ID   SLA1_SCLS1              Reviewed;        1150 AA.
AC   A7E8B6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Actin cytoskeleton-regulatory complex protein sla1;
GN   Name=sla1; ORFNames=SS1G_01544;
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS   (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN96618.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH476622; EDN96618.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001597350.1; XM_001597300.1.
DR   AlphaFoldDB; A7E8B6; -.
DR   SMR; A7E8B6; -.
DR   STRING; 665079.A7E8B6; -.
DR   GeneID; 5493263; -.
DR   KEGG; ssl:SS1G_01544; -.
DR   eggNOG; ENOG502QQC3; Eukaryota.
DR   InParanoid; A7E8B6; -.
DR   Proteomes; UP000001312; Unassembled WGS sequence.
DR   GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
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: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:0000147; P:actin cortical patch assembly; IBA:GO_Central.
DR   GO; GO:0044396; P:actin cortical patch organization; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR   CDD; cd11773; SH3_Sla1p_1; 1.
DR   CDD; cd11775; SH3_Sla1p_3; 1.
DR   Gene3D; 1.10.150.50; -; 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; IPR029922; Sla1.
DR   InterPro; IPR035800; Sla1_SH3_1.
DR   InterPro; IPR035821; Sla1_SH3_3.
DR   PANTHER; PTHR11216:SF134; PTHR11216:SF134; 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; 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..1150
FT                   /note="Actin cytoskeleton-regulatory complex protein sla1"
FT                   /id="PRO_0000349489"
FT   DOMAIN          2..69
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          70..127
FT                   /note="SH3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          393..455
FT                   /note="SH3 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          127..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          490..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          605..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          846..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1026..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1101..1150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..547
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..620
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..780
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        788..806
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..827
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        908..922
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1060
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1124..1150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1150 AA;  124099 MW;  7D542882A2F11ED4 CRC64;
     MGFLGVYSAV YDYVPAGEGE LTIKEGDILY VLEKSTEDDW WKAKKKASAE DEDEPVGLIP
     NNYIQEAAPS GKARALYDYT RQTDEELSFT EDAQLEVFDT SDPDWILVGF EGEYGFVPAN
     YIELSEEEQH KEAPAPSLPS RPRPASVPVE EEAPAAPQSP LSPQPAETPV ATPAAAIAGI
     LKQRQASAPA ARAPPEFTPE ASDEEPPTPT LPARPVSQVS VPQPTRGQEH DREREPARRY
     SPRLPASPVV TASPPHNRVS FSTMGVVNDV DEHKAARAPG GFHMYNISEM VHVMGKKKKM
     PTTLGINIAT GTILIAPEQA RDGPEQTWTA EKMTHYSLEG KHVFMELVRP SKSIDFHAGA
     KDTATEIVSA LGELAGAARA EGLREVIAAG SGSGQKRGQV LYDFVAQGDD EVDVNVGDEV
     VIIDDVKSEE WWMVRRVKNA KEGVVPSSYI EIMGAIQSAS SAGINAGRST VEQNRLEEAR
     LAREALKTAK KDEVEVGPGM RLPERGSSLF ARDNGNQSGE QKRRESVRES GQSRSSKSKP
     DPAKVRTWTD RSKSFSVEAQ FLALKDGKIN LHKMNGVKIA VPVVKMSVED LEYVERMTGI
     SLDEDKPLSD IKKQQKSRAA ERDSSNGASP APGPSASMGA GASIQTPEYD WFQFFLSCDV
     NVGLCERYAQ AFKRDSMDES VLPDIDATVL RNLGIREGDI IKIIRFLDKK YMRKDGKRNV
     SFGGEDEGEA GLFSGPGGAL KNNTRKGRPA PAVQTNDVVD ANAFSQNGTE KSSPQGVATP
     LANAPTPAEK DVKREGFDDD AWDVKPSKQE TTSSPPAQSI PAAAPQQPVI TGSMQELSLL
     STPLEPVKAQ PTAQASPQPQ APPAVTPSIF AGIGNQQTGV PQPQPLPSGP LLPANLARQR
     PAPPQMTANS TLIPPLPPSR PLSAPQAASA YAPPPLQAQA TGYGAFQPQI APPGQSLHDL
     NQQRMQQQQQ QQMQQQQFML QQQQQAGMMQ QPTGFNQFNP GVPNNFQQFP MQTGNPQQPF
     IPNQTGTPFA NPPAQPFQPQ PLQAQPTGFQ SAFPPGQQYP QPTGVNSYLP PALQPQPTGM
     MNGANGFNQN FTPPPIPPMP QQQPAPMLPQ ATGPAPPVRF GVNGTNNIAP QPTGRRANLA
     QATPQNPFGF