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Database: UniProt
Entry: A0A3Q1HBA2_ANATE
LinkDB: A0A3Q1HBA2_ANATE
Original site: A0A3Q1HBA2_ANATE 
ID   A0A3Q1HBA2_ANATE        Unreviewed;       287 AA.
AC   A0A3Q1HBA2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=E3 ubiquitin-protein ligase MARCHF8 {ECO:0000256|ARBA:ARBA00040153};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   AltName: Full=Membrane-associated RING finger protein 8 {ECO:0000256|ARBA:ARBA00043184};
DE   AltName: Full=Membrane-associated RING-CH protein VIII {ECO:0000256|ARBA:ARBA00041425};
DE   AltName: Full=RING-type E3 ubiquitin transferase MARCHF8 {ECO:0000256|ARBA:ARBA00043233};
OS   Anabas testudineus (Climbing perch) (Anthias testudineus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX   NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000002148.1, ECO:0000313|Proteomes:UP000265040};
RN   [1] {ECO:0000313|Ensembl:ENSATEP00000002148.1}
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: Cytoplasmic vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004439}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004439}. Early endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004520}. Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004337}. Lysosome membrane
CC       {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004155}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   AlphaFoldDB; A0A3Q1HBA2; -.
DR   STRING; 64144.ENSATEP00000002142; -.
DR   Ensembl; ENSATET00000002172.2; ENSATEP00000002148.1; ENSATEG00000001524.2.
DR   GeneTree; ENSGT00940000158282; -.
DR   InParanoid; A0A3Q1HBA2; -.
DR   OrthoDB; 1342875at2759; -.
DR   Proteomes; UP000265040; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0050687; P:negative regulation of defense response to virus; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR   CDD; cd16807; RING_CH-C4HC3_MARCH8; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45981:SF4; E3 UBIQUITIN-PROTEIN LIGASE MARCHF8; 1.
DR   PANTHER; PTHR45981; LD02310P; 1.
DR   Pfam; PF12906; RINGv; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS51292; ZF_RING_CH; 1.
PE   4: Predicted;
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   TRANSMEM        150..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        192..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          67..128
FT                   /note="RING-CH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51292"
FT   DOMAIN          75..122
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   287 AA;  32580 MW;  36A180FD089D9033 CRC64;
     MNMPLHQISV IPRDVTSSRV SGSGKAKDKD KQNEKPLGHS ASRSSNISKA GSPTSVNAPC
     SFSRTSVSPS SQDICRICHC EGDDESPLIT PCHCTGSLRF VHQGCLQQWI KSSDTRCCEL
     CKYEFIMETK LKPLRKWEKL QMTASERRKI MCSVTFHVIA ITCVVWSLYV LIDRTAEEIR
     QAGRIPGILE WPFWTKLVVV AIGFTGGLVF MYVQCKVYIH LWKRLKAYNR VIYVQNRPDM
     CKKLVLEKPP LVEPNLENKE ALAQTQSDTN SSQYTETEDY SMEVLHV
//
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