P3IP1_PONAB
ID P3IP1_PONAB Reviewed; 263 AA.
AC Q5RCS3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Phosphoinositide-3-kinase-interacting protein 1;
DE AltName: Full=Kringle domain-containing protein HGFL;
DE Flags: Precursor;
GN Name=PIK3IP1; Synonyms=HGFL;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Negative regulator of hepatic phosphatidylinositol 3-kinase
CC (PI3K) activity. {ECO:0000250|UniProtKB:Q7TMJ8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96FE7};
CC Single-pass type I membrane protein {ECO:0000255}.
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DR EMBL; CR858196; CAH90434.1; -; mRNA.
DR RefSeq; NP_001125218.1; NM_001131746.1.
DR AlphaFoldDB; Q5RCS3; -.
DR STRING; 9601.ENSPPYP00000013087; -.
DR GeneID; 100172110; -.
DR KEGG; pon:100172110; -.
DR CTD; 113791; -.
DR eggNOG; ENOG502QTWD; Eukaryota.
DR InParanoid; Q5RCS3; -.
DR OrthoDB; 1027586at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
DR CDD; cd00108; KR; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR Pfam; PF00051; Kringle; 1.
DR SMART; SM00130; KR; 1.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Kringle; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..263
FT /note="Phosphoinositide-3-kinase-interacting protein 1"
FT /id="PRO_0000280349"
FT TOPO_DOM 22..168
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..101
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT REGION 242..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DISULFID 46..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DISULFID 70..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 263 AA; 28091 MW; DF62EDC107C1258E CRC64;
MLLAWVQAFL VSNMLLAEAY GSGGCFWDNG HLYREDQTSP APGLRCLNWL DAQSGLASAP
VSGAGNHSYC RNPDEDPRGP WCYVSGEAGV PEKRPCENLS CPETTSQALP ASTTEIEEAS
EGPGADEVQV FAPANALPAR SEAAAVQPVI GISQRVRMNS KEKKDLGTLG YVLGITMMVI
IVAIGAGIIL GYSYKRGKDL KEQHDQKVCE REMQRITLPL SAFTNPTCEI VDEKTVVVHT
SQTPVDPQEG STPLMGQAGT PGA