ZFY_PANTR
ID ZFY_PANTR Reviewed; 801 AA.
AC Q6B4Z5; Q52V17;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Zinc finger Y-chromosomal protein;
GN Name=ZFY;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15703238; DOI=10.1093/molbev/msi109;
RA Ebersberger I., Meyer M.;
RT "A genomic region evolving toward different GC contents in humans and
RT chimpanzees indicates a recent and regionally limited shift in the mutation
RT pattern.";
RL Mol. Biol. Evol. 22:1240-1245(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hughes J.F., Pyntikova T., Skaletsky H., Minx P.J., Rozen S., Wilson R.K.,
RA Page D.C.;
RT "The DNA sequence of the chimpanzee Y chromosome.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable transcriptional activator. Binds to the consensus
CC sequence 5'-AGGCCY-3' (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: The binding of ZFY to DNA is mediated by the interaction of the
CC GGCC core base pairs with zinc fingers 12 and 13. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. ZFX/ZFY subfamily. {ECO:0000305}.
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; AY913763; AAX94760.1; -; Genomic_DNA.
DR EMBL; AY679779; AAT84367.1; -; mRNA.
DR RefSeq; NP_001009003.1; NM_001009003.1.
DR RefSeq; XP_009443987.1; XM_009445712.2.
DR RefSeq; XP_009443992.1; XM_009445717.2.
DR AlphaFoldDB; Q6B4Z5; -.
DR SMR; Q6B4Z5; -.
DR STRING; 9598.ENSPTRP00000038749; -.
DR PaxDb; Q6B4Z5; -.
DR PRIDE; Q6B4Z5; -.
DR Ensembl; ENSPTRT00000085840; ENSPTRP00000071475; ENSPTRG00000022471.
DR GeneID; 449580; -.
DR KEGG; ptr:449580; -.
DR CTD; 7544; -.
DR VGNC; VGNC:5894; ZFY.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158684; -.
DR HOGENOM; CLU_021097_0_0_1; -.
DR InParanoid; Q6B4Z5; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF335557; -.
DR Proteomes; UP000002277; Chromosome Y.
DR Bgee; ENSPTRG00000022471; Expressed in testis and 11 other tissues.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR006794; Transcrp_activ_Zfx/Zfy-dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 7.
DR Pfam; PF04704; Zfx_Zfy_act; 1.
DR SMART; SM00355; ZnF_C2H2; 13.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..801
FT /note="Zinc finger Y-chromosomal protein"
FT /id="PRO_0000047262"
FT ZN_FING 421..443
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 452..474
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 484..506
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 515..538
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 544..566
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 572..595
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 601..623
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 629..652
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 658..680
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 686..709
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 715..737
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 743..766
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 772..795
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17012"
SQ SEQUENCE 801 AA; 90513 MW; 703152A8956963CE CRC64;
MDEDEFELQP QEPNSFFDGI GADATHMDGD QIVVEIQEAV FVSNIVDSDI AVHNFVPDDP
DSVVIQDVIE DVVIEEDVQC SDILEEADVS ENVIIPEQVL DSDVTEEVSL PHCTVPDDVL
ASDITSTSMS MPEHVLTSES MHVCDIEHVE HMVHDSVVEA EIITDPLTSD IVSEEVLVAD
CAPEAIIDAS GISVDQQDND KASCEDYLMI SLDDAGKIEH DGSTGVTIDA ESEMDPCKVD
STCPEVIKVY IFKADPGEDD LGGTVDIVES EPENDHGVEL LDQNSSIRVP REKMVYMTVN
DSQQEDEDLN VAEIADEVYM EVIVGEEDAA VAAAAAAVHE QQIDEDEMKT FVPIAWAAAY
GNNSDGIENR NGTASALLHI DESAGLGRLA KQKPKKKRRP DSRQYQTAII IGPDGHPLTV
YPCMICGKKF KSRGFLKRHM KNHPEHLAKK KYHCTDCDYT TNKKISLHNH LESHKLTSKA
EKAIECDECG KHFSHAGALF THKMVHKEKG ANKMHKCKFC EYETAEQGLL NRHLLAVHSK
NFPHICVECG KGFRHPSELK KHMRIHTGEK PYQCQYCEYR SADSSNLKTH IKTKHSKEMP
LKCDICLLTF SDTKEVQQHT LVHQESKTHQ CLHCDHKSSN SSDLKRHVIS VHTKDYPHKC
EMCEKGFHRP SELKKHVAVH KGKKMHQCRH CDFKIADPFV LSRHILSVHT KDLPFRCKRC
RKGFRQQNEL KKHMKTHSGR KVYQCEYCEY STTDASGFKR HVISIHTKDY PHRCEYCKKG
FRRPSEKNQH IMRHHKEVGL P