PCID2_MOUSE
ID PCID2_MOUSE Reviewed; 399 AA.
AC Q8BFV2; Q147Z6; Q8C951;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=PCI domain-containing protein 2;
DE AltName: Full=CSN12-like protein;
GN Name=Pcid2;
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=Cerebellum, and Corpora quadrigemina;
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].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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).
RN [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=20870947; DOI=10.4049/jimmunol.1002026;
RA Nakaya T., Kuwahara K., Ohta K., Kitabatake M., Toda T., Takeda N.,
RA Tani T., Kondo E., Sakaguchi N.;
RT "Critical role of Pcid2 in B cell survival through the regulation of MAD2
RT expression.";
RL J. Immunol. 185:5180-5187(2010).
CC -!- FUNCTION: Required for B-cell survival through the regulation of the
CC expression of cell-cycle checkpoint MAD2L1 protein during B cell
CC differentiation (PubMed:20870947). As a component of the TREX-2
CC complex, involved in the export of mRNAs to the cytoplasm through the
CC nuclear pores (By similarity). Binds and stabilizes BRCA2 and is thus
CC involved in the control of R-loop-associated DNA damage and
CC transcription-associated genomic instability. R-loop accumulation does
CC not increase in PCID2-depleted cells (By similarity).
CC {ECO:0000250|UniProtKB:Q5JVF3, ECO:0000269|PubMed:20870947}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC)-associated TREX-2
CC complex (transcription and export complex 2), composed of at least
CC GANP, 2 copies of ENY2, PCID2, SEM1/DSS1, and either centrin CETN2 or
CC centrin CETN3. The TREX-2 complex also associates with ALYREF/ALY and
CC with the nucleoporin NUP153 (By similarity). Interacts with BRCA2 (By
CC similarity). {ECO:0000250|UniProtKB:Q5JVF3}.
CC -!- DEVELOPMENTAL STAGE: In B lineage cells, expressed in a stage-dependent
CC manner at high levels in bone marrow pre-B and immature B-cells, and in
CC spleen transitional 1 and follicular B-cells, but at lower levels in
CC pro-B, transitional 2, and marginal zone B-cells.
CC {ECO:0000269|PubMed:20870947}.
CC -!- SIMILARITY: Belongs to the CSN12 family. {ECO:0000305}.
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DR EMBL; AK045796; BAC32494.1; -; mRNA.
DR EMBL; AK042945; BAC31414.1; -; mRNA.
DR EMBL; AK048722; BAC33434.1; -; mRNA.
DR EMBL; AK163697; BAE37463.1; -; mRNA.
DR EMBL; BC118533; AAI18534.1; -; mRNA.
DR CCDS; CCDS52484.1; -.
DR RefSeq; NP_848823.2; NM_178708.3.
DR AlphaFoldDB; Q8BFV2; -.
DR SMR; Q8BFV2; -.
DR BioGRID; 231489; 7.
DR IntAct; Q8BFV2; 1.
DR STRING; 10090.ENSMUSP00000133204; -.
DR iPTMnet; Q8BFV2; -.
DR PhosphoSitePlus; Q8BFV2; -.
DR EPD; Q8BFV2; -.
DR MaxQB; Q8BFV2; -.
DR PaxDb; Q8BFV2; -.
DR PRIDE; Q8BFV2; -.
DR ProteomicsDB; 294345; -.
DR Antibodypedia; 25858; 97 antibodies from 16 providers.
DR DNASU; 234069; -.
DR Ensembl; ENSMUST00000164416; ENSMUSP00000133204; ENSMUSG00000038542.
DR GeneID; 234069; -.
DR KEGG; mmu:234069; -.
DR UCSC; uc012fzt.1; mouse.
DR CTD; 55795; -.
DR MGI; MGI:2443003; Pcid2.
DR VEuPathDB; HostDB:ENSMUSG00000038542; -.
DR eggNOG; KOG2688; Eukaryota.
DR GeneTree; ENSGT00390000001101; -.
DR HOGENOM; CLU_031567_2_0_1; -.
DR InParanoid; Q8BFV2; -.
DR OMA; TYLIPCH; -.
DR OrthoDB; 706700at2759; -.
DR PhylomeDB; Q8BFV2; -.
DR TreeFam; TF106136; -.
DR BioGRID-ORCS; 234069; 24 hits in 67 CRISPR screens.
DR ChiTaRS; Pcid2; mouse.
DR PRO; PR:Q8BFV2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BFV2; protein.
DR Bgee; ENSMUSG00000038542; Expressed in ileal epithelium and 259 other tissues.
DR ExpressionAtlas; Q8BFV2; baseline and differential.
DR Genevisible; Q8BFV2; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0044615; C:nuclear pore nuclear basket; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070390; C:transcription export complex 2; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:1905457; P:negative regulation of lymphoid progenitor cell differentiation; IMP:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:UniProtKB.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR GO; GO:1900049; P:regulation of histone exchange; IMP:UniProtKB.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:UniProtKB.
DR GO; GO:0048536; P:spleen development; IMP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR045114; Csn12-like.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12732; PTHR12732; 1.
DR Pfam; PF01399; PCI; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Acetylation; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5JVF3"
FT CHAIN 2..399
FT /note="PCI domain-containing protein 2"
FT /id="PRO_0000121030"
FT DOMAIN 210..391
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q5JVF3"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JVF3"
FT CONFLICT 227
FT /note="K -> N (in Ref. 1; BAC31414)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 46132 MW; EA4B7DC9891D59F7 CRC64;
MAHITINQYL QQVYEAIDTR DGASCAELVS FKHPHVANPR LQMASPEEKC QQVLEPPYDE
MFAAHLRCTY AVGNHDFIEA YKCQTVIVQS FLRAFQAHKE ENWALPVMYA VALDLRIFAN
NADQQLVKKG KSKVGDMLEK AAELLMSCFR VCASDTRAGI EDSKKWGMLF LVNQLFKIYF
KINKLHLCKP LIRAIDSSNL KDDYSTAQRI TYKYYVGRKA MFDSDFKQAE EYLSFAFEHC
HRSSQKNKRM ILIYLLPVKM LLGHMPTIEL LRKYHLMQFS EVTKAVSEGN LLLLNEALAK
HETFFIRCGI FLILEKLKII TYRNLFKKVY LLLKTHQLSL DAFLVALKFM HVEDVDIDEV
QCILANLIYM GHIKGYISHQ HQKLVVSKQN PFPPLSTVC
