GTSF1_MOUSE
ID GTSF1_MOUSE Reviewed; 167 AA.
AC Q9DAN6;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Gametocyte-specific factor 1 {ECO:0000312|MGI:MGI:1921424};
DE AltName: Full=Protein FAM112B;
GN Name=Gtsf1 {ECO:0000312|MGI:MGI:1921424};
GN Synonyms=Cue110 {ECO:0000303|PubMed:19735653},
GN Fam112b {ECO:0000312|MGI:MGI:1921424};
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=17919994; DOI=10.1016/j.modgep.2007.08.003;
RA Yoshimura T., Miyazaki T., Toyoda S., Miyazaki S., Tashiro F., Yamato E.,
RA Miyazaki J.;
RT "Gene expression pattern of Cue110: a member of the uncharacterized UPF0224
RT gene family preferentially expressed in germ cells.";
RL Gene Expr. Patterns 8:27-35(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19735653; DOI=10.1016/j.ydbio.2009.09.003;
RA Yoshimura T., Toyoda S., Kuramochi-Miyagawa S., Miyazaki T., Miyazaki S.,
RA Tashiro F., Yamato E., Nakano T., Miyazaki J.;
RT "Gtsf1/Cue110, a gene encoding a protein with two copies of a CHHC Zn-
RT finger motif, is involved in spermatogenesis and retrotransposon
RT suppression in murine testes.";
RL Dev. Biol. 335:216-227(2009).
RN [4]
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: Required for spermatogenesis and is involved in the
CC suppression of retrotransposon transcription in male germ cells.
CC {ECO:0000269|PubMed:19735653}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17919994,
CC ECO:0000269|PubMed:19735653}.
CC -!- TISSUE SPECIFICITY: Expressed abundantly in adult testis, at moderate
CC levels in unfertilized eggs and ovaries and weakly in embryonic stem
CC cells. {ECO:0000269|PubMed:17919994}.
CC -!- DEVELOPMENTAL STAGE: In the male gonad, barely detected at 13.5 dpc or
CC at birth, detected weakly on postnatal day 14 and maximally expressed
CC in the 4- or 7-week-old mouse testis but not detected in the epididymis
CC of the 7-week-old mouse (at protein level). In the female gonad, low
CC levels detected at birth (at protein level). In the adult testis,
CC present predominantly in pachytene spermatocytes and round spermatids
CC but not in spermatogonia, preleptotene spermatocytes or elongating
CC spermatids (at protein level). {ECO:0000269|PubMed:17919994}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice grow normally and appear healthy but
CC males are sterile due to massive germ cell apoptotic death after
CC postnatal day 14 with meiocytes ceasing meiotic progression before the
CC early meitoic phase. There is also increased transcription of LINE-1
CC and IAP retrotransposons accompanied by demethylation of their promoter
CC regions. {ECO:0000269|PubMed:19735653}.
CC -!- SIMILARITY: Belongs to the UPF0224 (FAM112) family. {ECO:0000305}.
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DR EMBL; AK005675; BAB24181.1; -; mRNA.
DR CCDS; CCDS49744.1; -.
DR RefSeq; NP_083073.1; NM_028797.1.
DR RefSeq; XP_006521554.1; XM_006521491.2.
DR RefSeq; XP_011244051.1; XM_011245749.2.
DR RefSeq; XP_011244052.1; XM_011245750.2.
DR RefSeq; XP_011244053.1; XM_011245751.1.
DR PDB; 6X46; NMR; -; A=1-115.
DR PDBsum; 6X46; -.
DR AlphaFoldDB; Q9DAN6; -.
DR SMR; Q9DAN6; -.
DR IntAct; Q9DAN6; 1.
DR STRING; 10090.ENSMUSP00000023129; -.
DR PhosphoSitePlus; Q9DAN6; -.
DR REPRODUCTION-2DPAGE; IPI00118855; -.
DR PaxDb; Q9DAN6; -.
DR PRIDE; Q9DAN6; -.
DR ProteomicsDB; 271063; -.
DR Antibodypedia; 48366; 99 antibodies from 17 providers.
DR Ensembl; ENSMUST00000023129; ENSMUSP00000023129; ENSMUSG00000022487.
DR Ensembl; ENSMUST00000136480; ENSMUSP00000116366; ENSMUSG00000022487.
DR Ensembl; ENSMUST00000141364; ENSMUSP00000119234; ENSMUSG00000022487.
DR Ensembl; ENSMUST00000146675; ENSMUSP00000122193; ENSMUSG00000022487.
DR Ensembl; ENSMUST00000153930; ENSMUSP00000114244; ENSMUSG00000022487.
DR GeneID; 74174; -.
DR KEGG; mmu:74174; -.
DR UCSC; uc007xyd.2; mouse.
DR CTD; 121355; -.
DR MGI; MGI:1921424; Gtsf1.
DR VEuPathDB; HostDB:ENSMUSG00000022487; -.
DR eggNOG; KOG4376; Eukaryota.
DR GeneTree; ENSGT00940000156784; -.
DR InParanoid; Q9DAN6; -.
DR OMA; TANFCGN; -.
DR OrthoDB; 1359124at2759; -.
DR PhylomeDB; Q9DAN6; -.
DR TreeFam; TF323837; -.
DR BioGRID-ORCS; 74174; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q9DAN6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9DAN6; protein.
DR Bgee; ENSMUSG00000022487; Expressed in seminiferous tubule of testis and 39 other tissues.
DR ExpressionAtlas; Q9DAN6; baseline and differential.
DR Genevisible; Q9DAN6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR007917; GTSF1_vertebrate.
DR InterPro; IPR022776; TRM13/UPF0224_CHHC_Znf_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR21402:SF9; PTHR21402:SF9; 1.
DR Pfam; PF05253; zf-U11-48K; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS51800; ZF_CHHC_U11_48K; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Differentiation; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Spermatogenesis; Zinc; Zinc-finger.
FT CHAIN 1..167
FT /note="Gametocyte-specific factor 1"
FT /id="PRO_0000221622"
FT ZN_FING 14..41
FT /note="CHHC U11-48K-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT ZN_FING 48..75
FT /note="CHHC U11-48K-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01141"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WW33"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:6X46"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:6X46"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:6X46"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:6X46"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:6X46"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:6X46"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:6X46"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:6X46"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:6X46"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6X46"
SQ SEQUENCE 167 AA; 19083 MW; CF370101EAAF7314 CRC64;
MEDTYIDSLD PEKLLQCPYD KNHQIRACRF PYHLIKCRKN HPDVANKLAT CPFNARHQVP
RAEISHHISS CDDKSCIEQD VVNQTRNLGQ ETLAESTWQC PPCDEDWDKD LWEQTSTPFV
WGTASFCGNN SPANNIVMEH KSNLASGMRV PKSLPYVLPW KNNGNAQ
