ID A0A0D2E6K8_9EURO Unreviewed; 1158 AA.
AC A0A0D2E6K8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
GN ORFNames=PV05_09818 {ECO:0000313|EMBL:KIW51063.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW51063.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW51063.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW51063.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847322; KIW51063.1; -; Genomic_DNA.
DR RefSeq; XP_013311648.1; XM_013456194.1.
DR AlphaFoldDB; A0A0D2E6K8; -.
DR STRING; 348802.A0A0D2E6K8; -.
DR GeneID; 25331726; -.
DR OrthoDB; 2906837at2759; -.
DR Proteomes; UP000054342; 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; 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 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; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342};
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 371..433
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 129..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..943
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..839
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1025
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1111
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1158 AA; 125456 MW; C69A1A1F33513233 CRC64;
MGFVAVCTAI YDYQPQSTGE LEIKEGELLY ILEKSTEDDW WRAKKKAAAD DEDEPEGLIP
SNYVESAKPT HTAKALYDYT RQTDEEVSLT EDATLDVYDT SDPDWTLVGI GDDFGFAPTN
YIEISDAARA SPTIPSSRQS APVALEPEAP TSPVSPARSV DSPAANLARV LGGQAPTSPT
AARPIPSPPR VQFTPEASDD EESAPALPQR PPSQSIPAPI SYSEHDDEAL GVLPSPPYNR
AIGRPDDEDA PIRSPGGYHL YNINEMVSAM GRRRKMPTTL GINIATGTIM VSPEKSRDGP
AQEWTADKMT HYSIEGKHVF LELVRPSKSL DLHAGAKDTA EEIVRALGEI AGAHRAEDSI
RDVIEAAAGG GSQKKGQVLY DFMAQGEDEV TVGVGDEVII LDDTKSEEWW NVRRLKNGKE
GVVPSSYIEV TGFVNIEPPS RSGLNAGLST VEQNRLEEER LAKEAARADR ARQQVDQTRS
RGEVGPGMQL PQRGSSLADD QTSRRDRREK DDRKKRSKPD AAKVRTWTDH SGTFKVEAQF
LGVAEGKIHL HKVNGVKIAV PVTKMSPEDL AYVEKVTNES IEEHIPVADL IKMRRRSQQS
SEQSKHRSGA SIEHRAPEQP KVPDYDWFDF FLKAGVGPHQ CERYSQAMIR DSMDETVLPD
ITADTLRTLG LKEGDTLKVM KYLDQRFGRT RSASVNGTNG ETTAGGIFSG PGGALHNNTR
RGRPEANRQT TDVVDPDAFT NKESDRPSDA KATPLTEAPP RKPEGGFEDD AWTVKQPTQT
AAPPAPKPPT GAIRDLSLLD APLVPTPAQP STPAVSQPPP APAQPQPPTV QPPPATTPAQ
QPQQTGANPQ FFSQLNQQQT GIPTQQTGFQ PQQFNPPRQR PAAPQQSFTG AGLLPPPPRP
TSAPQNPQQN QFGLQPLQPQ LTGIPVTSAM QAPPGQSLND LTQQRLQQQY QQFQLQSQPT
GLGQFGLAPQ PTGFQQPQPF GQFQQPYING NATGSPFADP RPSFQPQPTG MPFQQSPPPG
GINSILPPAM QPQRTGFASP MQQTQSNGFG QGQGIQPQQT GFPQAQPLQA QSTGFQQPLQ
SQATGFGQLP QPNGFQSFSP PPVPPIPQQH SIAPLQPQRT GPAPNIKFGV SPAKKLTPQP
TGRRANLANA TADNPFGF
//
