ID A0A3P6TGJ1_LITSI Unreviewed; 510 AA.
AC A0A3P6TGJ1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Post-GPI attachment to proteins factor 2 {ECO:0000256|ARBA:ARBA00016871};
GN ORFNames=NLS_LOCUS5642 {ECO:0000313|EMBL:VDK82203.1};
OS Litomosoides sigmodontis (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX NCBI_TaxID=42156 {ECO:0000313|EMBL:VDK82203.1, ECO:0000313|Proteomes:UP000277928};
RN [1] {ECO:0000313|EMBL:VDK82203.1, ECO:0000313|Proteomes:UP000277928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the lipid remodeling steps of GPI-anchor
CC maturation. Required for stable expression of GPI-anchored proteins at
CC the cell surface. {ECO:0000256|ARBA:ARBA00024944}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004653}.
CC -!- SIMILARITY: Belongs to the PGAP2 family.
CC {ECO:0000256|ARBA:ARBA00007414}.
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; UYRX01000436; VDK82203.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P6TGJ1; -.
DR STRING; 42156.A0A3P6TGJ1; -.
DR Proteomes; UP000277928; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.2100; -; 1.
DR Gene3D; 3.30.1490.490; -; 1.
DR InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR InterPro; IPR039545; PGAP2.
DR InterPro; IPR014898; Znf_C2H2_LYAR.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR12892; FGF RECEPTOR ACTIVATING PROTEIN 1; 1.
DR PANTHER; PTHR12892:SF11; POST-GPI ATTACHMENT TO PROTEINS FACTOR 2; 1.
DR Pfam; PF10277; Frag1; 1.
DR Pfam; PF08790; zf-LYAR; 1.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR PROSITE; PS51804; ZF_C2HC_LYAR; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01145};
KW Reference proteome {ECO:0000313|Proteomes:UP000277928};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01145};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01145}.
FT TRANSMEM 16..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 258..285
FT /note="Zinc finger C2H2 LYAR-type"
FT /evidence="ECO:0000259|Pfam:PF08790"
FT REGION 374..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 57847 MW; 59B863C203151A01 CRC64;
MALVGEEELL CISFRWFVLV TAGLPFTALF LCISLALALH LDESTRTHCG VVNYLPSVSA
AVASFSPERY VWRFFIALHS APRIVEALAF KNLLLTSPLR PLNDRIWFEV ACQLACFVNI
AGSLFLLLLT TASSVENHAL HKISFAGFAL CSIIYMLIAT SLFQYSGRRR TSSLGEKSFQ
YKVLMCSISA LSLLLAVYFF QRHNTYCEPG IYTIILEGFG LITRNIVIMV FFSCDTCSEA
LKKNQVIKHG FRCRETTYSC LDCGESFSIE TYKSHIKCVT EKKKYGGKNY VEKENKGEAK
QNQWVEQVER AIENVTDKGL KDLLQQIHGF NNVPRKEAKF INFLQNSIKI RDRDLCVKAW
SCISEQAQKL RRETEVESKR NGESCNSVGD EKGLSSEQEI SKGNEEEVGE IENERRKKQN
GMWEDDNDGA RQIKLTVEDV KKFKWKRAIK RALKEAENGE MKVKRLKSKV IQSYLASGQC
SGSDENPETI FNSKLCSLGL HIDDKVVRLN
//
