ZC3HE_MOUSE
ID ZC3HE_MOUSE Reviewed; 735 AA.
AC Q8BJ05; A0PJE7; A1A4A9; Q3TU70; Q8BIY8; Q8R3Q8; Q8R3R2; Q9DAA8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Zinc finger CCCH domain-containing protein 14;
GN Name=Zc3h14;
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; 2 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Head, Liver, and Testis;
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 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 128-735 (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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-309, AND IDENTIFICATION BY
RP 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 TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=19303045; DOI=10.1016/j.gene.2009.02.022;
RA Leung S.W., Apponi L.H., Cornejo O.E., Kitchen C.M., Valentini S.R.,
RA Pavlath G.K., Dunham C.M., Corbett A.H.;
RT "Splice variants of the human ZC3H14 gene generate multiple isoforms of a
RT zinc finger polyadenosine RNA binding protein.";
RL Gene 439:71-78(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-515 AND SER-527, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, 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 [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21734151; DOI=10.1073/pnas.1107103108;
RA Pak C., Garshasbi M., Kahrizi K., Gross C., Apponi L.H., Noto J.J.,
RA Kelly S.M., Leung S.W., Tzschach A., Behjati F., Abedini S.S., Mohseni M.,
RA Jensen L.R., Hu H., Huang B., Stahley S.N., Liu G., Williams K.R.,
RA Burdick S., Feng Y., Sanyal S., Bassell G.J., Ropers H.H., Najmabadi H.,
RA Corbett A.H., Moberg K.H., Kuss A.W.;
RT "Mutation of the conserved polyadenosine RNA binding protein, ZC3H14/dNab2,
RT impairs neural function in Drosophila and humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12390-12395(2011).
CC -!- FUNCTION: Involved in poly(A) tail length control in neuronal cells.
CC Binds the polyadenosine RNA oligonucleotides.
CC {ECO:0000250|UniProtKB:Q6PJT7}.
CC -!- SUBUNIT: Interacts with HOOK2. Interacts with ZFC3H1 in a RNase-
CC sensitive manner. {ECO:0000250|UniProtKB:Q6PJT7}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:19303045,
CC ECO:0000269|PubMed:21734151}. Note=Colocalizes with poly(A) RNA in
CC nuclear speckles. {ECO:0000269|PubMed:21734151}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BJ05-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BJ05-2; Sequence=VSP_033179;
CC Name=3;
CC IsoId=Q8BJ05-3; Sequence=VSP_033180;
CC Name=4;
CC IsoId=Q8BJ05-4; Sequence=VSP_033177, VSP_033178, VSP_033180;
CC -!- TISSUE SPECIFICITY: Expressed in hippocampal pyramidal neurons (at
CC protein level) (PubMed:21734151).Expressed in kidney, liver, muscle,
CC heart brain and testes (PubMed:19303045). Expressed in hippocampal
CC pyramidal neurons (PubMed:21734151). {ECO:0000269|PubMed:21734151}.
CC -!- SIMILARITY: Belongs to the ZC3H14 family. {ECO:0000305}.
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DR EMBL; AK006009; BAB24364.1; -; mRNA.
DR EMBL; AK048046; BAC33222.1; -; mRNA.
DR EMBL; AK050226; BAC34134.1; -; mRNA.
DR EMBL; AK160937; BAE36101.1; -; mRNA.
DR EMBL; BC021797; AAH21797.1; -; mRNA.
DR EMBL; BC024824; AAH24824.1; -; mRNA.
DR EMBL; BC024856; AAH24856.1; -; mRNA.
DR EMBL; BC026610; AAH26610.1; -; mRNA.
DR CCDS; CCDS26099.1; -. [Q8BJ05-3]
DR CCDS; CCDS26100.1; -. [Q8BJ05-1]
DR CCDS; CCDS49138.1; -. [Q8BJ05-2]
DR CCDS; CCDS49139.1; -. [Q8BJ05-4]
DR RefSeq; NP_001008506.2; NM_001008506.2. [Q8BJ05-3]
DR RefSeq; NP_001153579.1; NM_001160107.1. [Q8BJ05-2]
DR RefSeq; NP_001153580.1; NM_001160108.1. [Q8BJ05-4]
DR RefSeq; NP_083610.2; NM_029334.2. [Q8BJ05-1]
DR AlphaFoldDB; Q8BJ05; -.
DR BioGRID; 217572; 3.
DR STRING; 10090.ENSMUSP00000105732; -.
DR iPTMnet; Q8BJ05; -.
DR PhosphoSitePlus; Q8BJ05; -.
DR EPD; Q8BJ05; -.
DR jPOST; Q8BJ05; -.
DR MaxQB; Q8BJ05; -.
DR PaxDb; Q8BJ05; -.
DR PeptideAtlas; Q8BJ05; -.
DR PRIDE; Q8BJ05; -.
DR ProteomicsDB; 302046; -. [Q8BJ05-1]
DR ProteomicsDB; 302047; -. [Q8BJ05-2]
DR ProteomicsDB; 302048; -. [Q8BJ05-3]
DR ProteomicsDB; 302049; -. [Q8BJ05-4]
DR Antibodypedia; 26309; 147 antibodies from 23 providers.
DR DNASU; 75553; -.
