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Database: UniProt
Entry: A0A2K5Y4Y1_MANLE
LinkDB: A0A2K5Y4Y1_MANLE
Original site: A0A2K5Y4Y1_MANLE 
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
//
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