PCLI1_MOUSE
ID PCLI1_MOUSE Reviewed; 217 AA.
AC Q3UBG2; Q3UAR0; Q68EE9; Q7TPS1;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=PTB-containing, cubilin and LRP1-interacting protein;
DE Short=P-CLI1;
DE AltName: Full=Phosphotyrosine interaction domain-containing protein 1;
GN Name=Pid1; Synonyms=Pcli1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Egg;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 37-217 (ISOFORMS 1/2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-214, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-203 AND SER-214, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Increases proliferation of preadipocytes without affecting
CC adipocytic differentiation. {ECO:0000250}.
CC -!- SUBUNIT: Found in a complex with PID1/PCLI1, LRP1 and CUBNI. Interacts
CC with LRP1 and CUBN. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UBG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UBG2-2; Sequence=VSP_022913;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH54112.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH80290.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE30002.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE30254.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK150971; BAE30002.1; ALT_INIT; mRNA.
DR EMBL; AK151267; BAE30254.1; ALT_INIT; mRNA.
DR EMBL; AK162081; BAE36714.1; -; mRNA.
DR EMBL; BC054112; AAH54112.1; ALT_INIT; mRNA.
DR EMBL; BC080290; AAH80290.1; ALT_INIT; mRNA.
DR CCDS; CCDS15104.2; -. [Q3UBG2-1]
DR RefSeq; NP_001003948.2; NM_001003948.2. [Q3UBG2-1]
DR AlphaFoldDB; Q3UBG2; -.
DR SMR; Q3UBG2; -.
DR BioGRID; 221073; 3.
DR STRING; 10090.ENSMUSP00000127716; -.
DR iPTMnet; Q3UBG2; -.
DR PhosphoSitePlus; Q3UBG2; -.
DR MaxQB; Q3UBG2; -.
DR PaxDb; Q3UBG2; -.
DR PeptideAtlas; Q3UBG2; -.
DR PRIDE; Q3UBG2; -.
DR ProteomicsDB; 288073; -. [Q3UBG2-1]
DR ProteomicsDB; 288074; -. [Q3UBG2-2]
DR Antibodypedia; 34394; 120 antibodies from 17 providers.
DR Ensembl; ENSMUST00000168574; ENSMUSP00000127716; ENSMUSG00000045658. [Q3UBG2-1]
DR Ensembl; ENSMUST00000176559; ENSMUSP00000135164; ENSMUSG00000045658. [Q3UBG2-2]
DR GeneID; 98496; -.
DR KEGG; mmu:98496; -.
DR UCSC; uc007bst.2; mouse. [Q3UBG2-1]
DR CTD; 55022; -.
DR MGI; MGI:2138391; Pid1.
DR VEuPathDB; HostDB:ENSMUSG00000045658; -.
DR eggNOG; KOG4448; Eukaryota.
DR GeneTree; ENSGT00510000048154; -.
DR HOGENOM; CLU_088811_0_0_1; -.
DR InParanoid; Q3UBG2; -.
DR OMA; HHLDERG; -.
DR OrthoDB; 1145472at2759; -.
DR PhylomeDB; Q3UBG2; -.
DR BioGRID-ORCS; 98496; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Pid1; mouse.
DR PRO; PR:Q3UBG2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3UBG2; protein.
DR Bgee; ENSMUSG00000045658; Expressed in stroma of bone marrow and 231 other tissues.
DR ExpressionAtlas; Q3UBG2; baseline and differential.
DR Genevisible; Q3UBG2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IDA:BHF-UCL.
DR GO; GO:0071398; P:cellular response to fatty acid; IDA:BHF-UCL.
DR GO; GO:0071354; P:cellular response to interleukin-6; IDA:BHF-UCL.
DR GO; GO:0044320; P:cellular response to leptin stimulus; IDA:BHF-UCL.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:BHF-UCL.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISO:MGI.
DR GO; GO:2001170; P:negative regulation of ATP biosynthetic process; ISO:MGI.
DR GO; GO:0046325; P:negative regulation of glucose import; IMP:BHF-UCL.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0070346; P:positive regulation of fat cell proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:BHF-UCL.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
DR CDD; cd13167; PTB_P-CLI1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR039112; PID1.
DR InterPro; IPR039114; PID1_PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR PANTHER; PTHR16265; PTHR16265; 1.
DR Pfam; PF14719; PID_2; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..217
FT /note="PTB-containing, cubilin and LRP1-interacting
FT protein"
FT /id="PRO_0000274901"
FT DOMAIN 60..217
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 194..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319"
FT VAR_SEQ 1..15
FT /note="MWQPATERLQHFQTM -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022913"
FT CONFLICT 216
FT /note="D -> G (in Ref. 2; AAH54112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 24784 MW; 8362BA0722BE4CC9 CRC64;
MWQPATERLQ HFQTMLKSKL NVLTLKKEPI PAVLFHEPEA IELCTTTPLM KARTHSGCKV
TYLGKVSTTG MQFLSGCTEK PVIELWKKHT LAREDVFPAN ALLEIRPFQV WLHHLDHKGE
ATVHMDTFQV ARIAYCTADH NVSPNIFAWV YREINDDLSY QMDCHAVQCE SKLEAKKLAH
AMMEAFKKTF HSMKSDGRIH RSSSSEEASQ ELESDDG
