ID G3BC50_CANTC Unreviewed; 1163 AA.
AC G3BC50;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
GN ORFNames=CANTEDRAFT_128413 {ECO:0000313|EMBL:EGV60787.1};
OS Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS 10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN [1] {ECO:0000313|EMBL:EGV60787.1, ECO:0000313|Proteomes:UP000000707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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; GL996528; EGV60787.1; -; Genomic_DNA.
DR RefSeq; XP_006690001.1; XM_006689938.1.
DR AlphaFoldDB; G3BC50; -.
DR STRING; 590646.G3BC50; -.
DR GeneID; 18249303; -.
DR KEGG; cten:CANTEDRAFT_128413; -.
DR eggNOG; ENOG502QQC3; Eukaryota.
DR HOGENOM; CLU_003674_0_0_1; -.
DR OrthoDB; 2906837at2759; -.
DR Proteomes; UP000000707; 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; cd09532; SAM_SLA1_fungal; 1.
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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000000707};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 3..73
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 74..134
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 364..426
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 138..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 555..589
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 203..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1163 AA; 127035 MW; 64F1ED61FA86F163 CRC64;
MSLYIGVYVA LYEYQPQTDE ELSVTPDDIL YLLEKSQVDD WWKVKKRVLP VGDEEVDEPV
GLVPSNYIEP APTVKTCTAL YDYDKQTEEE LSFREGESFN VYDLNDPDWL LVGDAATGQS
FGFIPSNYVQ LNGDTVGAGS VPTPSQPSAV PIPGFAPPPQ HISRQVVQQP DPEPETYEED
AEEFNEAEPP LPSKPRPSQP SYEREVALDD DLPPPPMPSR PREDSRDAEI EEDLEAPIQE
HSFDGDFFKW LINEIDGKKK KAVTLAIGKG LIILKPTSPS PRKLRLRSSS SLDNEWRLKD
LTSFSSEKKH LFLEFKNPTT SVELHCGSKD VADAIMSILG DLKGAESAKG LREVEKASVP
STKGNKKIGR LIYDFKAQGS DELGCYEGDE VYIVNQEKSK DWWMCEHIDT GKSGVVPSAY
IEIVGSSNLD KLVDAPSRQK STTLSKSEAK KRQKQRHRDE REKIRERDRI EREKARASQR
STEKDVSPDK SMPNFHRVRT WIDSSGSFKV EAEFLGCIEG KIHLHKTNGV KIAVSATKLS
TEDLEYVEKV TGTSLESYKE QVLQQMAKRK AASEKKSDVS RDVKREERRS AMAVINDVAP
PQPTRPKASS TTQVSEPEYD WFDFFLTCGV DIGNCQRYTL NFNREQMDEN ILEDISPSLL
RTLGLREGDI IRVMKHLDEK LNRKKEEPTI SATPTGALFT EATGALKNNS TSEVSKVDAS
ALPAPSQAPA PSQAPAPSQP PTRSDNLMDD DAWAIKPAAR STEDLTKPQQ PQYTGSLQDL
VNIKPLEGGI NTNKPVPALP SEVTQASTGV PSATPLTPVR TGTIVSPQKT GTLVPVQRTG
GLVPVQRTGG FVPLQMTGGF VSAQPTGFIP ITAQPTGFVP IQATGISQQI TGFVPVQTGS
FSSMPPVSFG QPVLQTGTMT MPQTTFGQQL TGGFQVQAPQ PTGFAAMPQT SFGQMSVQRT
GPLVPAQRTG SSFPQNSFQP QSTFGQAISA PPTFNAQLTG GQPQFPQQSF PPQQTFQPQQ
TFQPQQTFGQ AQFQPQQTSF GQPSTSFGQP ATSFGQSATS FGQPQFGQNS FNNNMNQMTN
MFQNTGIAQQ PTGSFGQPPV SFNQASTSFG QPTTSFGSPS FEGFGALQAQ ATGSGFGNAP
LQAQATGKRA NLSAATPDNP FGF
//
