PIN4_MOUSE
ID PIN4_MOUSE Reviewed; 131 AA.
AC Q9CWW6; Q0VE57;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4;
DE EC=5.2.1.8;
DE AltName: Full=Parvulin-14;
DE Short=Par14;
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin4;
DE Short=PPIase Pin4;
DE AltName: Full=Rotamase Pin4;
GN Name=Pin4;
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].
RC STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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).
RN [5]
RP IDENTIFICATION IN PRE-RRNP COMPLEXES.
RX PubMed=11960984; DOI=10.1074/jbc.m201181200;
RA Fujiyama S., Yanagida M., Hayano T., Miura Y., Isobe T., Fujimori F.,
RA Uchida T., Takahashi N.;
RT "Isolation and proteomic characterization of human Parvulin-associating
RT pre-ribosomal ribonucleoprotein complexes.";
RL J. Biol. Chem. 277:23773-23780(2002).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, 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: Involved as a ribosomal RNA processing factor in ribosome
CC biogenesis. Binds to tightly bent AT-rich stretches of double-stranded
CC DNA (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC -!- SUBUNIT: Found in pre-ribosomal ribonucleoprotein (pre-rRNP) complexes.
CC {ECO:0000269|PubMed:11960984}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Colocalizes in the nucleolus during interphase and on the spindle
CC apparatus during mitosis with NPM1. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylation occurs both in the nucleus and the
CC cytoplasm. Phosphorylation at Ser-19 does not affect its PPIase
CC activity but is required for nuclear localization, and the
CC dephosphorylation is a prerequisite for the binding to DNA. The
CC unphosphorylated form associates with the pre-rRNP complexes in the
CC nucleus (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family. PIN4
CC subfamily. {ECO:0000305}.
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DR EMBL; AK010338; BAB26863.1; -; mRNA.
DR EMBL; AL807784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466564; EDL14129.1; -; Genomic_DNA.
DR EMBL; BC119355; AAI19356.1; -; mRNA.
DR EMBL; BC119357; AAI19358.1; -; mRNA.
DR CCDS; CCDS41082.1; -.
DR RefSeq; NP_081457.1; NM_027181.1.
DR RefSeq; XP_011249230.1; XM_011250928.1.
DR AlphaFoldDB; Q9CWW6; -.
DR BMRB; Q9CWW6; -.
DR SMR; Q9CWW6; -.
DR IntAct; Q9CWW6; 1.
DR MINT; Q9CWW6; -.
DR STRING; 10090.ENSMUSP00000109257; -.
DR iPTMnet; Q9CWW6; -.
DR PhosphoSitePlus; Q9CWW6; -.
DR EPD; Q9CWW6; -.
DR MaxQB; Q9CWW6; -.
DR PaxDb; Q9CWW6; -.
DR PeptideAtlas; Q9CWW6; -.
DR PRIDE; Q9CWW6; -.
DR ProteomicsDB; 287732; -.
DR Antibodypedia; 27865; 219 antibodies from 25 providers.
DR Ensembl; ENSMUST00000113627; ENSMUSP00000109257; ENSMUSG00000079480.
DR GeneID; 69713; -.
DR KEGG; mmu:69713; -.
DR UCSC; uc009tyj.1; mouse.
DR CTD; 5303; -.
DR MGI; MGI:1916963; Pin4.
DR VEuPathDB; HostDB:ENSMUSG00000079480; -.
DR eggNOG; KOG3258; Eukaryota.
DR GeneTree; ENSGT00510000047029; -.
DR HOGENOM; CLU_090028_2_1_1; -.
DR InParanoid; Q9CWW6; -.
DR OMA; AMSINVR; -.
DR OrthoDB; 1397633at2759; -.
DR PhylomeDB; Q9CWW6; -.
DR TreeFam; TF101102; -.
DR BioGRID-ORCS; 69713; 2 hits in 52 CRISPR screens.
DR ChiTaRS; Pin4; mouse.
DR PRO; PR:Q9CWW6; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9CWW6; protein.
DR Bgee; ENSMUSG00000079480; Expressed in embryonic brain and 61 other tissues.
DR Genevisible; Q9CWW6; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0030684; C:preribosome; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0003681; F:bent DNA binding; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; ISO:MGI.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR043323; PIN4.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR PANTHER; PTHR45995; PTHR45995; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; DNA-binding; Isomerase; Nucleus; Phosphoprotein;
KW Reference proteome; Rotamase.
FT CHAIN 1..131
FT /note="Peptidyl-prolyl cis-trans isomerase NIMA-interacting
FT 4"
FT /id="PRO_0000193439"
FT DOMAIN 35..129
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT REGION 1..41
FT /note="Necessary for association with the pre-rRNP
FT complexes"
FT /evidence="ECO:0000250"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..25
FT /note="Necessary for nuclear localization and DNA-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y237"
SQ SEQUENCE 131 AA; 13815 MW; 290BDEF72DC69CA6 CRC64;
MPPKGKSGSG KGGKGGAASG SDSADKKSQG PKGGGNAVKV RHILCEKHGK IMEAMEKLKS
GMRFSEVATQ YSEDKARQGG DLGWMTRGSM VGPFQEAAFA LPVSGMDKPV FTDPPVKTKF
GYHIIMVEGR K
