DR InterPro; IPR035821; Sla1_SH3_3.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR PANTHER; PTHR15735:SF20; PROTEIN NERVOUS WRECK; 1.
DR Pfam; PF08226; DUF1720; 1.
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; SH3-domain; 3.
DR PROSITE; PS50002; SH3; 3.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 2..69
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 70..127
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 369..431
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 125..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..801
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..927
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1133..1149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1149 AA; 122435 MW; 8D53CB3DF4EC0546 CRC64;
MGFSGVCKAI YDYAPQAEGE LAISDGDVLY ILEKNAEDDW WKAKKKASAD DEDEPEGLIP
NNYVEEAQPI AKARALYEYT RQTDEELSFP EDALIDVYDT SDPDWILVGL DGDYGFVPSN
YIEMSESEDA APQPSPPPAL PSRTSIPPAP GPDSNPERPE STNSAPSLPN NPAAALAGVI
AGRSAPAPRA ESPPISPQSP LSEPSDEEHV RSPALPARPI SQVAPPPARI QSQRSIDTHL
YDNSPEVEEP PYRAPGGFHM YNINEMVSVM GKRKKMPTTL GVNLATGTIL IAPERAQDGP
SQEWTADKMT HYSREGKHVF LELVRPSKSV DFHAGAKDTA EEIVSALGEL AGAVRAEGLR
EVILAGAGKA QKKGQVLYDF MAQGDDEVTV AIGDDVVIID DTKSEEWWQV RRVKNGKEGV
VPSSYIEITG SITPPPSNTG INAAKSTVEQ NRLEEIRLTK EAVKAAQRDS SQQVGPGMPL
PKRGSSLMAR ENGNNYGQRI KRENGRGEGS GQSRSGKSKP DPSKVRTWTD RSKSFSVDAQ
FLGLKDGKIN LHKMNGVKIA VPVAKMSVGD LEYVERITGI SLDEDKPLSN VKKARAASQA
GAARDSASGG VGASVGPPQK PEYDWFQFFL SCDVAVGLCE RYAQAFSKDS MDESVLPDVD
ASILRNLGLR EGDIIKVMRT LDQKFGRVRG GDKSSAEGDG GSGGLFTGPG GALRNNTRKG
RPAPAVQTSD VVDPKAFARK EDGPAEDPSS KSLSSAPGPS PGQTSGFDDD AWDVKPAKQL
QEPAAGSSPI PPVPAATQPP TQPVQQPVSQ SVPSPQVPAL TGSMQELSLL STPLEPQRTA
QTPAQKPTAS QPLAPAQAPQ PTGATPSFFA TVRPNTTSTQ SPQQPMQRQR PTPPAATSSQ
GVLMPPPPSR PLSAPQSAQP SAFAPPPLAP QMTGFQTPVA PPGQSMNEIS QARLQQQFAI
QQQQQQQMAQ SQMNPYPAPQ QQPIPGVMGF NAGMQQPGGQ FMQSMQPMMT GATNQSPFAD
PQRPNQFNPM QVQPTGFPGQ FGNNQTFNPQ ATGINSFLPP AMEPQRTAAP GFQPQQTGFQ
PQQTGFGGFN SLGGASSLAA PVQPLQPQKT GPPPPVRFGV TGDAKKIMAQ PTGRRANLSQ
ATPNNPFGF
//
