ID A0A395HPF8_ASPHC Unreviewed; 276 AA.
AC A0A395HPF8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Protein YIP {ECO:0000256|RuleBase:RU361264};
GN ORFNames=BO97DRAFT_427050 {ECO:0000313|EMBL:RAL09842.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL09842.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL09842.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL09842.1,
RC ECO:0000313|Proteomes:UP000248961};
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 (FEB-2018) 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}.
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DR EMBL; KZ824300; RAL09842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395HPF8; -.
DR STRING; 1450537.A0A395HPF8; -.
DR VEuPathDB; FungiDB:BO97DRAFT_427050; -.
DR OrthoDB; 8905at2759; -.
DR Proteomes; UP000248961; Unassembled WGS sequence.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR InterPro; IPR006977; Yip1_dom.
DR InterPro; IPR039765; Yip5/YIPF1/YIPF2.
DR PANTHER; PTHR12822:SF2; PROTEIN YIPF; 1.
DR PANTHER; PTHR12822; UNCHARACTERIZED; 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:UP000248961};
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 125..145
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361264"
FT TRANSMEM 157..181
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361264"
FT TRANSMEM 193..214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361264"
FT TRANSMEM 220..241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361264"
FT TRANSMEM 253..274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361264"
FT DOMAIN 105..268
FT /note="Yip1"
FT /evidence="ECO:0000259|Pfam:PF04893"
FT REGION 49..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 276 AA; 30284 MW; B0A33F892A62CF59 CRC64;
MANRGYDVVV DVDAEGDLGH TDLQEDLEFH HSNFEHDQRS AKMQAASTPF LSGGGGVGGS
STSRGGRDRS PGGTPTKHTW WTIHYYAQYF DVDTNEVLRR CMATLYPRNN FLDVLEGNAD
LYGPFWIATT VVVILFLTGT ISQWLSNNDD AHFAYDFTLL SGAAGLVYGY TGVIPIALWG
LLKWFGSSSA ELVEAWALYG YSNLVWIAVA LVSWSPLTAL NWALVGVGFG WTVFFLLRNL
YPVLSATDAK ASKILLVLVV LLHAGFALAI KILFFA
//
