ID A0A3P9CM31_9CICH Unreviewed; 278 AA.
AC A0A3P9CM31;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005023142.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005023142.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005023142.1}
RP IDENTIFICATION.
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 RefSeq; XP_004544644.1; XM_004544587.3.
DR RefSeq; XP_004544645.1; XM_004544588.3.
DR AlphaFoldDB; A0A3P9CM31; -.
DR STRING; 106582.ENSMZEP00005023142; -.
DR Ensembl; ENSMZET00005023903.1; ENSMZEP00005023142.1; ENSMZEG00005017332.1.
DR GeneID; 101466586; -.
DR KEGG; mze:101466586; -.
DR CTD; 113791; -.
DR GeneTree; ENSGT00390000017774; -.
DR OrthoDB; 2881180at2759; -.
DR Proteomes; UP000265160; LG12.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 PRINTS; PR00018; KRINGLE.
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:UP000265160};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..278
FT /note="Phosphoinositide-3-kinase-interacting protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017944802"
FT TRANSMEM 179..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..118
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT REGION 129..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 60..99
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 278 AA; 30334 MW; 8C3FF482F0F2C6A6 CRC64;
MLSVKSARQL CKVFFSLHVV FLSVALVESR ASNGDQKDCV RSHGVDYRGE QQNSSSGLSC
LIWTNTTRDY DVTIHPDSEK GVGDHNYCRN PDASERPWCY IAGPDGAIQR ESCALETCKE
QYSSIPAKTE SLSTKATTPS TESAQPAKAS RGDVPALQPV MGISQRVHTG PKKKKDLGAI
GYVLAIIMMG IIIVLGVGIT LGYFYKRGRD LKKQHEQRVY EREMQRITLP LSAFSNPTCE
LVDENTIVIT AEHETTPVQD DADGGDPLMA QQAGTPGA
//
