PCLI1_HUMAN
ID PCLI1_HUMAN Reviewed; 250 AA.
AC Q7Z2X4; B3KU82; Q68CJ2; Q6ZUS3; Q8IXL0; Q9NWP6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=PTB-containing, cubilin and LRP1-interacting protein;
DE Short=P-CLI1;
DE AltName: Full=Phosphotyrosine interaction domain-containing protein 1;
DE AltName: Full=Protein NYGGF4;
GN Name=PID1; Synonyms=NYGGF4, PCLI1; ORFNames=HMFN2073;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Liver;
RX PubMed=15221005; DOI=10.1038/sj.onc.1207782;
RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S.,
RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S.,
RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.;
RT "Expression profiling and differential screening between hepatoblastomas
RT and the corresponding normal livers: identification of high expression of
RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.";
RL Oncogene 23:5901-5911(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Adipose tissue;
RX PubMed=16815647; DOI=10.1016/j.gene.2006.05.008;
RA Wang B., Zhang M., Ni Y.-H., Liu F., Fan H.-Q., Fei L., Pan X.-Q., Guo M.,
RA Chen R.-H., Guo X.-R.;
RT "Identification and characterization of NYGGF4, a novel gene containing a
RT phosphotyrosine-binding (PTB) domain that stimulates 3T3-L1 preadipocytes
RT proliferation.";
RL Gene 379:132-140(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), VARIANT
RP 44-HIS--LYS-93 DUP, AND POLYMORPHISM.
RC TISSUE=Brain, Ileal mucosa, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Ovary;
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 [6]
RP IDENTIFICATION IN A COMPLEX WITH LRP1 AND CUBN, AND INTERACTION WITH LRP1
RP AND CUBN.
RX PubMed=17124247; DOI=10.1074/mcp.m600289-mcp200;
RA Caratu G., Allegra D., Bimonte M., Schiattarella G.G., D'Ambrosio C.,
RA Scaloni A., Napolitano M., Russo T., Zambrano N.;
RT "Identification of the ligands of protein interaction domains through a
RT functional approach.";
RL Mol. Cell. Proteomics 6:333-345(2007).
CC -!- FUNCTION: Increases proliferation of preadipocytes without affecting
CC adipocytic differentiation. {ECO:0000269|PubMed:16815647}.
CC -!- SUBUNIT: Found in a complex with PID1/PCLI1, LRP1 and CUBNI. Interacts
CC with LRP1 and CUBN. {ECO:0000269|PubMed:17124247}.
CC -!- INTERACTION:
CC Q7Z2X4; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-10256685, EBI-10173507;
CC Q7Z2X4; Q8N9N5: BANP; NbExp=3; IntAct=EBI-10256685, EBI-744695;
CC Q7Z2X4; Q8NA61: CBY2; NbExp=3; IntAct=EBI-10256685, EBI-741724;
CC Q7Z2X4; O43186: CRX; NbExp=3; IntAct=EBI-10256685, EBI-748171;
CC Q7Z2X4; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10256685, EBI-618309;
CC Q7Z2X4; Q9HD26: GOPC; NbExp=3; IntAct=EBI-10256685, EBI-349832;
CC Q7Z2X4; Q99750: MDFI; NbExp=3; IntAct=EBI-10256685, EBI-724076;
CC Q7Z2X4; P15531: NME1; NbExp=3; IntAct=EBI-10256685, EBI-741141;
CC Q7Z2X4; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-10256685, EBI-945833;
CC Q7Z2X4; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-10256685, EBI-741515;
CC Q7Z2X4-3; Q8N684-3: CPSF7; NbExp=3; IntAct=EBI-11953174, EBI-11523759;
CC Q7Z2X4-3; Q9NQM4: DNAAF6; NbExp=3; IntAct=EBI-11953174, EBI-10239299;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16815647}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q7Z2X4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z2X4-2; Sequence=VSP_022910;
CC Name=3;
CC IsoId=Q7Z2X4-3; Sequence=VSP_022909, VSP_022912;
CC Name=4;
CC IsoId=Q7Z2X4-4; Sequence=VSP_022911;
CC -!- TISSUE SPECIFICITY: Expressed in subcutaneous fat, heart, skeletal
CC muscle, brain, colon, thymus, spleen, kidney, liver, small intestine,
CC placenta, lung and peripheral blood leukocyte.
