SLA1_VANPO
ID SLA1_VANPO Reviewed; 1202 AA.
AC A7TKW4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1;
GN Name=SLA1; ORFNames=Kpol_1025p40;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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 {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}.
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DR EMBL; DS480410; EDO17119.1; -; Genomic_DNA.
DR RefSeq; XP_001644977.1; XM_001644927.1.
DR AlphaFoldDB; A7TKW4; -.
DR SMR; A7TKW4; -.
DR STRING; 436907.A7TKW4; -.
DR EnsemblFungi; EDO17119; EDO17119; Kpol_1025p40.
DR GeneID; 5545314; -.
DR KEGG; vpo:Kpol_1025p40; -.
DR eggNOG; ENOG502QQC3; Eukaryota.
DR HOGENOM; CLU_003674_0_0_1; -.
DR InParanoid; A7TKW4; -.
DR OMA; PDWILVG; -.
DR OrthoDB; 1483210at2759; -.
DR PhylomeDB; A7TKW4; -.
DR Proteomes; UP000000267; 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; Membrane; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1202
FT /note="Actin cytoskeleton-regulatory complex protein SLA1"
FT /id="PRO_0000349491"
FT DOMAIN 3..70
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 71..132
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 380..442
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 133..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1202 AA; 131240 MW; B2073CCFE3097335 CRC64;
MTVFIGIYKA IYNYEPQTPD ELTIQEDDLL YLLEKSNVDD WWTVKKRVIG SDIDEPAGLV
PSNYVEVADV ISQVKAVYDY HEVQNPDEEL VFNENDTFDV YDDKDPDWIL ARSISTNQFG
FIPGNYVEPL NAETGSAVPP SQPAAAAALP PPIATSATSP PAPALTAIDI STLPPPPQHS
SKTNAQASDS GNRDYADKDL PDLPPNKPSR SNTETNEDDY YDAPPTKPAR PNSTSNEQDT
RQKARSRTSY YDQHYEDDAE DYRSSQRDDD YNDSEPSGEL RTWNVAEIEG RKKRKAKLSI
GNNRLFFSPQ KGSPQDWSVD KLISYDNEKK HLFLEFVDPY KSLELHTGDN DTCKEILSVI
GEIKGASRDP GFKEVEMASK SKKKGNVLYD FTAESNDELT IKQGQVVYII NDQKSKDWWL
CELIDSGKRG VVPSHFIEPI QEKLTSSHTG GLFKSIKKFA KGGKSSKASD DAYSGSWEDD
GMEGSTERRS RSGSYSTRKR ASSTTSKKEL PNPKKSRIWE DRSGTFKVEA QFIGCKEGKV
HLHKANGVKI AVAAEKLSDD DLVYVERVTG FSLDKYKVRG SGTSSSRQDP RESERERRRR
LRENDEKDRD RRLRERELNE LQKARQLLDN ERTKLQEQNE QPPSKPPRPS SGMGNRSRSQ
STKDNYDWFE FFLNSGVDVS SCQRYTSNFE KERITEDMMV DINDSILRTL GLREGDIVRV
MKYLDKKLGR DVSPQTAVVA GGMFSEADGS LKNNNSENQS SVGQQLLPNN PDLVSNTPID
DDTWTVRPAA KSEATLAPKT AEFTGSMQDL LDLKPLEPKK TEQLPIANLA VTESVVPEPN
LKNLEPVRTG NVVQKPLANT LTGGATLVPL DPFKTGGNNV LPVTTGFVMM PFATGGAMPI
QRTGGIIVPQ TTFGTNAAGG IMPAQITGGL IPVATTGGLM PQTSFGVTPV ANVVPLQRTG
GAVMPIATTG GANILPQTTF NLPPSGTVLP IQRTANGLMA ANTTGGMMPL NTTGGMMPLN
TTGGMIPLNT TGGMMPMNTT GGVMSLQRTG GMMPQTSFGT QQMTGGAMNM MPQISFGAQQ
MTGGAMNVFP QTSFGAQQMT GGAMQNPNMG TMQNPNMGVM QNPNMGAFQP KSQFGMTLQR
TGGAMAQPIM DAGVTGIAQG VQNMSMAQPL QNQPTGFGFG NGPQQPVQAN IYNASASNPF
GF
