ID A0A0S7DWD8_9EURO Unreviewed; 1230 AA. AC A0A0S7DWD8; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 13-SEP-2023, entry version 33. DE SubName: Full=Meiotically up-regulated gene 190 protein {ECO:0000313|EMBL:GAQ08249.1}; GN ORFNames=ALT_008568 {ECO:0000313|EMBL:GIM40081.1}, ALT_5570 GN {ECO:0000313|EMBL:GAQ08249.1}; OS Aspergillus lentulus. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GAQ08249.1}; RN [1] {ECO:0000313|EMBL:GAQ08249.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GAQ08249.1}; RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.; RT "Aspergillus lentulus strain IFM 54703T."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:GIM40081.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM40081.1}; RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.; RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus RT lentulus IFM 54703T."; RL Genome Announc. 4:e01568-15(2016). 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:GAQ08249.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BCLY01000009; GAQ08249.1; -; Genomic_DNA. DR EMBL; BCLY01000009; GIM40081.1; -; Genomic_DNA. DR STRING; 293939.A0A0S7DWD8; -. DR VEuPathDB; FungiDB:TMP_alenIFM54703_5686; -. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:InterPro. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR CDD; cd04041; C2A_fungal; 1. DR CDD; cd04052; C2B_Tricalbin-like; 1. DR CDD; cd21676; SMP_Mug190; 1. DR Gene3D; 2.60.40.150; C2 domain; 2. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR037767; C2A_Mug190-like. DR InterPro; IPR037765; C2B_Tricalbin. DR InterPro; IPR031468; SMP_LBD. DR PANTHER; PTHR47348; MEIOTICALLY UP-REGULATED GENE 190 PROTEIN; 1. DR PANTHER; PTHR47348:SF3; MEIOTICALLY UP-REGULATED GENE 190 PROTEIN; 1. DR Pfam; PF00168; C2; 2. DR SMART; SM00239; C2; 2. DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2. DR PROSITE; PS50004; C2; 2. DR PROSITE; PS51847; SMP; 1. PE 4: Predicted; KW Lipid transport {ECO:0000256|ARBA:ARBA00023055}; KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 206..222 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 377..395 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 249..476 FT /note="SMP-LTD" FT /evidence="ECO:0000259|PROSITE:PS51847" FT DOMAIN 474..601 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT DOMAIN 662..807 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT REGION 1..99 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 701..723 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1042..1192 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..31 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 36..68 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 79..99 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 703..723 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1042..1061 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1092..1106 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1126..1173 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1230 AA; 138327 MW; 4DC5E4ECE637EAF3 CRC64; MAPNPNSKGG STSPQQHRVG EPWSGTNPVP TISKFMERLR SEEQQQKEYE EAQTARERQT EGGASPHQPR KRAKGKTRKV RDPVTGKDME VEDQDEHSMD TVKDPKLVVP NANLGKPTEV KTDAHQDLSE YKENQDVTAP PDPIAEGTTS DVPIHGEKTN ILFHPTPTIS YKPMFDQLEK RATGVCLGLF IGVLFLGRVF GGSLWGLIPL ACCTTTGIWL WMKEVIRSGR EMEWSSEQLR GQTATANLLP ESVEWMNTFL GVVWGLLNPD MLAPVADTIE DIMQASAPSV VENVRIAEID QGNNPIRILS MRALPDEHVQ QLKDNIREEN KKNKDPQEAA AAEEGGSYYN LEASFAYHAK PSGQSASSKA RNMHMQVIFF LGIQGLFGVP FPVFVELIEM VGTIRLRLQM MPEAPFMKEV TYSLVGIPHI RAGCMPMVRH GINILNLPLI SNFVNYAIGA ACSLFAAPKS MTMDLGMLLK GDDIIKETQA IGVMWVRIHR AVGLSKQDKR GTHGGGSDPY INLSFSKYGK PMYCTRVITD DLNPIWEETT ALLVTPELIK VDENLSVELW DSDRNTADDI VGKVELPIRE MLAHPGCMYP QVSKLQGLND GSEMPGELHW EVGFFGKPKL RPELRTDGKR KDLPENLQDI PEFQDEKGTI ITEEEDAITH TPPDPLWPSG ILSVVVHQIV HLQLANIKGT TGSRKGREYE PAKNYGEGTE EEGKDLPTSY CKIMLNDELV YRTRAKALSS KPIFNAGTER FVRDWRSSMV TVTVRDQRYR EHDPILGVVQ LKLTDLFQKS SQVTRWYPLD GGVGFGRIRI SLLFRHVETK LPPNMLGWDV GTFHFVSDKL TLQGFNHRAK IKLRTGGSSG KIPRGQCHIE GNNSYYDLTN EDFRRSIRLP VKHRYRSPVV FELHTQGKHG AAGYAVLWLQ HLVDNEETEI DLPIWSTKNG SRLTQNYITE ENWKAKEVPG LEDLHEIGRL QLRGLFTPGI DDSHEHYVVD SNSRETFETW EACMAEGVRP HRITAEIPED VDKLHEQSLR AGRDVLKHSH PRERKRWIDK QGNDWSGAFG DDPAAYVDSK GRKIAEPGRD QPPQDPVNPP PKEVEPTGAA HPSDYEEDSS ESSSEEDAQP EQQQEQQQEQ QQEQQQQQRQ PSEPHTITAQ PSEASSSNAP SKRAAKRSEQ RQQRGLMQWK PARNAVFARD EAKYALRKVK HKFTGSLSGR EPDIETETGQ //