ID A0A2G8JG84_STIJA Unreviewed; 122 AA.
AC A0A2G8JG84;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Post-GPI attachment to proteins factor 2 {ECO:0000256|ARBA:ARBA00016871};
GN ORFNames=BSL78_28439 {ECO:0000313|EMBL:PIK34743.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK34743.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK34743.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK34743.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK34743.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
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 -!- 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:PIK34743.1}.
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; MRZV01002090; PIK34743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8JG84; -.
DR STRING; 307972.A0A2G8JG84; -.
DR Proteomes; UP000230750; 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 InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR InterPro; IPR039545; PGAP2.
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.
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 Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..122
FT /note="Post-GPI attachment to proteins factor 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013688097"
SQ SEQUENCE 122 AA; 14118 MW; 8C1419B406CAB440 CRC64;
MYFINRKPRL ARDVLHWFPA LQLSLCFSCA LCIAWPQCQK TIRTQNHSNG SGGFLDKRCC
FVTAMGFYYL HNAYCRPGVY TIFAFLEYII VLSNIAYHVC VSLDFSDREI RFGVIQSKNS
LN
//
