ID A0A2K5Y4Y1_MANLE Unreviewed; 855 AA.
AC A0A2K5Y4Y1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=MARCHF6 {ECO:0000313|Ensembl:ENSMLEP00000010613.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000010613.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000010613.1}
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 AlphaFoldDB; A0A2K5Y4Y1; -.
DR Ensembl; ENSMLET00000034028.1; ENSMLEP00000010613.1; ENSMLEG00000029472.1.
DR GeneTree; ENSGT00940000155171; -.
DR Proteomes; UP000233140; 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:UP000233140};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 235..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 467..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 578..600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..644
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 665..688
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 708..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 750..773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 793..812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..55
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 130..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..191
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 855 AA; 96411 MW; BA2036493BB3064A CRC64;
ICRVCRSEGT PEKPLYHPCV CTGSIKFIHQ ECLVQWLKHS RKEYCELCKH RFAFTPSRIY
KCLFTGSVSS LLTLPLDMLS TENLLADCLQ GCFVVTCTLC AFISLVWLRE QIVHGGAPIW
LEHAAPPFNA AGHHQNEAPA GGNGAENVAA DQPANPPAEN AVVGENPDAQ DDQAEEEEED
NEEEDDAGVE DAADANNGAQ DDMNWNALEW DRAAEELTWE RMLGLDGSLV FLEHVFWVVS
LNTLFILVFA FCPYHIGHFS LVGLGFEEHV QASHFEGLIT TIVGYILLAI TLIICHGLAT
LVKFHRSRRL LGVCYIVVKV SLLVVVEIGV FPLICGWWLD ICSLEMFDAT LKDRELSFQS
APGTTMFLHW LVGMVYVFYF ASFILLLREV LRPGVLWFLR NLNDPDFNPV QEMIHLPIYR
HLRRFILSVI VFGSIVLLML WLPIRIIKSV LPHFLPYNVM LYSDAPVSEL SLELLLLQVV
LPALLEQGHT RQWLKGLVRA WTVTAGYLLD LHSYLLGDQE ENENSANQQV NNNQHARNNN
AIPVVGEGLH AAHQAILQQG GPVGFQPYRR PLNFPLRIFL LIVFMCITLL IASLICLTLP
VFAGRWLMSF WTGTAKIHEL YTAACGLYVC WLTIRAVTVM VAWMPQGRRV IFQKVKEWSL
MIMKTLIVAV LLAGVVPLLL GLLFELVIVA PLRVPLDQTP LFYPWQDWAL GVLHAKIIAA
ITLMGPQWWL KTVIEQVYAN GIRNIDLHYI VRRLAAPVIS VLLLSLCVPY VIASGVVPLL
GVTAEMQNLV HRRIYPFLLM VVVLMAILSF QVRQFKRLYE HIKNDKYLVG QRLVNYERKS
GKQGSSPAPP QSSQE
//