CC {ECO:0000269|PubMed:16815647}.
CC -!- INDUCTION: Up-regulated in fat of obese subjects.
CC {ECO:0000269|PubMed:16815647}.
CC -!- POLYMORPHISM: Some sequences seem to have a duplication of exon 2.
CC {ECO:0000303|PubMed:14702039}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD38656.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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 EMBL; AB075874; BAD38656.1; ALT_INIT; mRNA.
DR EMBL; AY317148; AAP79437.1; -; mRNA.
DR EMBL; AK000708; BAA91333.1; -; mRNA.
DR EMBL; AK096636; BAG53344.1; -; mRNA.
DR EMBL; AK125359; BAC86145.1; -; mRNA.
DR EMBL; CH471063; EAW70891.1; -; Genomic_DNA.
DR EMBL; BC040164; AAH40164.1; -; mRNA.
DR CCDS; CCDS2471.1; -. [Q7Z2X4-2]
DR CCDS; CCDS42830.1; -. [Q7Z2X4-4]
DR CCDS; CCDS82577.1; -. [Q7Z2X4-1]
DR CCDS; CCDS82578.1; -. [Q7Z2X4-3]
DR RefSeq; NP_001094288.1; NM_001100818.1. [Q7Z2X4-4]
DR RefSeq; NP_001317085.1; NM_001330156.1. [Q7Z2X4-1]
DR RefSeq; NP_001317086.1; NM_001330157.1. [Q7Z2X4-3]
DR RefSeq; NP_060403.3; NM_017933.4. [Q7Z2X4-2]
DR AlphaFoldDB; Q7Z2X4; -.
DR SMR; Q7Z2X4; -.
DR BioGRID; 120352; 27.
DR CORUM; Q7Z2X4; -.
DR IntAct; Q7Z2X4; 12.
DR STRING; 9606.ENSP00000375907; -.
DR iPTMnet; Q7Z2X4; -.
DR PhosphoSitePlus; Q7Z2X4; -.
DR BioMuta; PID1; -.
DR DMDM; 74713284; -.
DR EPD; Q7Z2X4; -.
DR jPOST; Q7Z2X4; -.
DR MassIVE; Q7Z2X4; -.
DR PaxDb; Q7Z2X4; -.
DR PeptideAtlas; Q7Z2X4; -.
DR PRIDE; Q7Z2X4; -.
DR ProteomicsDB; 68980; -. [Q7Z2X4-1]
DR ProteomicsDB; 68981; -. [Q7Z2X4-2]
DR ProteomicsDB; 68982; -. [Q7Z2X4-3]
DR ProteomicsDB; 68983; -. [Q7Z2X4-4]
DR Antibodypedia; 34394; 120 antibodies from 17 providers.
DR DNASU; 55022; -.
DR Ensembl; ENST00000354069.6; ENSP00000283937.8; ENSG00000153823.19. [Q7Z2X4-1]
DR Ensembl; ENST00000392054.7; ENSP00000375907.3; ENSG00000153823.19. [Q7Z2X4-2]
DR Ensembl; ENST00000392055.8; ENSP00000375908.3; ENSG00000153823.19. [Q7Z2X4-4]
DR Ensembl; ENST00000409462.1; ENSP00000386826.1; ENSG00000153823.19. [Q7Z2X4-3]
DR GeneID; 55022; -.
DR KEGG; hsa:55022; -.
DR MANE-Select; ENST00000392055.8; ENSP00000375908.3; NM_001100818.2; NP_001094288.1. [Q7Z2X4-4]
DR UCSC; uc002vpr.5; human. [Q7Z2X4-1]
DR CTD; 55022; -.
DR DisGeNET; 55022; -.
