ID S8AYB8_PENO1 Unreviewed; 1161 AA.
AC S8AYB8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
GN ORFNames=PDE_06283 {ECO:0000313|EMBL:EPS31328.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS31328.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS31328.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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}.
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DR EMBL; KB644413; EPS31328.1; -; Genomic_DNA.
DR AlphaFoldDB; S8AYB8; -.
DR STRING; 933388.S8AYB8; -.
DR eggNOG; ENOG502QQC3; Eukaryota.
DR HOGENOM; CLU_003674_0_0_1; -.
DR OrthoDB; 2906837at2759; -.
DR PhylomeDB; S8AYB8; -.
DR Proteomes; UP000019376; 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; 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:SF19; ACTIN CYTOSKELETON-REGULATORY COMPLEX PROTEIN SLA1; 1.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR Pfam; PF08226; DUF1720; 1.
DR Pfam; PF00018; SH3_1; 3.
DR Pfam; PF03983; SHD1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SH3-domain; 3.
DR PROSITE; PS50002; SH3; 2.
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:UP000019376};
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 399..461
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 132..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1100..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..210
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..944
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1161 AA; 125563 MW; 8CEB6FE93D56BE5E CRC64;
MGFLGVYTAV YDYQPQGEGE LEIKEGDLLC VLEKNSEDDW WKAKKKAERD DDDEPEGLIP
NNYIEEAQPI HRAKALFDYT RQTDEEVSFS EDADILVYDT SDPDWTLVGV HSDYGFAPAN
YIEIVGHASA APLSPAADEE PAAPSLPVRP PQPQAAEDDD EPPSPSPIDS VQNPAAAAIA
NIIHQQHAPP PAQPEYSRDE PSPPRLPSRP PPEQEEYRAE SPPPPSLPRR PPSEVPTPTF
SHHDSEPASS PAHSNPPPPP MGGHSRPYVK ESPPYSRGGE ITPRSPSGYH IYNINEMVEV
MGKRKKMPTT LGINMATGII FISPEGDDRQ QEWTADKLTH YSIEGKHVFV DLIRPSKNID
FHAGAKDTAQ EIVAALGEIA GAYRAEGLRE VFAASEGGAG QKKGQILYDF MAQGDDEVTV
AVGDEVAILD DTKAEEWWMV RRLKNGREGV VPSSYVEIIG FMPGQPSPAI ESAKSTVERN
RSEEARLAKA AVGRPRTDSL ETPERSKRDS KRDSKRDSKT SKSKPDPSKV RKWTDRTKAF
TVEAEFIGLL DGKIQLHKVN GIKIAVPVAK MSVEDLEYVE KVAGVSLDED KPLSSIRARA
SDDAKRGPAG ASVQGPEYDW FDFFLKAGVG PHQCERYAQN FLKDSMDESV LPDITPETLR
TLGLKEGDIL RVMRHLDNTL GRTGSKSKLR NVSFGGEEVI SNGEEGGLFA GPGGMLRNNT
RKGRPTPAVQ AGDVVDPKAF EQADGSQPKK PEERTATPPT PAAPTATASA EKPVARGFED
DAWEVKKPQG SAAAPPPKTS ASPPPVQSPI QKQITGAMAD LSILQAPLQP TPASPAQPTP
SISSIPALQP QQTAVQSPPV QQPQQTGATP NFFNQIAQIG QHQQQQQLQQ QQQQQQQQQQ
LQAQPFSPQQ TGFQTQARPR PVAPQAMAQN SLLPPPPPRP LSAPQNFTPQ QTSFSPPPLQ
PQLTGIPQPG APSMGQPMNG VNQPGMQSPL QMQPQITGFM GPNQYQNGMM VPQPTGFTPQ
SQFGIQQQQQ NQLPYANGQP GFPNMAPQPT GMAPQPTGFG GYVPPLQPMA TGINAILPPA
LQPQPTGASR FGNASYSVHN PPPVPPIPSQ PTATPLMPQK TGPPPSIRFG VKPEGPKKLA
PQPTGMRANL AQATPNNPFG F
//
