ID   SPZ1_RAT                Reviewed;         400 AA.
AC   Q6AXY9;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Spermatogenic leucine zipper protein 1;
GN   Name=Spz1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-207, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Transcription factor that binds to the DNA sequence 5'-
CC       CANNTG-3'(E box) and the G-box motif. May play an important role in the
CC       regulation of cell proliferation and differentiation during
CC       spermatogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PPP1CC isoform gamma-2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- PTM: Phosphorylated by MAPK1/ERK2 and MAPK3/ERK1. {ECO:0000250}.
CC   -!- MISCELLANEOUS: The helix-loop-helix and basic motifs form a SPZ1
CC       specific bHLH different from the classical one. {ECO:0000250}.
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DR   EMBL; BC079262; AAH79262.1; -; mRNA.
DR   RefSeq; NP_001019468.1; NM_001024297.1.
DR   AlphaFoldDB; Q6AXY9; -.
DR   SMR; Q6AXY9; -.
DR   STRING; 10116.ENSRNOP00000017408; -.
DR   iPTMnet; Q6AXY9; -.
DR   PhosphoSitePlus; Q6AXY9; -.
DR   PaxDb; Q6AXY9; -.
DR   PRIDE; Q6AXY9; -.
DR   Ensembl; ENSRNOT00000017408; ENSRNOP00000017408; ENSRNOG00000013050.
DR   GeneID; 499510; -.
DR   KEGG; rno:499510; -.
DR   UCSC; RGD:1562395; rat.
DR   CTD; 84654; -.
DR   RGD; 1562395; Spz1.
DR   eggNOG; ENOG502QS87; Eukaryota.
DR   GeneTree; ENSGT00950000182767; -.
DR   HOGENOM; CLU_062447_0_0_1; -.
DR   InParanoid; Q6AXY9; -.
DR   OMA; FNIHVAR; -.
DR   OrthoDB; 1269936at2759; -.
DR   PhylomeDB; Q6AXY9; -.
DR   TreeFam; TF337798; -.
DR   PRO; PR:Q6AXY9; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000013050; Expressed in testis.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   InterPro; IPR042961; Spz1.
DR   PANTHER; PTHR47889; PTHR47889; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..400
FT                   /note="Spermatogenic leucine zipper protein 1"
FT                   /id="PRO_0000280509"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..127
FT                   /note="Helix-loop-helix motif"
FT                   /evidence="ECO:0000255"
FT   REGION          128..193
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255"
FT   REGION          252..273
FT                   /note="Leucine-zipper"
FT   REGION          295..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          182..231
FT                   /evidence="ECO:0000255"
FT   COILED          268..293
FT                   /evidence="ECO:0000255"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         207
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   400 AA;  45814 MW;  535ED083C3FDD2E1 CRC64;
     MADSDSSSEM PAHSPSPSPI PCAKQKPPNT GITISLLEIG SLPTFCCSSF SEPNNNMCPI
     RKQGKVQKFS NLLKDVKDVL KNIAGFEEKT TDGDPFDDTY IPEDLSELNI RGFDKRNKLR
     FKDDLFIHFD PERENTMRQE MLFKSHSAKN MVQKFARDLC NSEEKRGCDG VQLNAKRRRT
     GSVHIRGEYR KLRNNMEQLL QEADHWSKQH NELSELMRSY QECHKEIKDI VDCSRVCSQT
     QNNNEVPSKQ KLEEQVKKLS QDTHSLHLIA ALLENECQIL QQRVDILREL HLHEAGPGHE
     KPLQTSGEQD KKCGEQDKKC GEQDKKCGEQ DKKCPKLAEA EKMDGSKHTM KTTEGTITRK
     PKIFRCPNDC LTKKARNNRF NARVAKKSLV GKRRTISSFR