LIN41_CHICK
ID LIN41_CHICK Reviewed; 876 AA.
AC Q1PRL4; Q2QDD9; Q3LAF8;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM71;
DE EC=2.3.2.27;
DE AltName: Full=Protein lin-41 homolog;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM71 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 71;
GN Name=TRIM71; Synonyms=LIN41;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=16477647; DOI=10.1002/dvdy.20712;
RA Kanamoto T., Terada K., Yoshikawa H., Furukawa T.;
RT "Cloning and regulation of the vertebrate homologue of lin-41 that
RT functions as a heterochronic gene in Caenorhabditis elegans.";
RL Dev. Dyn. 235:1142-1149(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 156-876, AND DEVELOPMENTAL STAGE.
RX PubMed=16245339; DOI=10.1002/dvdy.20591;
RA Lancman J.J., Caruccio N.C., Harfe B.D., Pasquinelli A.E., Schageman J.J.,
RA Pertsemlidis A., Fallon J.F.;
RT "Analysis of the regulation of lin-41 during chick and mouse limb
RT development.";
RL Dev. Dyn. 234:948-960(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 277-876.
RC TISSUE=Embryo;
RA Howell G.R., Beatie K., Towers M., Wilson S.A., Tickle C.A.;
RT "The role of Lin41 in limb development.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION.
RX PubMed=16247770; DOI=10.1002/dvdy.20599;
RA Maller Schulman B.R., Esquela-Kerscher A., Slack F.J.;
RT "Reciprocal expression of lin-41 and the microRNAs let-7 and mir-125 during
RT mouse embryogenesis.";
RL Dev. Dyn. 234:1046-1054(2005).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that cooperates with the
CC microRNAs (miRNAs) machinery and promotes embryonic stem cells
CC proliferation and maintenance. Binds to miRNAs and participates in
CC post-transcriptional repression of transcripts. Required to maintain
CC proliferation and prevent premature differentiation of neural
CC progenitor cells during early neural development.
CC {ECO:0000250|UniProtKB:Q1PSW8}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q2Q1W2}.
CC -!- DEVELOPMENTAL STAGE: Expression is strong at early stages and decreases
CC as development proceeds. At stage 9, expressed in the segmental plate
CC mesoderm. At stage 15, expressed in branchial axs. At stage 19-27,
CC expressed in branchial axs, limb buds and tail buds. At stage 27-29,
CC expressed in the tips of digits. {ECO:0000269|PubMed:16245339,
CC ECO:0000269|PubMed:16477647}.
CC -!- DOMAIN: The NHL domain, containing the 6 NHL repeats, is necessary and
CC sufficient to target RNA but not to repress mRNA. The minimal region
CC needed to execute repression consists of the coiled coil domain and the
CC Filamin repeat. The RING-type domain is dispensable for mRNA
CC repression. {ECO:0000250|UniProtKB:Q2Q1W2}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ57335.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAJ32595.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ278876; ABB88564.1; -; mRNA.
DR EMBL; DQ117917; AAZ57335.1; ALT_INIT; mRNA.
DR EMBL; AM087669; CAJ32595.1; ALT_INIT; mRNA.
DR RefSeq; NP_001032352.2; NM_001037275.2.
DR AlphaFoldDB; Q1PRL4; -.
DR SMR; Q1PRL4; -.
DR STRING; 9031.ENSGALP00000030515; -.
DR PaxDb; Q1PRL4; -.
DR GeneID; 428445; -.
DR KEGG; gga:428445; -.
DR CTD; 131405; -.
DR VEuPathDB; HostDB:geneid_428445; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q1PRL4; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q1PRL4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q1PRL4; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0010586; P:miRNA metabolic process; ISS:UniProtKB.
DR GO; GO:0035278; P:miRNA-mediated gene silencing by inhibition of translation; ISS:UniProtKB.
DR GO; GO:0021915; P:neural tube development; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0060964; P:regulation of miRNA-mediated gene silencing; ISS:UniProtKB.
DR GO; GO:2000177; P:regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; ISS:UniProtKB.
DR Gene3D; 2.120.10.30; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 6.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 6.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Developmental protein; Metal-binding;
KW Reference proteome; Repeat; RNA-binding; RNA-mediated gene silencing;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..876
FT /note="E3 ubiquitin-protein ligase TRIM71"
FT /id="PRO_0000279513"
FT REPEAT 487..588
FT /note="Filamin"
FT REPEAT 601..644
FT /note="NHL 1"
FT REPEAT 648..691
FT /note="NHL 2"
FT REPEAT 695..738
FT /note="NHL 3"
FT REPEAT 742..785
FT /note="NHL 4"
FT REPEAT 789..832
FT /note="NHL 5"
FT REPEAT 836..876
FT /note="NHL 6"
FT ZN_FING 12..90
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 200..247
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 281..322
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 344..373
FT /evidence="ECO:0000255"
FT COILED 399..434
FT /evidence="ECO:0000255"
FT COMPBIAS 171..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 876 AA; 94188 MW; 0BEEA115A2816F58 CRC64;
MASFPEADFQ VCPLCKEMCG SPAPLSSNSS TSSSSSQTSG SSGGGGSSCG GAARRLHVLP
CLHAFCRQCL EAQRHPAAGD ALKLRCPICD QKVVISEPSG MDALPSSNFL LSNLLDVVVV
AAAADEQKNG RAAGSGPAAG SGAGGGGANN RHHGRPPPHR AAAAASSPAA GSAAPSASSS
SSSGGGGPAA LLLRRPHSRQ GEPRCSSCDE GNAASSRCLD CQEHLCDNCV RAHQRVRLTK
DHFIERFAAG PAAASAGPAA PLALSPPYPA SPYNILSVFP ERASYCQHHD DEVLHFYCDT
CSVPICRECT MGRHVGHSFI YLQDALQDSR TLTIQLLADA QQGRQAIQLS IEQAQAVAEQ
VEMKAKVVQS EVKAVTTRHK KALEERECEL LWKVEKIRQV KAKSLYLQVE KLRQNLNKLD
NTISAVQQVL EEGRTIDILL ARDRMLAQVQ ELKNVRGLLQ PQEDDRIMFT PPDQALYMAI
KSMGFVSSGA FAPLTKATGE GLKRALQGKV ASFTVIGYDH DGEPRLSGGD MISAVVMGPD
GNLFGADVSD QQNGTYLVSY RPQLEGEHLV SVMMCNQHIE NSPFKVVVKS GRSYIGIGLP
GLSFGSEGDS DGKLCRPWGV SVDKEGYIIV ADRSNNRIQV FKPCGTFHHK FGTLGSRPGQ
FDRPAGVACD VSRRIVVADK DNHRIQIFTF EGQFILKFGE KGTKNGQFNY PWDVAVNAEG
KILVSDTRNH RVQLFGPDGV FLNKYGFEGA LWKHFDSPRG VTFNHEGHLV VTDFNNHRLL
VIHADCQSAR FLGSEGSGNG QFLRPQGVAV DQEGRIIVAD SRNHRVQIFE SNGSFLCKFG
AQGSGFGQMD RPSGIAVTPD GMIVVVDFGN NRILVF
