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Database: UniProt
Entry: Q5BU71_LYMST
LinkDB: Q5BU71_LYMST
Original site: Q5BU71_LYMST 
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
//
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