ID Q5BU71_LYMST Unreviewed; 816 AA.
AC Q5BU71;
DT 12-APR-2005, integrated into UniProtKB/TrEMBL.
DT 12-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Tripartite motif protein L-TRIM {ECO:0000313|EMBL:AAX20126.1};
OS Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Lymnaeidae; Lymnaea.
OX NCBI_TaxID=6523 {ECO:0000313|EMBL:AAX20126.1};
RN [1] {ECO:0000313|EMBL:AAX20126.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15866048; DOI=10.1016/j.mcn.2005.01.005;
RA van Diepen M.T., Spencer G.E., van Minnen J., Gouwenberg Y., Bouwman J.,
RA Smit A.B., van Kesteren R.E.;
RT "The molluscan RING-finger protein L-TRIM is essential for neuronal
RT outgrowth.";
RL Mol. Cell. Neurosci. 29:74-81(2005).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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DR EMBL; AY864892; AAX20126.1; -; mRNA.
DR AlphaFoldDB; Q5BU71; -.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd14960; NHL_TRIM2_like; 1.
DR CDD; cd16586; RING-HC_TRIM2_like_C-VII; 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; IPR047153; TRIM45/56/19.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR25462; BONUS, ISOFORM C-RELATED; 1.
DR PANTHER; PTHR25462:SF229; NHL (RING FINGER B-BOX COILED COIL) DOMAIN CONTAINING; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
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 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 187..228
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 395..497
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 548..588
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 594..635
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 636..677
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 681..724
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 728..771
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 772..815
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REGION 132..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 88842 MW; 5E1AFEA0210FAE02 CRC64;
MTSVRMTSTA TRFWDSNINL LSCAICDQRY KDPKVLPCLH TFCELCLSNV IPSESLSVTC
PVCRQQSILP LDGVSALQTN GFVLNLLNAI TSPDVCTSCG VISSRPTSKC LDCQKFLCDT
CSVQHCNMDN TNNNIQDPSP KLDPDNKMNA HSENGEGQGL HHVVSLAEMA SRKSPPLTNG
GIKDDGGGDI VCPNHAGSPL KYYCSLCDTA VCETCTQVEH IGHMTVVLSE AVTEHKTTLT
SLVARVRQMT PEVERAIEEV EVMQNQLHAN TTDAESKIKE LFDELVTILE ERKQSAIEEL
AKVSAVKEYV LDEQKKALHK HLSCISSCCE LTEDSLLHGN DMDVVMVKKE MAGKLNDLLT
NGVTLQPETN PLALFDEKDF EGLRETINCL GSVCNNSAIP QQTTVGGEAF SGCVAGKAST
VTVTTRDRNG DLVKTGFAPI TAFISTDKSE DRLTPTITDH QNGTYDLTFV LQAPGIYYLT
VTMFGQHTKG SPYKIRAVDI GEANGDGSAR IPRTMAVKQK GVKRPSSSRS QGSSNRRTNR
IEDDLIIRIG VKGRNKGEFS NPQGLCYHEE KVLVADSNNQ AVQVFVPSGE CRLKFGTPGR
APGKIQRPTG VAVTQNGNYL VADYDNKWIS VFSPDGKYMS RIGAGRLQGP KGVAVDREGR
IIVVDNKSSC ILIFQSNGKL LHKFGTRGNR DDQFAGPHYA AINENNDIII SDFHNHCVKV
FDRDGAFKFC FGSNGEGNGQ FNAPTGVAVD DKGNMLVADW GNSRIQVFDS TGSFLSYVNT
ASEPLYGPQG LAVTTQGILV VADSGNHCIK YYKYLQ
//