ID   RNF39_PANTR             Reviewed;         420 AA.
AC   Q7YR31; Q1XHV6; Q1XHV9;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=RING finger protein 39;
DE   AltName: Full=Protein HZFw;
GN   Name=RNF39; Synonyms=HZFW;
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=12799463; DOI=10.1073/pnas.1230533100;
RA   Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
RA   Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
RA   Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., Meyer A.,
RA   Ikeo K., Gojobori T., Bahram S., Inoko H.;
RT   "Comparative sequencing of human and chimpanzee MHC class I regions unveils
RT   insertions/deletions as the major path to genomic divergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA   Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA   Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA   Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA   Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA   Inoko H., Bahram S.;
RT   "Rapid evolution of major histocompatibility complex class I genes in
RT   primates generates new disease alleles in humans via hitchhiking
RT   diversity.";
RL   Genetics 173:1555-1570(2006).
CC   -!- FUNCTION: May play a role in prolonged long term-potentiation (LTP)
CC       maintenance. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; BA000041; BAC78186.1; -; Genomic_DNA.
DR   EMBL; AB210195; BAE92811.1; -; Genomic_DNA.
DR   EMBL; AB210196; BAE92814.1; -; Genomic_DNA.
DR   RefSeq; NP_001107640.1; NM_001114168.1.
DR   AlphaFoldDB; Q7YR31; -.
DR   SMR; Q7YR31; -.
DR   STRING; 9598.ENSPTRP00000073690; -.
DR   PaxDb; 9598-ENSPTRP00000054045; -.
DR   Ensembl; ENSPTRT00000087266.1; ENSPTRP00000073690.1; ENSPTRG00000031491.2.
DR   GeneID; 750730; -.
DR   KEGG; ptr:750730; -.
DR   CTD; 80352; -.
DR   VGNC; VGNC:57537; RNF39.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000162641; -.
DR   InParanoid; Q7YR31; -.
DR   OMA; WEVETTD; -.
DR   OrthoDB; 207577at2759; -.
DR   Proteomes; UP000002277; Chromosome 6.
DR   Bgee; ENSPTRG00000031491; Expressed in primary visual cortex and 8 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   CDD; cd16592; RING-HC_RNF39; 1.
DR   CDD; cd12888; SPRY_PRY_TRIM7_like; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR   PANTHER; PTHR24103:SF557; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..420
FT                   /note="RING finger protein 39"
FT                   /id="PRO_0000056082"
FT   DOMAIN          210..420
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         88..135
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          246..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   420 AA;  45579 MW;  2F537C90A52D5599 CRC64;
     MWWRDLTRLR LWLKREAIPG EGRKAAKVNA GVGEKGIYTA SSRGGPPSAR SKAVTVVAEG
     AASRSWLSMD APELGPGLVE RLEQLATCPL CGGSFEDPVL LACEHSFCRA CLARRWGTPP
     ATGTEASPTA CPCCGLPCPR RSLRSNVRLA VEVRISRELR EKLAEPGARA GRRRGGRIPT
     MGCLDLPGED MRKTWRRFEV PTPKSSNSED DLPEDYPVVK NMLHRLTADL TLDPGTAHRR
     LLISADRRSV QLAPPGTPAP PDGPKRFDQL PAVLGAQGFG AGRHCWEVET ADAASCRDSS
     GEDEDDEESH YAVGAAGESV QRKGCVRLCP AGAVWAVEGR GGRLWALTAP EPTLLGGVEP
     PPRRIRVDLD WERGRVAFYD GRSLDLLYAF QAPGPLGERI FPLFCTCDPR APLRIVPAES
//