DR GeneCards; PID1; -.
DR HGNC; HGNC:26084; PID1.
DR HPA; ENSG00000153823; Low tissue specificity.
DR MIM; 612930; gene.
DR neXtProt; NX_Q7Z2X4; -.
DR OpenTargets; ENSG00000153823; -.
DR PharmGKB; PA162399462; -.
DR VEuPathDB; HostDB:ENSG00000153823; -.
DR eggNOG; KOG4448; Eukaryota.
DR GeneTree; ENSGT00510000048154; -.
DR HOGENOM; CLU_088811_0_0_1; -.
DR InParanoid; Q7Z2X4; -.
DR OMA; HHLDERG; -.
DR OrthoDB; 1145472at2759; -.
DR PhylomeDB; Q7Z2X4; -.
DR PathwayCommons; Q7Z2X4; -.
DR SignaLink; Q7Z2X4; -.
DR BioGRID-ORCS; 55022; 13 hits in 1077 CRISPR screens.
DR ChiTaRS; PID1; human.
DR GenomeRNAi; 55022; -.
DR Pharos; Q7Z2X4; Tbio.
DR PRO; PR:Q7Z2X4; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q7Z2X4; protein.
DR Bgee; ENSG00000153823; Expressed in descending thoracic aorta and 179 other tissues.
DR ExpressionAtlas; Q7Z2X4; baseline and differential.
DR Genevisible; Q7Z2X4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:BHF-UCL.
DR GO; GO:0071398; P:cellular response to fatty acid; ISS:BHF-UCL.
DR GO; GO:0071354; P:cellular response to interleukin-6; ISS:BHF-UCL.
DR GO; GO:0044320; P:cellular response to leptin stimulus; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:BHF-UCL.
DR GO; GO:0006112; P:energy reserve metabolic process; IC:BHF-UCL.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:BHF-UCL.
DR GO; GO:2001170; P:negative regulation of ATP biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0046325; P:negative regulation of glucose import; IDA:BHF-UCL.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IDA:BHF-UCL.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0070346; P:positive regulation of fat cell proliferation; IDA:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0010635; P:regulation of mitochondrial fusion; IC:BHF-UCL.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:BHF-UCL.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISS: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..250
FT /note="PTB-containing, cubilin and LRP1-interacting
FT protein"
FT /id="PRO_0000274900"
FT DOMAIN 93..250
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 229..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UBG2"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UBG2"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022909"
FT VAR_SEQ 1..43
FT /note="MFSLPLSLPLCEDTAFLPSKCCSSHKTIKQARTLIMIFLASGT -> MPRIA
FT GNHLMLEESRTCSSPELLDGVWPCQPLHFGLPASEM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022910"
FT VAR_SEQ 1..43
FT /note="MFSLPLSLPLCEDTAFLPSKCCSSHKTIKQARTLIMIFLASGT -> MWQPA
FT TERLQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15221005"
FT /id="VSP_022911"
FT VAR_SEQ 83..92
FT /note="MKTRTHSGCK -> MWQPATERLQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022912"
FT VARIANT 43
FT /note="T -> THFQTMLKSKLNVLTLKKEPLPAVIFHEPEAIELCTTTPLMKTRTHS
FT GCK (in variant with duplicated exon 2)"
FT /id="VAR_030361"
SQ SEQUENCE 250 AA; 28272 MW; 3C2F4AE5254D2885 CRC64;
MFSLPLSLPL CEDTAFLPSK CCSSHKTIKQ ARTLIMIFLA SGTHFQTMLK SKLNVLTLKK
EPLPAVIFHE PEAIELCTTT PLMKTRTHSG CKVTYLGKVS TTGMQFLSGC TEKPVIELWK
KHTLAREDVF PANALLEIRP FQVWLHHLDH KGEATVHMDT FQVARIAYCT ADHNVSPNIF
AWVYREINDD LSYQMDCHAV ECESKLEAKK LAHAMMEAFR KTFHSMKSDG RIHSNSSSEE
VSQELESDDG
