BNC1_MOUSE
ID BNC1_MOUSE Reviewed; 961 AA.
AC O35914; O54886;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Zinc finger protein basonuclin-1;
GN Name=Bnc1; Synonyms=Bnc;
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=129; TISSUE=Skin;
RX PubMed=9300825; DOI=10.1016/s0378-1119(97)00176-5;
RA Matsuzaki K., Iuchi S., Green H.;
RT "Conservation of human and mouse basonuclins as a guide to important
RT features of the protein.";
RL Gene 195:87-92(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-262, FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=9687312; DOI=10.1095/biolreprod59.2.388;
RA Mahoney M.G., Tang W., Xiang M.M., Moss S.B., Gerton G.L., Stanley J.R.,
RA Tseng H.;
RT "Translocation of the zinc finger protein basonuclin from the mouse germ
RT cell nucleus to the midpiece of the spermatozoon during spermiogenesis.";
RL Biol. Reprod. 59:388-394(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22266914; DOI=10.1002/dvg.22014;
RA Zhang X., Chou W., Haig-Ladewig L., Zeng W., Cao W., Gerton G.,
RA Dobrinski I., Tseng H.;
RT "BNC1 is required for maintaining mouse spermatogenesis.";
RL Genesis 50:517-524(2012).
RN [4]
RP FUNCTION, INTERACTION WITH HSF2BP, AND SUBCELLULAR LOCATION.
RX PubMed=23707421; DOI=10.1016/j.febslet.2013.04.049;
RA Wu Y., Liao S., Wang X., Wang S., Wang M., Han C.;
RT "HSF2BP represses BNC1 transcriptional activity by sequestering BNC1 to the
RT cytoplasm.";
RL FEBS Lett. 587:2099-2104(2013).
CC -!- FUNCTION: Transcriptional activator (PubMed:9687312, PubMed:23707421).
CC It is likely involved in the regulation of keratinocytes terminal
CC differentiation in squamous epithelia and hair follicles (By
CC similarity). Required for the maintenance of spermatogenesis
CC (PubMed:22266914). It is involved in the positive regulation of oocyte
CC maturation, probably acting through the control of BMP15 levels and
CC regulation of AKT signaling cascade (By similarity). May also play a
CC role in the early development of embryos (PubMed:9687312).
CC {ECO:0000250|UniProtKB:Q01954, ECO:0000269|PubMed:22266914,
CC ECO:0000269|PubMed:23707421, ECO:0000269|PubMed:9687312}.
CC -!- SUBUNIT: Interacts with HSF2BP (via C-terminus).
CC {ECO:0000269|PubMed:23707421}.
CC -!- INTERACTION:
CC O35914; Q9D4G2: Hsf2bp; NbExp=4; IntAct=EBI-8527667, EBI-8527688;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23707421,
CC ECO:0000269|PubMed:9687312}. Cytoplasm {ECO:0000269|PubMed:23707421,
CC ECO:0000269|PubMed:9687312}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:23707421}. Note=Relocates to the midpiece of the
CC flagellum during late spermiogenesis in spermatids.
CC {ECO:0000269|PubMed:9687312}.
CC -!- TISSUE SPECIFICITY: Epidermis and germ cells of testis and ovary.
CC {ECO:0000269|PubMed:9687312}.
CC -!- DEVELOPMENTAL STAGE: Appears to be expressed by primary and secondary
CC spermatocytes and spermatids. Detected in oocytes within the primary
CC follicles. It is also present in secondary oocytes.
CC {ECO:0000269|PubMed:9687312}.
CC -!- PTM: Phosphorylation on Ser-505 and Ser-509 leads to cytoplasmic
CC localization. {ECO:0000250|UniProtKB:Q01954}.
CC -!- DISRUPTION PHENOTYPE: Viable, although fertility is severely reduced in
CC both males and females. Males have significantly reduced testis size,
CC with progressive degeneration of seminiferous epithelium and loss of
CC germ cells from 8 weeks of age. Sperm motility is also reduced.
CC {ECO:0000269|PubMed:22266914}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U88064; AAC53347.1; -; mRNA.
