ID M3VWF4_FELCA Unreviewed; 311 AA.
AC M3VWF4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Phosphoinositide-3-kinase-interacting protein 1 {ECO:0000256|ARBA:ARBA00044176};
DE AltName: Full=Kringle domain-containing protein HGFL {ECO:0000256|ARBA:ARBA00044210};
GN Name=PIK3IP1 {ECO:0000313|Ensembl:ENSFCAP00000001227.6,
GN ECO:0000313|VGNC:VGNC:64177};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000001227.6, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000001227.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001227.6,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000001227.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001227.6,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000001227.6}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001227.6};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Negative regulator of hepatic phosphatidylinositol 3-kinase
CC (PI3K) activity. {ECO:0000256|ARBA:ARBA00043894}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR EMBL; AANG04000189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006938661.1; XM_006938599.3.
DR AlphaFoldDB; M3VWF4; -.
DR STRING; 9685.ENSFCAP00000001227; -.
DR Ensembl; ENSFCAT00000001319.6; ENSFCAP00000001227.6; ENSFCAG00000001319.6.
DR GeneID; 101097180; -.
DR KEGG; fca:101097180; -.
DR CTD; 113791; -.
DR VGNC; VGNC:64177; PIK3IP1.
DR eggNOG; ENOG502QTWD; Eukaryota.
DR GeneTree; ENSGT00390000017774; -.
DR HOGENOM; CLU_092099_0_0_1; -.
DR InParanoid; M3VWF4; -.
DR OMA; HDQKVCE; -.
DR OrthoDB; 2881180at2759; -.
DR Proteomes; UP000011712; Chromosome D3.
DR Bgee; ENSFCAG00000001319; Expressed in uterus and 10 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0036313; F:phosphatidylinositol 3-kinase catalytic subunit binding; IBA:GO_Central.
DR GO; GO:0141039; F:phosphatidylinositol 3-kinase inhibitor activity; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central.
DR CDD; cd00108; KR; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR PANTHER; PTHR24261:SF16; PHOSPHOINOSITIDE-3-KINASE-INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR24261; PLASMINOGEN-RELATED; 1.
DR Pfam; PF00051; Kringle; 1.
DR SMART; SM00130; KR; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..311
FT /note="Phosphoinositide-3-kinase-interacting protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023803115"
FT TRANSMEM 217..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..149
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT REGION 32..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 72..149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 311 AA; 33204 MW; AC9A3C82525CD70B CRC64;
MLLAWVKTFL IGNMLLAEAY GSGGVTTTLQ GRWGFPSEGR GAPTGPASPS RDRLGFPAGH
SVSGGLLFIT GCFWDNGHLY RADQPSPAPG LRCLNWLEAQ SGLASAPASG DTGNHSYCRN
PDQDPRGPWC YVRGEAGAPE KWPCEDLHCP ETTSQSPPTF TTETEEASEV PSGDEVQVFA
PANALPARSE AAAVQPVIGI SQRVRVNSKE KKDLGTLGYV LGITMMVIII AIGAGIVLGY
TYKRGKDLKE QHDQRVCERE MQRITLPLSA FTNPTCEIVD EKTIVVHTNQ TPVDLQEGSA
PLMGQAGTPG A
//