ID A0A2Y9QIR0_DELLE Unreviewed; 766 AA.
AC A0A2Y9QIR0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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|RefSeq:XP_022455293.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022455293.1};
RN [1] {ECO:0000313|RefSeq:XP_022455293.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022455293.1};
RG RefSeq;
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_022455293.1; XM_022599585.2.
DR AlphaFoldDB; A0A2Y9QIR0; -.
DR STRING; 9749.A0A2Y9QIR0; -.
DR KEGG; dle:111187691; -.
DR InParanoid; A0A2Y9QIR0; -.
DR OrthoDB; 5387006at2759; -.
DR Proteomes; UP000248483; Unplaced.
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 Reference proteome {ECO:0000313|Proteomes:UP000248483};
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 41..82
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 131..172
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 338..439
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 491..534
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 538..581
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 582..623
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 627..674
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 678..721
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 722..765
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 450..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 766 AA; 83877 MW; 10E74BECDE0FFDB4 CRC64;
MRQRAGSKTA GPPCQWSRMA SEATNIPSPV VRQIDKQFLI CSICLERYKN PKVLPCLHTF
CERCLQNYIP AHSLTLSCPV CRQTSILPEK GVAALQNNFF ITNLMDVLQR TPGSNAEESS
ILETVTAVAA GKPLSCPNHD GNVMDFYCQS CETAMCRECT EGEHAEHPTV PLKDVVEQHK
ASLQVQLDAV NKRLPEIDSA LQFISEIIHQ LTDQKASIVD DIHSTFDELQ KTLNVRKSVL
LMELEVNYGL KHKVLQSQLD TLLEGQESIK SCSSFTAQAL NHGTETEVLL VKKQMSEKLN
ELADQDFPLH PRENDQLDFI VETEGLKKSI HNLGTILTTN AVASETVATG EGLRQTIIGQ
PMSVTITTKD KDGELCKTGN AYITAELSTP DGSVADGEIL DNKNGTYEFL YTVQKEGDFT
LSLRLYDQHI RGSPFKLKVI RSADVSPTTE GVKRRVKSPG SGHVKQKAVK RPASMYSTGK
RKENPIEDDL IFRVGTKGRN KGEFTNLQGV AASTNGKILI ADSNNQCVQI FSNDGQFKSR
FGIRGRSPGQ LQRPTGVAVH PSGDIIIADY DNKWVSIFSS DGKFKTKIGS GKLMGPKGVS
VDRNGHIIVV DNKACCVFIF QPNGKIVTRF GSRGNGDRQF AGTLDGPHFA AVNSNNEIIV
TDFHNHSVKV FNQEGEFMLK FGSNGEGNGQ FNAPTGVAVD SNGNIIVADW GNSRIQVFDG
SGSFLSYINT SADPLYGPQG LALTSDGHVV VADSGNHCFK VYRYLQ
//
