ID A0A175VRD6_9PEZI Unreviewed; 1167 AA.
AC A0A175VRD6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
GN ORFNames=MMYC01_209796 {ECO:0000313|EMBL:KXX73610.1};
OS Madurella mycetomatis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariales incertae sedis; Madurella.
OX NCBI_TaxID=100816 {ECO:0000313|EMBL:KXX73610.1, ECO:0000313|Proteomes:UP000078237};
RN [1] {ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA van de Sande W.W.J.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KXX73610.1, ECO:0000313|Proteomes:UP000078237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=mm55 {ECO:0000313|Proteomes:UP000078237};
RA Van De Sande W.;
RT "Madurella mycetomatis genome sequencing.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KXX73610.1}.
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DR EMBL; LCTW02000446; KXX73610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A175VRD6; -.
DR STRING; 100816.A0A175VRD6; -.
DR VEuPathDB; FungiDB:MMYC01_209796; -.
DR OrthoDB; 2906837at2759; -.
DR Proteomes; UP000078237; 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; cd11774; SH3_Sla1p_2; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000078237};
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 70..127
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 384..446
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 127..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..152
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..815
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..893
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..956
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1167 AA; 124505 MW; 66A65502D78AF3B4 CRC64;
MGFLGIYKAL YDYTPQAEGE LQIAEGDVLY VLEKSTDDDW WKAKKKATAE DDDEPVGLIP
NNYVEEVQPQ AKARALYEYT RQTDEELSFT EDAQLTVFDT SDPDWILVGH DGDYGFVPAN
YIEIGEGGGK EEEAEPPMPT PPPLPARTPS DVQSPPLPAR NQIPSEPSTP AAPASPPAPN
PATMIAGMMA ARAGSSQQPP APLDLPPRPQ YADDESEPEA KSPPLPARPR GDSHISIVEP
ARPSPPPEQR RIDYDSPRTP RTAPLTPGDF HMYNINEMVS IMGKKKKMPT TLGINLRTGM
ILIAPEHAQD GPSMEWTADR MTHYSREGKH VFMELVKPSK SIDFHAGAKD TAEEIVTMLG
ELAGAVRAEG LREVIMAATT QKPIQQKKGV VMYDFMAQGE DEVTVGIGDE VIVLDDTKSD
EWWMVRRVKN QKEGVVPSSY IEVTGILDTP VSAGTSGVNA GKSTIEQNRM EEARLTKEAI
KAGQREDQRE RDKARSHEVG PGLLLPERNS SLLARNSNTG GQQRSRRENG RTEASGSSKS
NGKSKPDPSK IRTWTDRTKS FTVEAQFLGI KDGKLNLHKT NGVRIAVPVA KMSLEDLEYV
ERMTGISLDE DKPLSDLKKR SGGDSSRSGS GVKVGASVQP KKPDYDWFQF FLSCDVQPGL
CERYAQAFAR ESMDESVLPD VDATVLRNLG LREGDIIKVT RFLDAKYCRG KKATGADDEA
TGGLFSGPGG ALRNNTRKGR PAPPVETNNT VDPNAFSQQK ASATGEAKTP SPTSATTPAT
TKPTGGFEDD AWDVKPSKTS EPATQPPPAP AAAPAPAASP AAAAPAAAPA PSTAKLTGSM
QELSLLTQPL TPEKVQSPVS VPPALNLAPA SATSAAPTSA PAQIPQPTGA TPGFFSGMQP
PAVNGTQQQL PQAVARQRPM APQYTQGQGG LMPPPPPSRP LSAPQSAHPS AFAPPPLQPQ
MTGYQTQVAP PGQSLNEMAQ ARMQQQYAQM QQQQQQPLMP MMTGMPGPAG QFMAPQPTGM
LGASGPGMQM GLQPQPTGFN PMGQFPQQQQ IGGGLPAPLE PQRTAMPTPT GPMGVGMGMN
MGMGGMNPLG MQQPPQPMQP QPTGFGTSTP PATGGLHAPM QPLVPQKTGP PPPVRFGVTE
GPKKLAPQPT GRRANLAAAT PDNPFGF
//
