ID A0A3B4Y2V4_SERLL Unreviewed; 402 AA.
AC A0A3B4Y2V4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=E3 ubiquitin-protein ligase RNF167-like {ECO:0000313|Ensembl:ENSSLDP00000022356.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000022356.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000022356.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A3B4Y2V4; -.
DR STRING; 1841481.ENSSLDP00000022356; -.
DR Ensembl; ENSSLDT00000023078.1; ENSSLDP00000022356.1; ENSSLDG00000017455.1.
DR GeneTree; ENSGT00940000163061; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd02123; PA_C_RZF_like; 1.
DR CDD; cd16796; RING-H2_RNF13; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR044744; ZNRF4/RNF13/RNF167_PA.
DR PANTHER; PTHR47168:SF6; PROTEASE-ASSOCIATED (PA) RING_U-BOX ZINC FINGER FAMILY PROTEIN; 1.
DR PANTHER; PTHR47168; RING ZINC FINGER DOMAIN SUPERFAMILY PROTEIN-RELATED; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 183..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 241..283
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 286..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 44820 MW; CB568B494640D6BF CRC64;
MVHLGVWSVG ARLNVPILVF CSILVTSPTH AYIYAHYSNM TSMLFEDLPA LFGSPLPKDG
LMGVLVVSRP LNGCAAIDPP PPLPPSYDSN TTKFIVLIRR YDCNFDIKVL HAQRAGYNAA
IVHNMYSDTL LNMNYSNDTI AEEIEIPSVF TSYYASQILR NFIIPEQGAY VILKPEFAFP
LSYYLIPFTG VVGMIILVMF VVLIIRCVRY RKRLRKNRLS KEQLKRIPTH RFTKGDDYDL
CAICLDEYEE GDKLRVLPCS HAYHCKCVDP WLTQTKKTCP VCKQRVTRNN PEHSESESEE
ETGGRGEGEG AEGEADSERT PLLRPSNPGS PSGSPGAYSA TTTTTTAQCL ASPAHCDSPI
LGYEGYYSPQ EDTDSESDDS GEDRHHTDDD TAQLIGRDRV EV
//
