ID F7AUU5_XENTR Unreviewed; 711 AA.
AC F7AUU5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 4.
DT 27-MAR-2024, entry version 73.
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=trim2 {ECO:0000313|Ensembl:ENSXETP00000003876};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000003876};
RN [1] {ECO:0000313|Ensembl:ENSXETP00000003876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000003876};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [2] {ECO:0000313|Ensembl:ENSXETP00000003876}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) 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 AlphaFoldDB; F7AUU5; -.
DR Ensembl; ENSXETT00000003876; ENSXETP00000003876; ENSXETG00000001837.
DR AGR; Xenbase:XB-GENE-942459; -.
DR Xenbase; XB-GENE-942459; trim2.
DR Bgee; ENSXETG00000001837; Expressed in brain and 13 other cell types or tissues.
DR ExpressionAtlas; F7AUU5; baseline.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19824; Bbox2_TRIM2_C-VII; 1.
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 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..386
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 444..483
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 487..530
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 531..572
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 576..619
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 625..666
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 667..710
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
SQ SEQUENCE 711 AA; 77368 MW; 44316435D7A5858A CRC64;
MASEGSNIPS PVVRQIDKQF LICSICLDRY KNPKVLPCLH TFCERCLQNY IPAHSLTLSC
PVCRQTSILP EKGVSALQNN FFITNLMDVL QRSPDNGIEE SSILETVSAV AAGKPLSCPN
HDGNVMEFYC QSCETAMCQD CTGGEHAEHP TVPLKDVVEQ HKAALQAQLD AVKKRLPEID
SALQCVSEIV NQLASQKTSI VEEIHSTFDD LQKTLNVRKS VLLMELEVNY GLKHKVLQAQ
LDTLIEGQES IKSCTTFTAQ ALNHGTETEV LLVKKQMSDK LNELAEQDFP LQPHENDQLD
FIVETEGLKK SIHNLGTILT TNAVASETVA TGEGLRQSVI GQPMSVTITT KDKDGELCKT
GSAYISAELF TPDGSVTDGE VVDNKNEGVK RRVKSPGSGH VKQKAVKRPA SMYSTGKRKE
NPIEDDLIFR VGSRKDEDVR SLTGTKGRNK GEFTNLQGVA ASTNGKILIA DSNNQCVQIF
SNDGQFKSRF GIRGRSPGQL QRPTGVAVHP SGDIIIADYD NKWVSIFSAD GKFKTKIGSG
KLMGPKGVSV DRNGHIIVVD NKACCVFIFQ PNGKIVTRFG SRGNGDKQFA GPHFAAVNSN
NEIIVTDFHN HSVKVFNQDG EFILKFGSNG EGNGQFNAPT GVAVDSNGNI IVADWGNSRI
QVFDGSGSFL SYINTSADPL YGPQGLSLTS DGHVVVADSG NHCFKVYRYL Q
//