DR Ensembl; ENSMUST00000021399; ENSMUSP00000021399; ENSMUSG00000021012. [Q8BJ05-4]
DR Ensembl; ENSMUST00000057000; ENSMUSP00000055879; ENSMUSG00000021012. [Q8BJ05-2]
DR Ensembl; ENSMUST00000110104; ENSMUSP00000105731; ENSMUSG00000021012. [Q8BJ05-3]
DR Ensembl; ENSMUST00000110105; ENSMUSP00000105732; ENSMUSG00000021012. [Q8BJ05-1]
DR GeneID; 75553; -.
DR KEGG; mmu:75553; -.
DR UCSC; uc007org.1; mouse. [Q8BJ05-1]
DR UCSC; uc007orh.1; mouse. [Q8BJ05-3]
DR UCSC; uc007ori.1; mouse. [Q8BJ05-2]
DR UCSC; uc007orl.2; mouse. [Q8BJ05-4]
DR CTD; 79882; -.
DR MGI; MGI:1919824; Zc3h14.
DR VEuPathDB; HostDB:ENSMUSG00000021012; -.
DR eggNOG; KOG3702; Eukaryota.
DR GeneTree; ENSGT00440000038430; -.
DR HOGENOM; CLU_022605_0_0_1; -.
DR InParanoid; Q8BJ05; -.
DR OMA; TFYHPTV; -.
DR OrthoDB; 893844at2759; -.
DR PhylomeDB; Q8BJ05; -.
DR TreeFam; TF329509; -.
DR BioGRID-ORCS; 75553; 6 hits in 69 CRISPR screens.
DR ChiTaRS; Zc3h14; mouse.
DR PRO; PR:Q8BJ05; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BJ05; protein.
DR Bgee; ENSMUSG00000021012; Expressed in spermatocyte and 254 other tissues.
DR ExpressionAtlas; Q8BJ05; baseline and differential.
DR Genevisible; Q8BJ05; MM.
DR GO; GO:1904115; C:axon cytoplasm; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; IBA:GO_Central.
DR InterPro; IPR040366; Nab2/ZC3H14.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14738; PTHR14738; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..735
FT /note="Zinc finger CCCH domain-containing protein 14"
FT /id="PRO_0000331313"
FT ZN_FING 595..620
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 621..640
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 641..656
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 681..698
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 700..718
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 78..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 357
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT CROSSLNK 489
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6PJT7"
FT VAR_SEQ 1..295
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033177"
FT VAR_SEQ 296..426
FT /note="LPVVSSVVKVKRFSHDGEEEEEDEDYGTRIGSLSSSVSVPAKPERRPSLPPS
FT KQANKNLILKAISEAQESVTKTTNYSAVPQKQTLPVAPRTRTSQEELLAEMVQGQNRAP
FT RISPPVKEEEAKGDNTGKSQ -> MKMSSRFSSPSLPVFLSPEPADLGSLTSASCSLNE
FT LGNISYLLRKIATDINEMKGMKAAILTVEANLFDLNVRVSQNEAKISSLEVKMNEYLTS
FT TSECNRQLEDFQERLEFESQSETTDANLIGFLTEVEK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033178"
FT VAR_SEQ 427..582
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_033179"
FT VAR_SEQ 452..582
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_033180"
FT CONFLICT 27
FT /note="D -> H (in Ref. 1; BAC34134)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="T -> A (in Ref. 1; BAE36101)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 735 AA; 82409 MW; 550696563E7E87C3 CRC64;
MEIGTEISRK IRSAIKGKLQ ELGAYVDEEL PDYIMVMVAN KKSQDQMTED LSLFLGNNTI
RFTVWLHGVL DKLRSVTTEP SSLKSPDASI FDSHVPSNKS SFSRGDERRH EAAVPPLAVS
SSRPEKRDSR VSTSSQEQKS TNVRHSYDDG ASTRLMSTVK PLREPAPSED VIDIKPEPDD
LIDEDLNFVQ ENPLSQKKPT VTLTYGSSRP SIEIYRPPAS RNADTGTHLN RLQLHPQQSS
AHAAKQLDVQ SSQVSEAGRL CEPPVLSSVE DTYSPFFRNN LDKMSIEDEN FRKRKLPVVS
SVVKVKRFSH DGEEEEEDED YGTRIGSLSS SVSVPAKPER RPSLPPSKQA NKNLILKAIS
EAQESVTKTT NYSAVPQKQT LPVAPRTRTS QEELLAEMVQ GQNRAPRISP PVKEEEAKGD
NTGKSQGTQQ RQLLSRLQID PVMVETMEMS QDYYDMESMV HADTRSFILK KPKLSEEIVV
TPNQDSGMKT ADALRVLSGH LMQTRDLVQP DKPASPKFIV TLDGVPSPPG YMSDQEEEMC
FEGMKPVNQT SASNKGLRGL LHPQQLHLLS RQLEDPDGSF SNAEMTDLSV AQKPEKLLER
CKYWPACKNG DECVYHHPIS PCKAFPNCKF AEKCLFVHPN CKYDTKCTKA DCPFTHMSRR
ASILTPKPVS SPAPSSNGQL CRYFPACKKM ECPFYHPKHC RFNTQCTRPD CTFYHPTITV
PPRHALKWIR PQSSE
