PIGS_RAT
ID PIGS_RAT Reviewed; 555 AA.
AC Q5XI31;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=GPI transamidase component PIG-S;
DE AltName: Full=Phosphatidylinositol-glycan biosynthesis class S protein;
GN Name=Pigs;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Component of the GPI transamidase complex. Essential for
CC transfer of GPI to proteins, particularly for formation of carbonyl
CC intermediates (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBUNIT: Forms a complex with PIGK/GPI8, PIGT, PIGU and GAA1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIGS family. {ECO:0000305}.
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DR EMBL; BC083862; AAH83862.1; -; mRNA.
DR RefSeq; NP_001006602.1; NM_001006602.1.
DR AlphaFoldDB; Q5XI31; -.
DR SMR; Q5XI31; -.
DR STRING; 10116.ENSRNOP00000015207; -.
DR GlyGen; Q5XI31; 2 sites.
DR jPOST; Q5XI31; -.
DR PaxDb; Q5XI31; -.
DR PRIDE; Q5XI31; -.
DR Ensembl; ENSRNOT00000015207; ENSRNOP00000015207; ENSRNOG00000011366.
DR GeneID; 303277; -.
DR KEGG; rno:303277; -.
DR CTD; 94005; -.
DR RGD; 1359436; Pigs.
DR eggNOG; KOG2459; Eukaryota.
DR GeneTree; ENSGT00390000017203; -.
DR HOGENOM; CLU_010026_3_0_1; -.
DR InParanoid; Q5XI31; -.
DR OMA; AEHKYAV; -.
DR OrthoDB; 1399804at2759; -.
DR PhylomeDB; Q5XI31; -.
DR TreeFam; TF105857; -.
DR Reactome; R-RNO-162791; Attachment of GPI anchor to uPAR.
DR UniPathway; UPA00196; -.
DR PRO; PR:Q5XI31; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000011366; Expressed in ovary and 19 other tissues.
DR Genevisible; Q5XI31; RN.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; ISO:RGD.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; ISO:RGD.
DR InterPro; IPR019540; PtdIno-glycan_biosynth_class_S.
DR PANTHER; PTHR21072; PTHR21072; 1.
DR Pfam; PF10510; PIG-S; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..555
FT /note="GPI transamidase component PIG-S"
FT /id="PRO_0000218606"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..520
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 555 AA; 61724 MW; A3FF73CA93F6A0AF CRC64;
MATAGAAATD LEVVRGKRAA LFFAAVAILL GLPLWWKTTE TYRAPLPYSE ISGLNALQLR
LMVPVTVVFT RDSVPLDDQE KLPFTVVHER EIPLKYKMKI KCRFQKAYRR ALEHEEEALS
LGSVHEAEAL LAEPEKQAEG SLTVYVISEH SSLLPQDMMS YIGPERTAIV RGMIHREAFN
IIGRRIIHVA QAMSLTEDVL AAALADHLPE DKWSSDKRRP LKSSLGYEIT FSLLNPDPKS
HDVHWDIEEG VQRYVQPFLN RLSAAGNFSV DSQILYYAML GVNPRFDPAS SSYSLAMHSL
PHVINPVESR LGSSAASLYP VLNFLLYVPE LAHSPLYIQD KDGAPVATNA FHSPRWGGIM
VYNVDPKIYN ASELPVRVEV DMAQVMEVFL AQLRLLFGIA QPQVPPKCLL SGPKSEGLMT
WELDRLLWAR SVENLATATT TLTSLAQLLG KISNIVIKDD VASEVYRAVA AVQKAAEALA
LGHLSSAFAA SQEAVTSSER AFFDPSLLHL LYFPDDQKFA IYIPLFLPMA VPILLSLVKI
FLETHKSWKK PEKID