ID   CBLL2_MACFA             Reviewed;         422 AA.
AC   Q4R361;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=E3 ubiquitin-protein ligase CBLL2;
DE            EC=2.3.2.27;
DE   AltName: Full=Cbl proto-oncogene-like protein 2;
DE   AltName: Full=E3 ubiquitin-protein ligase ZNF645;
DE   AltName: Full=RING-type E3 ubiquitin transferase ZNF645;
DE   AltName: Full=Zinc finger protein 645;
DE   AltName: Full=c-Cbl-like protein 2;
GN   Name=CBLL2; Synonyms=ZNF645; ORFNames=QtsA-19347;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of
CC       ubiquitin moieties onto substrate proteins. May operate on tyrosine-
CC       phosphorylated SRC substrates. {ECO:0000250|UniProtKB:Q8N7E2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q8N7E2};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q8N7E2}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9JIY2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N7E2}.
CC       Note=Localized over the postacrosomal perinuclear theca region and the
CC       entire length of sperm tail. {ECO:0000250|UniProtKB:Q8N7E2}.
CC   -!- DOMAIN: The HYB domain forms a phosphotyrosine-binding pocket upon
CC       dimerization, and mediates as well the recognition of its flanking
CC       acidic amino acids. {ECO:0000250|UniProtKB:Q9JIY2}.
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DR   EMBL; AB179407; BAE02458.1; -; mRNA.
DR   RefSeq; NP_001270666.1; NM_001283737.1.
DR   AlphaFoldDB; Q4R361; -.
DR   SMR; Q4R361; -.
DR   STRING; 9541.XP_005593225.1; -.
DR   GeneID; 101926745; -.
DR   CTD; 158506; -.
DR   eggNOG; KOG2932; Eukaryota.
DR   OrthoDB; 765364at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   CDD; cd16508; RING-HC_HAKAI_like; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR040380; HAKAI-like_RING-HC.
DR   InterPro; IPR040383; HAKAI/CBLL2.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR041042; Znf_Hakai.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR13480; PTHR13480; 1.
DR   Pfam; PF18408; zf_Hakai; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..422
FT                   /note="E3 ubiquitin-protein ligase CBLL2"
FT                   /id="PRO_0000056317"
FT   ZN_FING         54..94
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         109..135
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          93..151
FT                   /note="HYB domain"
FT                   /evidence="ECO:0000250"
FT   REGION          190..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..404
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  48206 MW;  26825F9A57EC7F71 CRC64;
     MPAGEQEREY NEDRKYYSKG VKLVRKKKKI PGYSWGDIKI NIIGEKDDSP IHFCDKCDLP
     IKIYGRIIPC KHAFCYNCAN LYDKIGYKIC PRCSYPVLRI EEHKRGSVFM CSVVQGCKRT
     YLSQKSLQAH IKRRHKRARK QVASASLEKL RPHIAPPRTE IAEIPKRLLD RDHLNYIPPE
     QHTMMSLPSM QQMPHEQHNQ PHKDLQVPPP ELSPSPPFPI QWETVSVFTR KHGNLIVDHI
     QNNSDSGAKK PSPPDYYPEY QSQPVVSSPC HIMPQKQHYA PPPSPSSPVN YPMPYPPQDV
     GTPNLVSSQA PALTTTYDLS LGYIIAQVPP YMNSPPPCAP QSQNGNSSAS EFAFHHYNPN
     FLTQFTENQE TLSPQFTQTD ATDHRRWPAW KGLPPPPPTW SPPPSTLHGG SHHSYQRRHR
     PY