ID H2LWS3_ORYLA Unreviewed; 744 AA.
AC H2LWS3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Tripartite motif-containing protein 2 {ECO:0000256|ARBA:ARBA00039484};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=E3 ubiquitin-protein ligase TRIM2 {ECO:0000256|ARBA:ARBA00041590};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM2 {ECO:0000256|ARBA:ARBA00043214};
GN Name=trim2a {ECO:0000313|Ensembl:ENSORLP00000010567.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000010567.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000010567.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000010567.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000010567.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000010567.2};
RG Ensembl;
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}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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DR RefSeq; XP_004066008.1; XM_004065960.2.
DR RefSeq; XP_011475405.1; XM_011477103.1.
DR STRING; 8090.ENSORLP00000044325; -.
DR Ensembl; ENSORLT00000010568.2; ENSORLP00000010567.2; ENSORLG00000008416.2.
DR Ensembl; ENSORLT00000038825.1; ENSORLP00000036981.1; ENSORLG00000008416.2.
DR Ensembl; ENSORLT00000039213.1; ENSORLP00000044325.1; ENSORLG00000008416.2.
DR Ensembl; ENSORLT00000045472.1; ENSORLP00000027655.1; ENSORLG00000008416.2.
DR GeneID; 101163547; -.
DR KEGG; ola:101163547; -.
DR CTD; 100003782; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000155905; -.
DR HOGENOM; CLU_008645_5_0_1; -.
DR OrthoDB; 5387006at2759; -.
DR TreeFam; TF331018; -.
DR Proteomes; UP000001038; Chromosome 1.
DR Bgee; ENSORLG00000008416; Expressed in brain and 12 other cell types or tissues.
DR GO; GO:0030371; F:translation repressor activity; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030099; P:myeloid cell differentiation; IEA:Ensembl.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0060215; P:primitive hemopoiesis; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd14960; NHL_TRIM2_like; 1.
DR CDD; cd16767; RING-HC_TRIM2; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001258; NHL_repeat.
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; PTHR24104; E3 UBIQUITIN-PROTEIN LIGASE NHLRC1-RELATED; 1.
DR PANTHER; PTHR24104:SF50; TRIPARTITE MOTIF-CONTAINING PROTEIN 2; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 6.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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:PRU00024}.
FT DOMAIN 23..64
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 113..154
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 320..421
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 473..516
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 520..563
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 564..605
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 609..652
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 656..699
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 700..743
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
SQ SEQUENCE 744 AA; 81564 MW; E83A3E51A769CF9D CRC64;
MASEISSIPS PVFRQIDKQF LICSICLDRY ENPKVLPCLH TFCERCLQNY IPAHSLTLSC
PVCRQTSILP EKGVAALQSN FFITNLMDVL QRAPDNCSQE DTILNNIACV ATGQLLSCPN
HGGSVMEFYC PPCETAMCQE CTSGEHGEHP TVPLRDVVEQ HKASLQDQLD VAKKRLPEID
SALHMLSEIL QQLTNQKSLI EDDIHTTFDE LQKTLNVRKS VLLMELEVNY GLKQKVLQAQ
LDTLLQGQEG INSSCNFTEQ ALNHGTEAEV LLVKKQMGER LMELASQELP LHPKENNQLD
FLVETEGLKK SIHNLGTIVT TNAVASETVA TGESLRHCVV GVPTSITITT KDKDGELCKM
GNALITTEIS PPDNSRDIGE ILDNKNGTYE YIFTAAKEGT FNLSLRLYNQ HIKGSPFRIK
AIKSIDACPK SDGTKKRLKS PGSGHIKQRA IKRPASMYSS GRRKENPIED DLIFRIGTKG
RNKGEFTNLQ GVAASSLGKV LIADSNNQCV QMFSNDGQFK SRFGVRGRTP GQLQRPTGVA
VHPNGDIIIA DYDNKWVSIF SSEGKFKNKI GSGKLMGPKG VAVDKNGHII VVDNKACCVF
IFQVNGKLVT KFGNRGNGDK QFAGPHFAAV NNNNEIIVTD FHNHSVKVFN TEGEFLLKFG
SNGEGNGQFN APTGVSVDAN GNIIVADWGN SRIQVFDGSG SFLSYINTSA DPLYGPQGLA
LTSDGHVVVA DSGNHCFKVY RYLQ
//
