ID A0A2K5I901_COLAP Unreviewed; 862 AA.
AC A0A2K5I901;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000013110.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000013110.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_011796367.1; XM_011940977.1.
DR AlphaFoldDB; A0A2K5I901; -.
DR Ensembl; ENSCANT00000036022.1; ENSCANP00000013110.1; ENSCANG00000029706.1.
DR GeneID; 105510976; -.
DR CTD; 10299; -.
DR OrthoDB; 1342875at2759; -.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16702; RING_CH-C4HC3_MARCH6; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13145:SF0; E3 UBIQUITIN-PROTEIN LIGASE MARCHF6; 1.
DR PANTHER; PTHR13145; SSM4 PROTEIN; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 242..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 320..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 432..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 474..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 627..651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 672..695
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 715..737
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 757..780
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 800..819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..62
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 137..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..198
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 97203 MW; 6CFF7F31B36CCB9C CRC64;
MDTAEEDICR VCRSEGTPEK PLYHPCVCTG SIKFIHQECL VQWLKHSRKE YCELCKHRFA
FTPSRIYKCL FTGSVSSLLT LPLDMLSTEN LLADCLQGCF VVTCTLCAFI SLVWLREQIV
HGGAPIWLEH AAPPFNAAGH HQNEAPAGGN GAENVAADQP ANPPAENAVV GENPDAQDDQ
AEEEEEDNEE EDDAGVEDAA DANNGAQDDM NWNALEWDRA AEELTWERML GLDGSLVFLE
HVFWVVSLNT LFILVFAFCP YHIGHFSLVG LGFEEHVQAS HFEGLITTIV GYILLAITLI
ICHGLATLVK FHRSRRLLGV CYIVVKVSLL VVVEIGVFPL ICGWWLDICS LEMFDATLKD
RELSFQSAPG TTMFLHWLVG MVYVFYFASF ILLLREVLRP GVLWFLRNLN DPDFNPVQEM
IHLPIYRHLR RFILSVIVFG SIVLLMLWLP IRIIKSVLPH FLPYNVMLYS DAPVSELSLE
LLLLQVVLPA LLEQGHTRQW LKGLVRAWTV TAGYLLDLHS YLLGDQEENE NSANQQVNNN
QHARNNNAIP VVGEGLHAAH QAILQQGGPV GFQPYRRPLN FPLRIFLLIV FMCITLLIAS
LICLTLPVFA GRWLMSFWTG TAKIHELYTA ACGLYVCWLT IRAVTVMVAW MPQGRRVIFQ
KVKEWSLMIM KTLIVAVLLA GVVPLLLGLL FELVIVAPLR VPLDQTPLFY PWQDWALGVL
HAKIIAAITL MGPQWWLKTV IEQVYANGIR NIDLHYIVRR LAAPVISVLL LSLCVPYVIA
SGVVPLLGVT AEMQNLVHRR IYPFLLMVVV LMAILSFQVR QFKRLYEHIK NDKYLVGQRL
VNYERKSGKQ GSSPAPPQSS QE
//
