ID H0GR36_SACCK Unreviewed; 1213 AA.
AC H0GR36;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
GN ORFNames=VIN7_5520 {ECO:0000313|EMBL:EHN03681.1};
OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN03681.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHN03681.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN03681.1,
RC ECO:0000313|Proteomes:UP000009009};
RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT origins.";
RL FEMS Yeast Res. 12:88-96(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. 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:EHN03681.1}.
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DR EMBL; AGVY01000126; EHN03681.1; -; Genomic_DNA.
DR AlphaFoldDB; H0GR36; -.
DR HOGENOM; CLU_003674_0_0_1; -.
DR PhylomeDB; H0GR36; -.
DR Proteomes; UP000009009; 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; cd09532; SAM_SLA1_fungal; 1.
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; 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; 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 Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 3..68
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 69..132
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 345..407
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 134..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1213 AA; 132544 MW; 4D56B68B44168600 CRC64;
MTVFLGIYRA IYAYEPQTPE ELAIEEDDLL YLLHKSDIDD WWTVKKRVIG SDSEEPVGLV
PSTYIEEAPI LKKVRAIYDY EQVQNADEEL TFHENDVFDV LDDKDVDWLL VKSTVSNEFG
FIPGNYVEPE EVAAPKQEEA AGAAPALPGS FLPPPQHSDR AHVLQSKQDQ VPAGEQEEEG
PPPAMPARPT TTTEMTETTA TAIRSRSRLS HSDEGNDNGE EEEEDDFYYN SNDNSVGNHD
YNTAYHSWNV TEIEGRKKKK AKLSIGNNKI NFIPQKGAPH EWSIDKLVSY DNEKKHMFLE
FVDPYRSLEL HTGNNNTCEE IMNIIGEYKG ASRDPGLKEV EMASKSKKRG IVQYNFMAES
QDELTVKSGD KVYILDAKKS KDWWMCQLVD SGKSGLVPAQ FIEPVRDKKH TESTASGIIK
SIKKNFTKSP SRSRSRSRSK SNATASASWK DDESQNDATN STVGKRSRKS SLSSHKKGST
NAKDFPNPKK SRLWVDRSGT FKVDAEFIGC AKGKIHLHKA NGVKIAVAAD KLSNEDLAYV
EKITGFSLEK FKVSDGSSSH GTDSRDSERE RRRRLKEQEE KERDRRLKER ELYELKKARE
LLDEERSRLQ EKELPPIKPP RPTSTASASN MTSTPSTENG NNNSNGNKYD WFEFFLNCGV
DVSNCQRYTI NFDREQITED MTSDINNSML RTLGLREGDI VRVMKYLDKK FGRENNTTIP
TNATGNMFSQ PDGSLNAATG AETPLPQQLL PQATAPTPSA SSETDDAWTV KPASKSESNL
LSKKSEFTGS MQDLLDLQPL EPKKTSTTTP EPNLKELEPV KTGGTPAATA SAPAPLDPFK
TGGNNFLPLS TGFVMMPMYT GGAMLPMQRT GGFVMPQTTF GMQSQATGGI LPVQKTNNGL
IAISNTGGAM MPQTTFGATP TVLPLQKTGG GLIPIATTGG GQFPQTSFNI QAQQQFPTGS
ILPVQKTANG LISANTGISM PSLQRTGGAM MPQPQIMGGA MMPQPQITGG AMMPQPQITG
GAMMPQTSFG VSQQLTGGAI IAQPQNTGSA MMPQTSFNSL PQNAAGAVMP LQRTGGALNT
FNTGGAMIPQ TSFNTQPQIT GGFRPQSQFG LTLQRTGGIA PLNQNQLTGG AMNTFNTGGI
LQQQQPQIMN TFNTGGAMQQ PQIMSTFNTG GAMQQPQQQA LQNQPTGFGF GNGPQQSRQA
NIFNATASNP FGF
//
