ID A0A161U9G2_XYLHT Unreviewed; 1214 AA.
AC A0A161U9G2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
GN ORFNames=L228DRAFT_267833 {ECO:0000313|EMBL:KZF23875.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF23875.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF23875.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF23875.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
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; KV407457; KZF23875.1; -; Genomic_DNA.
DR RefSeq; XP_018189430.1; XM_018335036.1.
DR AlphaFoldDB; A0A161U9G2; -.
DR STRING; 1328760.A0A161U9G2; -.
DR GeneID; 28900173; -.
DR InParanoid; A0A161U9G2; -.
DR OMA; FMAQGED; -.
DR OrthoDB; 2906837at2759; -.
DR Proteomes; UP000076632; 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:SF19; ACTIN CYTOSKELETON-REGULATORY COMPLEX PROTEIN SLA1; 1.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 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:UP000076632};
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 378..440
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 128..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..834
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..892
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..986
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1176
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1214 AA; 130082 MW; 53203C3731A08D38 CRC64;
MGFVGVYTAI YDYSPQGENE LSIKEGDLLY ILEKSTEDDW WKAKKKAGDD EEEEPLGLIP
NNYVEEAQPT ANAKALYDYT RQTDEELSFT EEAILSVYDT SDPDWTLIGL NGEYGFAPAN
YIEISESAPR HPPASVVEQQ PDHTRSASLS SAGSPLQSPA AALADIIHRK ASEPAIAAQS
PAAPQYSSMS PPSRPADYTP EESDDEVTPP APVLPQRPQS LQISPPSHYT KPLPLEPPGV
VASPPYNRLS HRHVDEAAYP SPGGYHLYNI NEMVSAMGKR KKLPTTLGIN IGTGTIMISP
EKSRDGPQQE WTADKLTHYS IEGKHVFLEL VRPSKSVDFH AGAKDTAQEI VAALGDMAGA
VRAEGLREVI AAGSGTGSTH KKGQMLYDFM AQGEDEVTVA VGDEVIVLDD SKSEEWWMVR
RLKNGKEGVV PSSYVELTGT TSVSNPSTTG INAGRSAVEQ NRLEEERLAK EAIRSSRKRG
ESDPRVSEVG PGMRLPARGS SLAGHSDGNE LSTQRSRHSS RSDAKAPSTS KPKPDASKTR
TWTDRSGSFK VEAEFIGLKD GKIHLHKLNG VKIAVPVPKM SVDDLEYVER VTGVSLDEDK
PLSDIRHRNL QKSGDRGKAR ITSAAGASVG PVKPEYDWFD FFLSCGVGPH LCERYAANFV
KDSMDEGILP DITPEVLRTL GLKEGDILRV MKYLDNKFGR AAGRTKRNVS FGGAEVIGKD
DEGEDEADGA ASGGLFSGPG GALRNNTRKG RPAPPVQTND VVDEKVFEQK KEPNLDTKKA
PTPLVSAPSA PKRANTGFDD DAWDVKPSKQ QPQPPARDAT PPPATQPAAQ PAPPQQPTLT
GSMKELSLLS PPLEPAVVHT TGAQQAAPPP APVPQTQTQA IPPAPQPPQP QAQVNVANPS
FFAQLGQQKT GPQFQSSVPQ PGPVPTFAPQ QTGFSVDSPS QPMPPRQRPQ PPPAAMAAGS
LVPPPPARPF SAPQNPSQPN GFGPPPLQPQ LTGYQGAAGF QPSVAPPGQS LNEINQQKLQ
QQFAQQQIQP QMTGFGQQQA GVGPFMMQQQ QPGFGQPVQA QPTGFQQAQP FLNGQQTGSP
FANPPPQQPA GFQAMLSQPT GFQTSFSPQP IQQQQPQPPQ LQPQMTGSVN SFLPPALQPQ
QTGVSGFGGQ GFGQVPPPPP VPQPPPMQPL QPQKTGPAPP VRFGVAPETK RLTPQPTGRK
ANLAQATPQN PFGF
//
