SLA1_YEAS7
ID SLA1_YEAS7 Reviewed; 1244 AA.
AC A6ZKU1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1;
GN Name=SLA1; ORFNames=SCY_0211;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 Interacts with ABP1, KRE6, LAS17, LSB5, RSP5, RVS167, VPS1 and YSC84
CC (By similarity). {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 -!- PTM: Phosphorylated by PRK1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLA1 family. {ECO:0000305}.
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DR EMBL; AAFW02000011; EDN64610.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZKU1; -.
DR SMR; A6ZKU1; -.
DR PRIDE; A6ZKU1; -.
DR EnsemblFungi; EDN64610; EDN64610; SCY_0211.
DR HOGENOM; CLU_003674_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
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; 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; 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; Isopeptide bond; Membrane; Phosphoprotein; Repeat; SH3 domain;
KW Ubl conjugation.
FT CHAIN 1..1244
FT /note="Actin cytoskeleton-regulatory complex protein SLA1"
FT /id="PRO_0000349493"
FT DOMAIN 3..68
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 69..132
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 353..415
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 868..874
FT /note="1"
FT REPEAT 877..883
FT /note="2"
FT REPEAT 887..893
FT /note="3"
FT REPEAT 923..929
FT /note="4"
FT REPEAT 945..951
FT /note="5"
FT REPEAT 1003..1009
FT /note="6"
FT REPEAT 1020..1026
FT /note="7"
FT REPEAT 1031..1037
FT /note="8"
FT REPEAT 1048..1054
FT /note="9"
FT REPEAT 1065..1071
FT /note="10"
FT REPEAT 1084..1090
FT /note="11"
FT REPEAT 1129..1135
FT /note="12"
FT REPEAT 1155..1161
FT /note="13"
FT REPEAT 1170..1176
FT /note="14"
FT REPEAT 1185..1191
FT /note="15"
FT REPEAT 1200..1206
FT /note="16"
FT REGION 130..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..1205
FT /note="16 X 7 AA approximate repeats of T-G-G-A-M-M-P"
FT COMPBIAS 201..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32790"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32790"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32790"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32790"
FT MOD_RES 831
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32790"
FT MOD_RES 858
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32790"
FT MOD_RES 887
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32790"
FT MOD_RES 904
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32790"
FT MOD_RES 984
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32790"
FT MOD_RES 993
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32790"
FT MOD_RES 996
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32790"
FT MOD_RES 1075
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P32790"
FT CROSSLNK 471
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P32790"
FT CROSSLNK 548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P32790"
SQ SEQUENCE 1244 AA; 135703 MW; 383CE56A40C1F8AB CRC64;
MTVFLGIYRA VYAYEPQTPE ELAIQEDDLL YLLQKSDIDD WWTVKKRVIG SDSEEPVGLV
PSTYIEEAPV LKKVRAIYDY EQVQNADEEL TFHENDVFDV FDDKDADWLL VKSTVSNEFG
FIPGNYVEPE NGSTSKQEQA AAAAEAPAAT PAAAPASAAV LPTNFLPPPQ HNDRARMMQS
KEDQAPDEDE EGPPPAMPAR PTATTETTDA TAAAVRSRTR LSYSDNDNDD EEDDYYYNSN
SNNVGNHEYN TEYHSWNVTE IEGRKKKKAK LSIGNNKINF IPQKGTPHEW SIDKLVSYDN
EKKHMFLEFV DPYRSLELHT GNTTTCEEIM NIIGEYKGAS RDPGLREVEM ASKSKKRGIV
QYDFMAESQD ELTIKSGDKV YILDDKKSKD WWMCQLVDSG KSGLVPAQFI EPVRDKKHTE
STASGIIKSI KKNFTKSPSR SRSRSRSKSN ANASWKDDEL QNDVVGSAAG KRSRKSSLSS
HKKNSSATKD FPNPKKSRLW VDRSGTFKVD AEFIGCAKGK IHLHKANGVK IAVAADKLSN
EDLAYVEKIT GFSLEKFKAN DGSSSRGTDS RDSERERRRR LKEQEEKERD RRLKERELYE
LKKARELLDE ERSRLQEKEL PPIKPPRPTS TTSVPNTTSV PPAESSNNNN SSNKYDWFEF
FLNCGVDVSN CQRYTINFDR EQLTEDMMPD INNSMLRTLG LREGDIVRVM KHLDKKFGRE
NIASIPTNAT GNMFSQPDGS LNVATSPETS LPQQLLPQTT SPAQTAPSTS AETDDAWTVK
PASKSESNLL SKKSEFTGSM QDLLDLQPLE PKKAAASTPE PNLKDLEPVK TGGTTVPAAP
VSSAPVSSAP APLDPFKTGG NNILPLSTGF VMMPMITGGA MLPMQRTGGF VVPQTTFGMQ
SQVTGGILPV QKTGNGLIPI SNTGGAMMPQ TTFGAAATVL PLQKTGGGLI PIATTGGAQF
PQTSFNVQGQ QQLPTGSILP VQKTANGLIS ANTGVSMPTV QRTGGTMIPQ TSFGVSQQLT
GGAMMTQPQN TGSAMMPQTS FNAVPQITGG AMMPQTSFNA LPQVTGGAMM PLQRTGGALN
TFNTGGAMIP QTSFSSQAQN TGGFRPQSQF GLTLQKTGGI APLNQNQFTG GAMNTLSTGG
VLQQQQPQTM NTFNTGGVMQ QPQMMTTFNT GGAMQQPQMM NTFNTGGIMQ QPQMMNTFNT
GGAMQQPQQQ ALQNQPTGFG FGNGPQQSRQ ANIFNATASN PFGF
