ID A0A091D6U7_FUKDA Unreviewed; 407 AA.
AC A0A091D6U7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=E3 ubiquitin-protein ligase TRIM13 {ECO:0000313|EMBL:KFO27834.1};
GN ORFNames=H920_10720 {ECO:0000313|EMBL:KFO27834.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO27834.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO27834.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO27834.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; KN122849; KFO27834.1; -; Genomic_DNA.
DR RefSeq; XP_010635263.1; XM_010636961.2.
DR RefSeq; XP_010635264.1; XM_010636962.2.
DR RefSeq; XP_010635265.1; XM_010636963.2.
DR RefSeq; XP_019064957.1; XM_019209412.1.
DR AlphaFoldDB; A0A091D6U7; -.
DR STRING; 885580.ENSFDAP00000001204; -.
DR Ensembl; ENSFDAT00000015207; ENSFDAP00000001204; ENSFDAG00000011244.
DR GeneID; 104871160; -.
DR CTD; 10206; -.
DR eggNOG; KOG2177; Eukaryota.
DR OMA; NLQVNYS; -.
DR OrthoDB; 5383069at2759; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19767; Bbox2_TRIM13_C-XI; 1.
DR CDD; cd16762; RING-HC_TRIM13_C-V; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF609; E3 UBIQUITIN-PROTEIN LIGASE TRIM13; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
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, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT TRANSMEM 316..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..58
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 89..131
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
SQ SEQUENCE 407 AA; 47009 MW; 8CC9A6573EF9C04D CRC64;
MELLEEDLTC PICCSLFDDP RVLPCSHNFC KKCLEGLLEG NVRNSLWRPS PFKCPTCRKE
TSATGVNSLQ VNYALKGIVE KYNKIKISPK MPVCKGHLGQ PLNIFCLTDM QLICGICATR
GEHTKHVFCS IEDAYVQERD AFESLIQSFE TWHRGDALSR LDTLESSKRK SLQLLTKDSD
KVKEFFEKLQ HTLDQKKNEI LSDFETMKLA VMQAYDPEIN KLNTILQEQR MAFNIAEAFK
DVSEPIVFLQ QMQEFREKIK VIKETPLPPS NLPTSPFMKN FDTSQWEDIK LVDVDKLYLP
QDTGTLISKI PPNFCLLLVI VLLLGLLIFF GPTIFLEWSL FDELATWKDH LSNFSSYLTK
TADFVEQSVF YWEEMLDGFF FFSERVKNFT LVVLNNVAEF VCKYKLL
//
