ID A0A1F8AHC5_9EURO Unreviewed; 1681 AA.
AC A0A1F8AHC5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1 {ECO:0000256|ARBA:ARBA00020357};
DE AltName: Full=High osmolarity signaling protein SHO1 {ECO:0000256|ARBA:ARBA00016255, ECO:0000256|ARBA:ARBA00017350};
DE AltName: Full=Osmosensor SHO1 {ECO:0000256|ARBA:ARBA00029697, ECO:0000256|ARBA:ARBA00030785};
GN ORFNames=ABOM_000334 {ECO:0000313|EMBL:OGM51136.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM51136.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM51136.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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:OGM51136.1}.
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DR EMBL; LYCR01000001; OGM51136.1; -; Genomic_DNA.
DR STRING; 109264.A0A1F8AHC5; -.
DR OrthoDB; 2906837at2759; -.
DR Proteomes; UP000179179; Unassembled WGS sequence.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-UniRule.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
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 GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:UniProtKB-UniRule.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:UniProtKB-UniRule.
DR CDD; cd11773; SH3_Sla1p_1; 1.
DR CDD; cd11775; SH3_Sla1p_3; 1.
DR Gene3D; 2.70.130.10; Mannose-6-phosphate receptor binding domain; 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; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR012913; OS9-like_dom.
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; PF07915; PRKCSH; 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; SSF50911; Mannose 6-phosphate receptor domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 3.
DR PROSITE; PS51914; MRH; 1.
DR PROSITE; PS50002; SH3; 2.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1681
FT /note="Actin cytoskeleton-regulatory complex protein SLA1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009534866"
FT DOMAIN 160..307
FT /note="MRH"
FT /evidence="ECO:0000259|PROSITE:PS51914"
FT DOMAIN 542..609
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 934..996
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 63..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1023..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1241..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1565..1681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..693
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..770
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1409
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1479
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1642
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1667..1681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1681 AA; 183773 MW; C19C25C93AC84880 CRC64;
MGRRNRIVAS LLTLACATST ALANKKVFNI HDDLLAFPQY QVLFPDEYVL DSHAKELLQT
QSSPPVYDDQ QGNSLQKPQI PLKPRTDESQ EHSARQEGGP QLTYEELTLQ GQRFLCQIPH
VERDEMGQTN RTKDANETDE KQELARATDR GLELLSEMEG KCMYYVSGWW SYSFCYKKQI
KQFHALPSGS GIPNYPPMED PATHSFILGR FPRGSDEEDD SEAERKKTAE TTTATTTDVA
ELQTKGGSRY LVQRLEGGTK CDLTGKNRKI EVQFHCHPQS TDRIGWIKEL TTCSYLMVIY
TPRLCNDVAF LPPQQEELHS IECREVLSPD QVPDWEAMRQ YHLAQRLVES SATTSEFPIV
GDIEVGAKKL VGTEGKEIEK GRVASAGEEK VEVVAKRENG EVLQLPKVDL EKLGLDPEKI
ETLKTRLEEL AQGKDWTLEH VTANGERGLR GIVDTDEDEE EEETGTKPGA KSEDHGTTGK
PHEKAPTEKE VPEVEVSEAK PKDEPKVEEP PAEDAEEGSE EIFKDELRNP IPVCQLTVPT
MGFLGVYTAL YDYHPQAQGE LELREGDLLY LLESNNEDDW WKAKKKAEHD DEDEPEGLVP
NNYIEEAQPI HAAKALFDYT RQTDEEVSFS EDAELVVYDI SDPDWTLVGV SGDFGFAPAN
YIEIAEQAAH APATSSVPSP PAEAAPPTLP QRPTAAPIEE ASSPVSSSPI GTVQNPAAAA
IADIIHKQHA EPEATRAVPP PPQPQPSYEP ELSYQREPSP PPPALPQRPP SQQMSPRVES
PRSPGLPLRP PQITLAQEQD TKGHVKESPP YNRVGPAPRS PSGYHIYNVN EMVEVMGKRK
KMPTTLGINI ATGTIFISPE DDGEEQEWTA DKLSHYSIEG KHVFVDLVRP SKSIDFHAGA
KDTAREIVAA LGEISGAYRA EGLREVIAAG SSGGGQKKGQ ILYDFVAQQD DEVGVSVGDE
VIVLDDTKSE EWWMVRRVKN GKEGVVPSSY VEITGYASSS QPSGVDSGLS AVERNRLEES
RLAKEALRKS RTDSIDSPRA EHHKRDSRSS QKSKPDPTKT RQWTDRTKTF TVDAQFIGLQ
DGKIHLHKMN GVKIAVPIPK MSIQDLEYVE KMTGVSLDED KPLSDIKRRS TLREAEKPRP
SAENKRSESA GASFQQSDYD WFDFFLKAGV GPHQCERYAQ NFTKDSMDES ILPDITPEVL
RTLGLKEGDI LRVMRHLDTM FSRTGAKSKL RNVSFGGEEV ISNGEDSGGL FAGPGGVLRN
NTRKGRPAPA VQTGDVVDPK AFEQKEDSNH AEPKEASPTS AASEKPVQRG FDDDAWEVKQ
PKQTAPAPAP APAAAAPAAS TPTSPPAAAS PVTTQPTQQQ LTGAMADLSV LHPPLQPTPT
QPTPVSQPPL AAQAPPAIQP QPTAIPAPAP QQPQQTGATP GFFSQLGQPA QQPLQNPTQG
FSPQATGFQQ ASRPRPQPPQ AMGQNSLLPP PPPRPLSAPQ NFPQQQSSFG LPPLQPQLTG
LPQAGPPLAA PGQSLAELNQ QRFQQPLQPQ PTAFMPHNQF QNGLMPQPTG FQPQSQFGIQ
QQQQHQAGFQ GLAPQPTGFG FQAQPQQPMH TGINSVLPPS LQPQPTGING AGSMPYNTTS
PPPIPPIPQQ PTAAPLTPQK TGPAPPIRFG VKHDAPKKLA PQPTGLRANL AQATPTNPFG
F
//
