ID D8PPF2_SCHCM Unreviewed; 1145 AA.
AC D8PPF2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
DE Flags: Fragment;
GN ORFNames=SCHCODRAFT_102521 {ECO:0000313|EMBL:EFJ02963.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFJ02963.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
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}.
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DR EMBL; GL377302; EFJ02963.1; -; Genomic_DNA.
DR RefSeq; XP_003037865.1; XM_003037819.1.
DR AlphaFoldDB; D8PPF2; -.
DR STRING; 578458.D8PPF2; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02687478; -.
DR eggNOG; ENOG502QQC3; Eukaryota.
DR HOGENOM; CLU_006319_0_0_1; -.
DR InParanoid; D8PPF2; -.
DR OMA; FMAQGED; -.
DR OrthoDB; 2906837at2759; -.
DR Proteomes; UP000007431; 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; cd00174; SH3; 2.
DR CDD; cd11773; SH3_Sla1p_1; 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 PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR PANTHER; PTHR15735:SF20; PROTEIN NERVOUS WRECK; 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 Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000007431};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 73..134
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 350..410
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 266..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..840
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..916
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1145
FT /evidence="ECO:0000313|EMBL:EFJ02963.1"
SQ SEQUENCE 1145 AA; 122364 MW; 3A956614ECC786B3 CRC64;
MPDELEEYLA VLKATYDYDA TEPDECTIKE NQLLLLLQRV DDDWWKIKVK GESADDDETP
SGMVPAAYVE PADRTSVVKA LYDYEASAPG ELSIKEDEIL DVFSTADDWL LAQTRRDGGK
AGYIPANYVE AASDDAEAEA EPVATPPPPA PAPAIIVPDS PPKPAYVDPE ERVASTKAES
AAKADAIKTW AISEVDSKNK KKKGTLGVGN GAVFFASESD KTPVKKWPTS HITHISTEKS
KHIHLDIAGD EPVSLHFHAG SKDTADEIID KLETSRAIAT EAEAGGKEEE EAEEEAPKPT
RAVPPASLGL GGSSGNRKPS VHFSPLSPQV IPPREEASDD EDEDGHVNGA GGEPATALYD
FEADGEDELS VAAGEKLTII EKDGDEWWKC RNAKGAEGVV PASYLEVATG SAALSGSAVE
DDDEEEEETS AKDAAAEQAE KDRIREKERQ LEERERELKR KEEAQRRAEQ AAQKAEEERR
KRHEARDAHK KTQPNERVPR PSSAAARPSA ERERPPPDQT RIWHDRTGQF RVEAAFLGVN
NGKFRLHKVN GVIVEVPQEK MSAEDVRYVE KLTRGNNRKS RGPPGPNDDD DVPLAMTAPK
RASVPPPQQP KKPRVDWFEF FLSAGCDIDD CTRYAASFER DKIDEAILPD ITESTMRSLG
LREGDIIRVK KLIDQRKPKV EKPSAALEEQ MRKDEELARR LQEEEQQGRK PAPNLFSGPG
GALKNPAKPP RRGRPEPSKT LPPTFVGADG IAAASARVGS PAQTTSPVSA PPRTSSAGAS
AAPATQPSGF DDDAWTVRPS STVADRTPSA PPTSTPATAP PPAPAPPPVP APPVAAPAPA
PAQPAANLAN KTESDIFDQL ARLSELRKTQ SPAAATPPPA VAPTPPIAAQ PTGYQQGMGM
GSSPSPIGQL QPQNTAVPYN GPRGPFAPVP ANQGLLQPLI PTQTGYNSFV PTRPTSALQG
SPFAGGVPAS QFLASQPTGF QPMQPQPTGF QPMQSQPTGF PGMQSQPTGF PGLQPQATGF
PGMQQQQPMM AQPTGMPMGG SPFQGGGFGG GVQTNPTGFN PGMSMGNFNN GMASPPPLPQ
QQSPQKDTSP ANIFAQMKSG TFASENAPQD ASKYDALRPQ QPMMAQPTGW VGGGFQGGYG
MGYQR
//
