ID S7S0G1_GLOTA Unreviewed; 1162 AA.
AC S7S0G1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
GN ORFNames=GLOTRDRAFT_136140 {ECO:0000313|EMBL:EPQ59209.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ59209.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ59209.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ59209.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; KB469297; EPQ59209.1; -; Genomic_DNA.
DR RefSeq; XP_007862260.1; XM_007864069.1.
DR AlphaFoldDB; S7S0G1; -.
DR STRING; 670483.S7S0G1; -.
DR GeneID; 19303475; -.
DR KEGG; gtr:GLOTRDRAFT_136140; -.
DR eggNOG; ENOG502QQC3; Eukaryota.
DR HOGENOM; CLU_006319_0_0_1; -.
DR OMA; FMAQGED; -.
DR OrthoDB; 2906837at2759; -.
DR Proteomes; UP000030669; 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 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 PANTHER; PTHR15735:SF19; ACTIN CYTOSKELETON-REGULATORY COMPLEX PROTEIN SLA1; 1.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000030669};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 77..138
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 342..402
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 297..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..851
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1162 AA; 124305 MW; 678F7B68ECCFB0B0 CRC64;
MSEPESYLAV LRASYDYEPQ AEDEIEIKEN QLLFLLDKTD NEHVPIVVWW KVKCKTDNPD
DEGPAGLVPA AYVEEAEHVA TVKALYDYEA TSAGELTVKE DEVLLVFAKE EDWWLVQRKS
GEGGAGYVPA TYVEETTDDA AAASPPAVPS IANIVVPPMP PRPTSTYVDP ADRVAASKAT
ADDIQTWSVS EVDKKGKKKK GTLGVGNGAV FFASESDKTP VQKWQTAAIS SSKIDKSKHI
LIEISDPPTS LHFHAHSKDV AEAIVAKLES SKAISAPAAP PSPPAPAERV SPKVHFAEEE
PEVIPPREPS EDGYEEPAQH EEPEEVVEVE EPATAATPEV DGEGEIAVAL YDFTADGEDE
LSVAEGEQLV VLEKDGDEWW KCRNAHGGEG VVPAQYLELK GGTAVAAPAE EDDTAAEEAA
AAQAEAERLE QERIERERAE KAALEREAKQ RAQAAAAAAD AERKRKEKEK EKERERKERE
AEEERKKVAA EQERARRSQE VEQRRTSSES PARTKSAQRD SAAGRSSTEK RGPPPEKCRI
WHDRSGQFSV EAALLAYQNG KLRLHKTNGV IIEVPSEKMS AEDMKYVEKL MGKKSGSRQS
STPLSEDDEP LAVRRQSLQP PATPQRNPPP KKGPTIDWFE FFLNAGCDVD DCTRYALSFE
RDKIDEAILP DITESTLRTL GMREGDIIRV KKAIAQRQPK PAQSNDAAMQ DQLRKDEELA
RALQAEETGG SRKSSSPAPN LFASGPNGAL KNVRRGRPQP SKSLPPSSVD LNAISSASDQ
IQRTGTPGSS SSTPLQPPAR SSSAAPVVSG FDDDAWTNRP SSTKPVATAT PASPPAPPAP
PAPPASDPVP VRAPSAPVTN NAQSQNTGGS GSNLAKTTES DIFEQLSRLA ELRTKSPPSS
YASTPVGNNS MLGSPAPGIT PSASYQSGLG MRSSPAPMGQ HLQSQQTGIL PPPQQQNGPR
GPFAPVPANQ ALLQPLIPTQ TGATGFVPTR PASATSPFQP QPQQPSFLNT QPTGFPGPSP
VLSQPTGFPN QAPMMSQPTG FLTQGPLFSQ PTGFSGSFGQ APTFQNKSGF GMPQSAPNGF
SGFGQAASPP PAPNGGLAVK DTSPANIFAQ MKSGTFASGN DAGNPQPADK YDALRPAPPL
TMQPTGWGFQ TNGFQGYTGY QR
//
