ID A0A2Y9S159_PHYMC Unreviewed; 398 AA.
AC A0A2Y9S159;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=E3 ubiquitin-protein ligase RNF149 {ECO:0000313|RefSeq:XP_023972346.1};
GN Name=RNF149 {ECO:0000313|RefSeq:XP_023972346.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023972346.1};
RN [1] {ECO:0000313|RefSeq:XP_023972346.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023972346.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_007130305.1; XM_007130243.1.
DR RefSeq; XP_023972346.1; XM_024116578.3.
DR AlphaFoldDB; A0A2Y9S159; -.
DR STRING; 9755.ENSPCTP00005016621; -.
DR Ensembl; ENSPCTT00005018333; ENSPCTP00005016621; ENSPCTG00005011779.
DR KEGG; pcad:102976818; -.
DR InParanoid; A0A2Y9S159; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000248484; Chromosome 12.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR CDD; cd02122; PA_GRAIL_like; 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 PANTHER; PTHR46539; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 1.
DR PANTHER; PTHR46539:SF30; RING FINGER PROTEIN 149; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..398
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015996549"
FT TRANSMEM 199..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 267..308
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 50..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 43196 MW; F98F11DD5589F3D5 CRC64;
MAWRRRRPEA RGGARGALAL LALVLCAPGA RGRALEWYSA VVSTEYVDPQ TNRSVRSVSE
SGRFGESSPK EGARGLVGVP RAEDRDPEGC APRTRFLVPG GREAAPWVAL VARGGCTFKD
KVLAAARRNA SAVVLYNEER HGNLTAPMSH AGTGNIVVIM VSYPKGREIV DLVQKDIPVT
MTIGLGTRHV QEFISGQSVV FVAIAFITMM IISLAWLIFY YIQRFLYTGS QFGSQSHRKE
TKKLIGQLPL HTVKHGEKGI DVDAESCAVC IENFKGKDVI RILPCKHIFH RICIDPWLLD
HRTCPMCKLD VIKALGYWGE LEDVQETPAP ESPPGGVSTA DLSLTLPDGD RSDAGSSSLP
TTSDSTPPCE ASFKEDAGEN TALLEPSRSD PQCEGPVS
//