GMCL1_MOUSE
ID GMCL1_MOUSE Reviewed; 524 AA.
AC Q920G9; Q9DBW5; Q9QUP6;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Germ cell-less protein-like 1;
DE Short=mGcl-1;
DE AltName: Full=DP-interacting protein;
DE Short=DIP;
GN Name=Gmcl1; Synonyms=Gcl, Gcl1;
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].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=10448096; DOI=10.1006/bbrc.1999.1160;
RA Kimura T., Yomogida K., Iwai N., Kato Y., Nakano T.;
RT "Molecular cloning and genomic organization of mouse homologue of
RT Drosophila germ cell-less and its expression in germ lineage cells.";
RL Biochem. Biophys. Res. Commun. 262:223-230(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=10727854; DOI=10.1016/s0925-4773(99)00335-4;
RA Leatherman J.L., Kaestner K.H., Jongens T.A.;
RT "Identification of a mouse germ cell-less homologue with conserved activity
RT in Drosophila.";
RL Mech. Dev. 92:145-153(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TMPO-BETA.
RX PubMed=11591818; DOI=10.1242/jcs.114.18.3297;
RA Nili E., Cojocaru G.S., Kalma Y., Ginsberg D., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Berger R., Shaklai S., Amariglio N., Brok-Simoni F.,
RA Simon A.J., Rechavi G.;
RT "Nuclear membrane protein LAP2beta mediates transcriptional repression
RT alone and together with its binding partner GCL (germ-cell-less).";
RL J. Cell Sci. 114:3297-3307(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [6]
RP INTERACTION WITH TFDP2.
RX PubMed=9878064; DOI=10.1093/emboj/18.1.212;
RA de la Luna S., Allen K.E., Mason S.L., La Thangue N.B.;
RT "Integration of a growth-suppressing BTB/POZ domain protein with the DP
RT component of the E2F transcription factor.";
RL EMBO J. 18:212-228(1999).
RN [7]
RP INTERACTION WITH TSG101.
RX PubMed=12927808; DOI=10.1016/s0006-291x(03)01497-9;
RA Masuhara M., Nagao K., Nishikawa M., Kimura T., Nakano T.;
RT "Enhanced degradation of MDM2 by a nuclear envelope component, mouse germ
RT cell-less.";
RL Biochem. Biophys. Res. Commun. 308:927-932(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND THR-66, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Possible function in spermatogenesis. Enhances the
CC degradation of MDM2 and increases the amount of p53 probably by
CC modulating the nucleocytoplasmic transport.
CC -!- SUBUNIT: Interacts with TMPO-Beta, TSG101 and TFDP2. Interacts with EMD
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels throughout
CC development and in adult tissues.
CC -!- DEVELOPMENTAL STAGE: Highest levels in pachytene and diplotene stage
CC spermatocytes and primordial germ cells of the male and the female.
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DR EMBL; AF163665; AAD52204.1; -; mRNA.
DR EMBL; AF186095; AAF01415.1; -; mRNA.
DR EMBL; AF282322; AAK69515.1; -; mRNA.
DR EMBL; AK004716; BAB23499.1; -; mRNA.
DR EMBL; BC054767; AAH54767.1; -; mRNA.
DR CCDS; CCDS20316.1; -.
DR PIR; JC7090; JC7090.
DR RefSeq; NP_035948.3; NM_011818.3.
DR AlphaFoldDB; Q920G9; -.
DR SMR; Q920G9; -.
DR BioGRID; 204775; 5.
DR DIP; DIP-24259N; -.
DR STRING; 10090.ENSMUSP00000001185; -.
DR iPTMnet; Q920G9; -.
DR PhosphoSitePlus; Q920G9; -.
DR EPD; Q920G9; -.
DR MaxQB; Q920G9; -.
DR PaxDb; Q920G9; -.
DR PRIDE; Q920G9; -.
DR ProteomicsDB; 271402; -.
DR DNASU; 23885; -.
DR Ensembl; ENSMUST00000001185; ENSMUSP00000001185; ENSMUSG00000001157.
DR GeneID; 23885; -.
DR KEGG; mmu:23885; -.
DR UCSC; uc009csl.2; mouse.
DR CTD; 64395; -.
DR MGI; MGI:1345156; Gmcl1.
DR VEuPathDB; HostDB:ENSMUSG00000001157; -.
DR eggNOG; KOG4682; Eukaryota.
DR GeneTree; ENSGT00940000156185; -.
DR HOGENOM; CLU_025961_2_0_1; -.
DR InParanoid; Q920G9; -.
DR OMA; GFNYGMD; -.
DR OrthoDB; 1111791at2759; -.
DR PhylomeDB; Q920G9; -.
DR TreeFam; TF316048; -.
DR BioGRID-ORCS; 23885; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Gmcl1; mouse.
DR PRO; PR:Q920G9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q920G9; protein.
DR Bgee; ENSMUSG00000001157; Expressed in spermatocyte and 245 other tissues.
DR ExpressionAtlas; Q920G9; baseline and differential.
DR Genevisible; Q920G9; MM.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0016363; C:nuclear matrix; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0007281; P:germ cell development; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; TAS:MGI.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR043380; Gcl-like.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR23231; PTHR23231; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Nucleus; Phosphoprotein;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..524
FT /note="Germ cell-less protein-like 1"
FT /id="PRO_0000087521"
FT DOMAIN 106..176
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 47..53
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 83..89
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 151
FT /note="P -> L (in Ref. 3; AAK69515)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="S -> N (in Ref. 3; AAK69515)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="D -> N (in Ref. 3; AAK69515)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="C -> W (in Ref. 3; AAK69515)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="E -> G (in Ref. 4; BAB23499)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 59654 MW; 3DCC974A758D14C3 CRC64;
MGALSSRVLR PAGRTEQPEP TPGAGGAARR SDAGEDAGHS FCYCPGGRKR KRSSGTFCYC
HPDSETDDDE DEGDEQQRLL NTPRRKKLKS TSKYIYQTLF LNGENSDIKI CALGEEWSLH
KIYLCQSGYF SSMFSGSWKE SSMNIIELEI PDQNIDIEAL QVAFGSLYRD DVLIKPSRVV
AILAAACMLQ LDGLIQQCGE TMKETISVRT VCGYYTSAGT YGLDSVKKKC LEWLLNNLMT
HQSVELFKEL SINVMKQLIG SSNLFVMQVE MDVYTALKKW MFLQLVPSWN GSLKQLLTET
DVWFSKWKKD FEGTTFLETE QGKPFAPVFR HLRLQYIISD LASARIIEQD SLVPSEWLAA
VYKQQWLAML RAEQDSEVGP QEINKEELEG NSMRCGRKLA KDGEYCWRWT GFNFGFDLLV
TYTNRYIIFK RNTLNQPCSG SVSLQPRRSI AFRLRLASFD SSGKLICSRA TGYQILTLEK
DQEQVVMNLD SRLLIFPLYI CCNFLYISPE KRTESNRHPE NPGH
