P3IP1_RAT
ID P3IP1_RAT Reviewed; 267 AA.
AC Q56A20;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 92.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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=AAH92208.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AC094950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC092208; AAH92208.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001017453.1; NM_001017453.1.
DR RefSeq; XP_006251355.1; XM_006251293.3.
DR AlphaFoldDB; Q56A20; -.
DR STRING; 10116.ENSRNOP00000054550; -.
DR PaxDb; Q56A20; -.
DR Ensembl; ENSRNOT00000057738; ENSRNOP00000054550; ENSRNOG00000018859.
DR GeneID; 305472; -.
DR KEGG; rno:305472; -.
DR UCSC; RGD:1311203; rat.
DR CTD; 113791; -.
DR RGD; 1311203; Pik3ip1.
DR eggNOG; ENOG502QTWD; Eukaryota.
DR GeneTree; ENSGT00390000017774; -.
DR InParanoid; Q56A20; -.
DR PhylomeDB; Q56A20; -.
DR PRO; PR:Q56A20; -.
DR Proteomes; UP000002494; Chromosome 14.
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; ISO:RGD.
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; ISO:RGD.
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..267
FT /note="Phosphoinositide-3-kinase-interacting protein 1"
FT /id="PRO_0000280350"
FT TOPO_DOM 22..172
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..101
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT REGION 91..122
FT /note="Disordered"
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"
SQ SEQUENCE 267 AA; 29101 MW; AF45F47425574A1C CRC64;
MLLAWVHTFL LSNMLLAEAY GSGGCFWDNG HLYREDQPSP APGLRCLNWL AAQGSGESLA
QPSPGNHNYC RNPDQDPRGP WCYISSETGV PEKRPCEDLR CPETTSQAPP PPPPSSTTEL
EEKFGVPGDK ETQVFPPANA LPARSEAAEV QPVIGISQRV RMNSKEKKDL GTLGYVLGVT
MTVIIIAIGV GIVLGYTYKR GKDLKEQHEQ KVCEREMQRI TLPLSAFTNP TCEIMDEKTI
IVHSNQTPAD VQEGSTLLTD QAGTPGA