DR EMBL; AF025301; AAB94675.1; -; mRNA.
DR AlphaFoldDB; O35914; -.
DR IntAct; O35914; 1.
DR MINT; O35914; -.
DR STRING; 10090.ENSMUSP00000026096; -.
DR iPTMnet; O35914; -.
DR PhosphoSitePlus; O35914; -.
DR PaxDb; O35914; -.
DR PRIDE; O35914; -.
DR ProteomicsDB; 273789; -.
DR MGI; MGI:1097164; Bnc1.
DR eggNOG; ENOG502QR8N; Eukaryota.
DR InParanoid; O35914; -.
DR PhylomeDB; O35914; -.
DR ChiTaRS; Asic2; mouse.
DR PRO; PR:O35914; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35914; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:ARUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000182; F:rDNA binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:1900195; P:positive regulation of oocyte maturation; ISO:MGI.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; ISO:MGI.
DR GO; GO:0006356; P:regulation of transcription by RNA polymerase I; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0042060; P:wound healing; IMP:MGI.
DR InterPro; IPR040436; Disconnected-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR15021; PTHR15021; 1.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Differentiation; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Spermatogenesis; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..961
FT /note="Zinc finger protein basonuclin-1"
FT /id="PRO_0000046933"
FT ZN_FING 325..348
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 353..382
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 687..711
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 715..743
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 895..918
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 923..950
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 210..219
FT /note="Hydrophobic"
FT REGION 370..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 501..507
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 544..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01954"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01954"
FT CONFLICT 100
FT /note="A -> V (in Ref. 2; AAB94675)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="Y -> D (in Ref. 2; AAB94675)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 961 AA; 106659 MW; 82CF949BF913C68F CRC64;
MAEAIGCTLN CSCQCFKPGK INHRQCEQCR HGWVAHALSK LRIPPVYPTS QVEIVQSNVV
FDISSLMLYG TQAIPVRLKI LLDRLFSVLK QDEVLQILHA LDWTLQDYIR GYVLQDASGK
VLDHWSIMTS EEEVATLQQF LRFGETKSIV ELMAIQEKEE QSVIVPPTTA NVDIRAFIES
CGHRSASLPT PVDKGSPGGM HPFENLISNM TFMLPFQFFN PLPPALIGSL PEQYMLEQGQ
DQSQEPKQEL HGPFSDSSFL TSTPFQVEKE QCLNCPETVP QKEDSAHLSD SSSYSIASKL
ERTQLSPEAK VKPERNSLSA KKGRVFCTAC EKTFYDKGTL KIHYNAVHLK IKHKCTIEGC
NMVFSSLRSR NRHSANPNPR LHMPMNRNNR DKDLRNSLNL ASSETYKRPG FTVVSPDCGP
LPGYTGSVED SKGQPAFSSI GQNGVLFPNL KTVQPVLPFY RSPATPAELA NTPGMLPSLP
LLSSSIPEQL VSTDMPFDAL PKKKSRKSSM PIKIEKEAVE IAEEKRHSLS SDDEVPLQVV
SEDEPEDSSP RSDRVPEEQH TQLSLEEPLP QGERACHLES VIESHGALSR TLEQTTLTER
EAEQKVALSS VMPREVEDGG HERHFTAGLV PQIPFPDYME LQQRLLAGGL FGALSNRGMA
FPFLEESKEL EHLGEHALVR QKEEARFQCD ICKKTFKNAC SMKTHEKNTH ARETHACTVE
GCGAAFPSRR SRDRHSSNLS LHQKVLNEEA LETSEDHFRA AYLLQDVAKE AYQDVAFTPQ
ASQTSVIFKG TSGMGSLVYP ISQVHSASLE SYNSGPPSEG TILDLSTTSS MKSESSSHSS
WDSDGVSEEG TALMEDSDGN CEGQSLVSGE DEYPLCVLME KADQSLASLP SGLPITCHLC
QKIYSNKGTF RAHYKTVHLR QLHKCKVPGC NTMFSSVRSR NRHSQNPNLH KSLASSPSHL
Q
