PHLA1_MOUSE
ID PHLA1_MOUSE Reviewed; 405 AA.
AC Q62392; Q3TY48; Q3UG87;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Pleckstrin homology-like domain family A member 1;
DE AltName: Full=Proline- and glutamine-rich protein;
DE Short=PQ-rich protein;
DE Short=PQR protein;
DE AltName: Full=T-cell death-associated gene 51 protein;
GN Name=Phlda1; Synonyms=Tdag51;
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 [MRNA], AND FUNCTION.
RX PubMed=8673705; DOI=10.1016/s1074-7613(00)80484-7;
RA Park C.G., Lee S.Y., Kandala G., Lee S.Y., Choi Y.;
RT "A novel gene product that couples TCR signaling to Fas(CD95) expression in
RT activation-induced cell death.";
RL Immunity 4:583-591(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-405.
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-405.
RC STRAIN=129; 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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=10428057; DOI=10.1046/j.1471-4159.1999.0730612.x;
RA Gomes I., Xiong W., Miki T., Rosner M.R.;
RT "A proline- and glutamine-rich protein promotes apoptosis in neuronal
RT cells.";
RL J. Neurochem. 73:612-622(1999).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=10594239; DOI=10.1007/s003359901182;
RA Frank D., Mendelsohn C.L., Ciccone E., Svensson K., Ohlsson R., Tycko B.;
RT "A novel pleckstrin homology-related gene family defined by Ipl/Tssc3,
RT TDAG51, and Tih1: tissue-specific expression, chromosomal location, and
RT parental imprinting.";
RL Mamm. Genome 10:1150-1159(1999).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=12738777; DOI=10.1074/jbc.m212897200;
RA Hossain G.S., van Thienen J.V., Werstuck G.H., Zhou J., Sood S.K.,
RA Dickhout J.G., de Koning A.B., Tang D., Wu D., Falk E., Poddar R.,
RA Jacobsen D.W., Zhang K., Kaufman R.J., Austin R.C.;
RT "TDAG51 is induced by homocysteine, promotes detachment-mediated programmed
RT cell death, and contributes to the development of atherosclerosis in
RT hyperhomocysteinemia.";
RL J. Biol. Chem. 278:30317-30327(2003).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=15037619; DOI=10.1074/jbc.m400661200;
RA Toyoshima Y., Karas M., Yakar S., Dupont J., Helman L., LeRoith D.;
RT "TDAG51 mediates the effects of insulin-like growth factor I (IGF-I) on
RT cell survival.";
RL J. Biol. Chem. 279:25898-25904(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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: Seems to be involved in regulation of apoptosis. May be
CC involved in detachment-mediated programmed cell death. May mediate
CC apoptosis during neuronal development. May be involved in regulation of
CC anti-apoptotic effects of IGF1. Required for TCR-induced apoptosis and
CC expression of TNFRSF6/FAS in a T-cell hybridoma cell line. May be
CC involved in translational regulation. {ECO:0000269|PubMed:15037619,
CC ECO:0000269|PubMed:8673705}.
CC -!- SUBUNIT: Interacts with RPL14, EIF3S7 and PABPC4. {ECO:0000250}.
CC -!- INTERACTION:
CC Q62392; P25685: DNAJB1; Xeno; NbExp=2; IntAct=EBI-309727, EBI-357034;
CC Q62392; P08107: HSPA1B; Xeno; NbExp=2; IntAct=EBI-309727, EBI-629985;
CC Q62392; Q92598: HSPH1; Xeno; NbExp=2; IntAct=EBI-309727, EBI-356829;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WV24}.
CC Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q8WV24}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q8WV24}. Note=Colocalizes with intracellular
CC vesicles. {ECO:0000250|UniProtKB:Q8WV24}.
CC -!- TISSUE SPECIFICITY: Widely expressed with very high levels in adult
CC liver and high levels in adult lung. According to PubMed:10428057
CC expressed at low levels in liver. Expressed at increased levels in
CC atherosclerotic lesions observed in hyperhomocysteinema.
CC {ECO:0000269|PubMed:10428057, ECO:0000269|PubMed:10594239,
CC ECO:0000269|PubMed:12738777}.
