ID   P3IP1_BOVIN             Reviewed;         261 AA.
AC   Q1RMT9; Q1JPA4;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2006) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABF57405.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BT025449; ABF57405.1; ALT_INIT; mRNA.
DR   EMBL; BC114715; AAI14716.1; -; mRNA.
DR   RefSeq; NP_001069020.1; NM_001075552.1.
DR   AlphaFoldDB; Q1RMT9; -.
DR   STRING; 9913.ENSBTAP00000014109; -.
DR   PaxDb; Q1RMT9; -.
DR   PRIDE; Q1RMT9; -.
DR   GeneID; 512082; -.
DR   KEGG; bta:512082; -.
DR   CTD; 113791; -.
DR   eggNOG; ENOG502QTWD; Eukaryota.
DR   HOGENOM; CLU_092099_0_0_1; -.
DR   InParanoid; Q1RMT9; -.
DR   OrthoDB; 1027586at2759; -.
DR   TreeFam; TF331319; -.
DR   Proteomes; UP000009136; 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:0036313; F:phosphatidylinositol 3-kinase catalytic subunit binding; IBA:GO_Central.
DR   GO; GO:0043553; P:negative regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
DR   GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
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; Kringle; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..261
FT                   /note="Phosphoinositide-3-kinase-interacting protein 1"
FT                   /id="PRO_0000280346"
FT   TOPO_DOM        22..166
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          24..101
FT                   /note="Kringle"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   REGION          90..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT   CONFLICT        120
FT                   /note="A -> P (in Ref. 1; ABF57405)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   261 AA;  27772 MW;  5DD806D776EBA48C CRC64;
     MLLAWVRTIL VSNMLLAEAY GSGGCFWDNG HLYRADQPSP APGHSCLNWL DAQSGLAFAP
     ESGAGNHSYC RNPDQDPRGP WCYVSGEAGA PEKRPCQDLR CPDTTSQGLP TSATETEEAA
     EVPGGDEVFA PANALPARSE AAAVQPVIGI SQRVRVNSKE KKDLGTLGYV LGITMMVIIV
     VIGAGIVLGY TYKRGKDLKA QHEQKVCERE LQRITLPLSA FTNPTCEIVD EKTVVVHASQ
     TPVDLQEGSA PLMGQAGTPG A