ID   ZFY_GORGO               Reviewed;         801 AA.
AC   Q52V16;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Zinc finger Y-chromosomal protein;
GN   Name=ZFY;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
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).
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}.
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DR   EMBL; AY913765; AAX94761.1; -; Genomic_DNA.
DR   EMBL; AY913764; AAX94761.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q52V16; -.
DR   SMR; Q52V16; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   InParanoid; Q52V16; -.
DR   Proteomes; UP000001519; Unplaced.
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:0000977; F:RNA polymerase II transcription regulatory region 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   3: Inferred from homology;
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_0000232440"
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;  90489 MW;  F56412E665A7C7C8 CRC64;
     MDEDEFELQP QEPNSFFDGI GADATHMDGD QIVVEIQEAV FVSNIVDSDI TVHNFVPDDP
     DSVVIQDVIE DVVIEEDVQC SDILEEADVS ENVIIPEQVL ESDVTEEVSL PHCTVPDDVL
     ASDITSTSTS MPEHVLTSES MHVCDIGHVE 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
     FKCDICLLTF SDTKEVQQHT LVHQESKTHQ CLHCDHKSSN SSDLKRHVIS VHTKDYPHKC
     EMCEKGFHRP SELKKHVAVH KGKKMHQCRH CDFKIADPFV LSRHILSVHT KDLPFRCKRC
     RKGFRQQNEL KKHMKTHSGR KVYQCEYCEY STTDASGFKR HVISIHTKDY PHRCEYCKKG
     FRRPSEKNQH IMRHHKEVGL P