ID H3DEK3_TETNG Unreviewed; 266 AA.
AC H3DEK3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000018946.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000018946.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; H3DEK3; -.
DR STRING; 99883.ENSTNIP00000018946; -.
DR Ensembl; ENSTNIT00000019174.1; ENSTNIP00000018946.1; ENSTNIG00000015861.1.
DR GeneTree; ENSGT00390000017774; -.
DR HOGENOM; CLU_092099_0_0_1; -.
DR InParanoid; H3DEK3; -.
DR OMA; HDQKVCE; -.
DR TreeFam; TF331319; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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:UP000007303};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..266
FT /note="Phosphoinositide-3-kinase-interacting protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003583343"
FT TRANSMEM 170..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..104
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT REGION 110..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 46..85
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 266 AA; 28627 MW; BCE8020EDAAB7570 CRC64;
QPDGLVLQDP LSAQMFVLLL LLSDCVRSSG VDYRGGQQIS SSGLTCLNWT EATRDYDVLI
HPDSQTGVGD HSYCRNPDSS ERPWCYIAGP DGTVQRQFCT IDTCTEEASD DPAEAKSLDS
AGLPSSTEGL RPTSLASSGH QAAAVQPVIG ISQHVHTGPK KKKDLGTTGY VLGILMMAII
IVLGAGITFG YFYKRGRDIK KQHEQRVYER KMQKINLPLS AFSNPSCELV DENTIVITAE
PETTPVQEDM DGGDPLIGQQ AGTPGA
//