ID A0A3Q7S2K1_VULVU Unreviewed; 615 AA.
AC A0A3Q7S2K1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=MARCH7 {ECO:0000313|RefSeq:XP_025849978.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025849978.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025849978.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025849978.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025849978.1};
RG RefSeq;
RL Submitted (NOV-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}.
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DR RefSeq; XP_025849978.1; XM_025994193.1.
DR AlphaFoldDB; A0A3Q7S2K1; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd16812; RING_CH-C4HC3_MARCH7; 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; PTHR14471:SF1; E3 UBIQUITIN-PROTEIN LIGASE MARCHF7; 1.
DR PANTHER; PTHR14471; MARCH7/10 E3 UBIQUITIN PROTEIN LIGASE FAMILY MEMBER; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 580..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 433..503
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 1..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 68236 MW; 54982839362BF554 CRC64;
MDSSWRHNQV PRSSSMVLGS FGTDLMRERR DLERRADSSI SNLMDYSHRS GDFTTSSYGQ
DRVPSSYSQG ARPKDNSVST LQLNTSSTNH QMPSEHHTIP CSRDNSRNSL RSNFSPRELE
SPQSSTQPGF SYISNRDETS TISSSDRVGS SQRSFQESSD NESRRSTRRL LSRIASSMSS
TFFSRRSSQD SLNTRSLSSE NSYVSPRILT ASQSRSNSAS TSDVPDSRAS EASQGFRFLR
RRWGLSSLSQ NHSSEPDSEN FNQESEGRNT GPWLSSSLRN RCTPLFSRRR REGRDESSRI
PTSDIPSRSH HIFRRESNEV VHLEAQSDPL GATANRAQAS ASSSNAATGG SPSDSAQSGR
NTGITGILPG SLFRFAVPPA LGNNLTDNVM ITVDIIPSGW SSSDGKSDKT KSAPSRDPER
LQKIKESLLL EDSEEEEGDL CRICQMAAAS SSNLLIEPCK CTGSLQYVHQ ECMKKWLQAK
INSGSSLEAV TTCELCKEKL QLNLEDFDIH ELHRAHANEQ AEYEFISSGL YLVVLLHLCE
QSFSDMMGNT NEPSTRVRVS NIGVGDGERV QCCKCLLWKA HFFICSHSVF FGGGFILKCI
LTKNKKKCIL KIKIL
//
