ID   HECD2_PONAB             Reviewed;         776 AA.
AC   Q5RD78;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase HECTD2;
DE            EC=2.3.2.26 {ECO:0000250|UniProtKB:Q5U5R9};
DE   AltName: Full=HECT domain-containing protein 2;
DE   AltName: Full=HECT-type E3 ubiquitin transferase HECTD2;
GN   Name=HECTD2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC       E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC       directly transfers the ubiquitin to targeted substrates.
CC       {ECO:0000250|UniProtKB:Q5U5R9}.
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=2.3.2.26; Evidence={ECO:0000250|UniProtKB:Q5U5R9};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:Q5U5R9}.
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DR   EMBL; CR858038; CAH90279.1; -; mRNA.
DR   RefSeq; NP_001125126.1; NM_001131654.1.
DR   AlphaFoldDB; Q5RD78; -.
DR   SMR; Q5RD78; -.
DR   STRING; 9601.ENSPPYP00000002871; -.
DR   GeneID; 100172010; -.
DR   KEGG; pon:100172010; -.
DR   CTD; 143279; -.
DR   eggNOG; KOG0941; Eukaryota.
DR   InParanoid; Q5RD78; -.
DR   OrthoDB; 339404at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   CDD; cd00078; HECTc; 1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..776
FT                   /note="Probable E3 ubiquitin-protein ligase HECTD2"
FT                   /id="PRO_0000240853"
FT   DOMAIN          437..776
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        744
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   MOD_RES         9
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CDU6"
SQ   SEQUENCE   776 AA;  88142 MW;  B1B5C8F349CD7A44 CRC64;
     MSEAVRVPSP ATPLVVAAAA PEERKGKESE REKLPPIVSA GAGATAGLDR GAKGQISTFS
     SFISAVSPKK EAAENRSSPA HLVFPNIKNV RDQPPICLDV RQKQRTSMDA SSSEMKAPVL
     PEPIHPIQPK TVKDFQEDVE KVKSSGDWKA VHDFYLTTFD SFPELNAAFK KDATASFNTI
     EDSGINAKFV NAVYDTLLNT PQDIQKTVLK GIINSLLREW KGPRTKDDLR AYFVLLQNPQ
     FNNTSTYVIY AHLLRQIATL VEADHHFLVH WFKRLSQKRF KQLVERLLQF ISLRLFPAKP
     EEFPPVTKCS WWIPSAAKVL ALLNTANNLV HPPLIPYTDF YNSTLDHIDL MEEYHTWQNF
     GNSHRFSFCQ YPFVISVAAK KIIIQRDSEQ QMINIARQSL VDKVSRRQRP DMNMLFLNMK
     VRRTHLVSDS LDELTRKRAD LKKKLKVTFV GEAGLDMGGL TKEWFLLLIR QIFHPDYGMF
     TYHKDSHCHW FSSFKCDNYS EFRLVGILMG LAVYNSITLD IRFPPCCYKK LLSPPIIPSD
     QNIPVGICSV TVDDLCQIMP ELAHGLSELL SHEGNVEEDF YSTFQVFQEE FGIIKSYNLK
     PGGDKISVTN QNRKEYVQLY TDFLLNKSIY KQFAAFYYGF HSVCASNALM LLRPEEVEIL
     VCGSPDLDMH ALQRSTQYDG YAKTDLTIKY FWDVVLGFPL DLQKKLLHFT TGSDRVPVGG
     MADLNFKISK NETSTNCLPV AHTCFNQLCL PPYKSKKDLK QKLIIGISNS EGFGLE