CC -!- INDUCTION: Induced by IGF-I. {ECO:0000269|PubMed:15037619}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC52674.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH10295.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE34715.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U44088; AAC52674.1; ALT_INIT; mRNA.
DR EMBL; AK148063; BAE28322.1; -; mRNA.
DR EMBL; AK158890; BAE34715.1; ALT_SEQ; mRNA.
DR EMBL; BC010295; AAH10295.1; ALT_INIT; mRNA.
DR CCDS; CCDS24167.2; -.
DR RefSeq; NP_033370.2; NM_009344.3.
DR AlphaFoldDB; Q62392; -.
DR BioGRID; 204087; 2.
DR IntAct; Q62392; 4.
DR MINT; Q62392; -.
DR STRING; 10090.ENSMUSP00000132815; -.
DR iPTMnet; Q62392; -.
DR PhosphoSitePlus; Q62392; -.
DR jPOST; Q62392; -.
DR MaxQB; Q62392; -.
DR PaxDb; Q62392; -.
DR PeptideAtlas; Q62392; -.
DR PRIDE; Q62392; -.
DR ProteomicsDB; 287931; -.
DR Antibodypedia; 4254; 243 antibodies from 31 providers.
DR DNASU; 21664; -.
DR Ensembl; ENSMUST00000164773; ENSMUSP00000132815; ENSMUSG00000020205.
DR GeneID; 21664; -.
DR KEGG; mmu:21664; -.
DR UCSC; uc007haf.2; mouse.
DR CTD; 22822; -.
DR MGI; MGI:1096880; Phlda1.
DR VEuPathDB; HostDB:ENSMUSG00000020205; -.
DR eggNOG; ENOG502RZ5Q; Eukaryota.
DR GeneTree; ENSGT00440000039564; -.
DR HOGENOM; CLU_062639_0_0_1; -.
DR InParanoid; Q62392; -.
DR OMA; GWGGWPI; -.
DR OrthoDB; 1412115at2759; -.
DR PhylomeDB; Q62392; -.
DR TreeFam; TF332320; -.
DR Reactome; R-MMU-8854521; Interaction between PHLDA1 and AURKA.
DR BioGRID-ORCS; 21664; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Phlda1; mouse.
DR PRO; PR:Q62392; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q62392; protein.
DR Bgee; ENSMUSG00000020205; Expressed in parotid gland and 289 other tissues.
DR Genevisible; Q62392; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0045210; P:FasL biosynthetic process; IDA:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR042832; PHLA1/2/3.
DR PANTHER; PTHR15478; PTHR15478; 2.
DR SMART; SM00233; PH; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Cytoplasmic vesicle; Nucleus; Reference proteome;
KW Repeat.
FT CHAIN 1..405
FT /note="Pleckstrin homology-like domain family A member 1"
FT /id="PRO_0000053898"
FT DOMAIN 153..277
FT /note="PH"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..344
FT /note="16 X 2 AA repeats of P-Q"
FT REGION 354..377
FT /note="11 X 2 AA repeats of P-H"
FT COMPBIAS 37..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..353
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..378
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 209
FT /note="P -> R (in Ref. 2; BAE28322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 45583 MW; 87F50D81EFC44C55 CRC64;
MRRTPAAERL SELGFPPRRG RQEPPFPLGV TRGWGGWPIE KRREGPRPVP FSERSPEDGR
EQPAHGSGIL WRVRTRLSLC RDPEPPPPPP PLCLLRVSLL CALRAGGRGS RWGEDGAGLL
LLPPAGASGS LKAERSSSTP YAGRMLENSG CKALKEGVLE KRSDGLLQLW KKKCCILTEE
GLLLIPPKQL QQQQQQQQPG QGTAEPSQPS GPTVASLEPP VKLKELHFSN MKTVDCVERK
GKYMYFTVVM TEGKEIDFRC PQDQGWNAEI TLQMVQYKNR QAILAVKSTR QKQQHLVQQQ
PPQTQQIQPQ PQPQIQPQPQ PQIQPQPQPQ PQPQPQPQPQ PQPQQLHSYP HPHPHPYSHP
HQHPHPHPHP HPHPHPHPYQ LQHAHQPLHS QPQGHRLLRS TSNSA
