ID A0A317VL21_9EURO Unreviewed; 299 AA.
AC A0A317VL21;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 03-MAY-2023, entry version 15.
DE RecName: Full=Protein YIP {ECO:0000256|RuleBase:RU361264};
GN ORFNames=BO70DRAFT_389133 {ECO:0000313|EMBL:PWY73638.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY73638.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY73638.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY73638.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU361264}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU361264}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the YIP1 family. {ECO:0000256|ARBA:ARBA00010596,
CC ECO:0000256|RuleBase:RU361264}.
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:PWY73638.1}.
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DR EMBL; MSFL01000024; PWY73638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317VL21; -.
DR STRING; 1448321.A0A317VL21; -.
DR VEuPathDB; FungiDB:BO70DRAFT_389133; -.
DR OrthoDB; 1968062at2759; -.
DR Proteomes; UP000247233; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR InterPro; IPR045231; Yip1/4-like.
DR InterPro; IPR006977; Yip1_dom.
DR PANTHER; PTHR21236; GOLGI MEMBRANE PROTEIN YIP1; 1.
DR PANTHER; PTHR21236:SF1; PROTEIN YIPF6; 1.
DR Pfam; PF04893; Yip1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361264};
KW Reference proteome {ECO:0000313|Proteomes:UP000247233};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361264};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361264}.
FT TRANSMEM 165..183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361264"
FT TRANSMEM 190..213
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361264"
FT TRANSMEM 219..244
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361264"
FT TRANSMEM 251..274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361264"
FT TRANSMEM 280..298
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361264"
FT DOMAIN 161..294
FT /note="Yip1"
FT /evidence="ECO:0000259|Pfam:PF04893"
FT REGION 29..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 299 AA; 32228 MW; A807E9DC978F94DA CRC64;
MASAHAHYPH EDLPDDESIL DDDVIDADDA IDADDPLNDT SDTAPLRGNI QPEPSSSRAA
NLSGNYLTSS IPGEDRRATQ STIDETVWET VSRDLRAVWE KMRQVLWPKY LIGGMLQRGG
GGIGAAERGE ATGFGGGLRN MVGRWPDADV VLQGGMSEGL RDWDLWGPLI FCLLLSMFLS
MRAKEDQASL VFSGVFSIVW IGEAVVTLQI KLLGGTISFF QSVCIIGYTL FPLVIASVLS
AFGLPTIARI PVYLVLIAWS LAAGVSILGG SGVLRNRVGI AVYPLFVFYI AIGCLCFIS
//
