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Database: UniProt
Entry: A0A2Y9Q899_DELLE
LinkDB: A0A2Y9Q899_DELLE
Original site: A0A2Y9Q899_DELLE 
ID   A0A2Y9Q899_DELLE        Unreviewed;       762 AA.
AC   A0A2Y9Q899;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
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_022455294.1};
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_022455294.1};
RN   [1] {ECO:0000313|RefSeq:XP_022455294.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022455294.1};
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_022455294.1; XM_022599586.2.
DR   AlphaFoldDB; A0A2Y9Q899; -.
DR   Ensembl; ENSDLET00000022820; ENSDLEP00000020715; ENSDLEG00000015055.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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..670
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          674..717
FT                   /note="NHL"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT   REPEAT          718..761
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   762 AA;  83490 MW;  268CBB038CE14684 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 AGPHFAAVNS NNEIIVTDFH
     NHSVKVFNQE GEFMLKFGSN GEGNGQFNAP TGVAVDSNGN IIVADWGNSR IQVFDGSGSF
     LSYINTSADP LYGPQGLALT SDGHVVVADS GNHCFKVYRY LQ
//
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