ID LZTR1_PONAB Reviewed; 840 AA.
AC Q5R4Q7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=Leucine-zipper-like transcriptional regulator 1;
DE Short=LZTR-1;
GN Name=LZTR1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex that mediates ubiquitination of Ras
CC (K-Ras/KRAS, N-Ras/NRAS and H-Ras/HRAS). Is a negative regulator of
CC RAS-MAPK signaling that acts by controlling Ras levels and decreasing
CC Ras association with membranes. {ECO:0000250|UniProtKB:Q8N653}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q8N653}.
CC -!- SUBUNIT: Homodimer. Component of the BCR(LZTR1) E3 ubiquitin ligase
CC complex, at least composed of CUL3, LZTR1 and RBX1. Interacts with Ras
CC (K-Ras/KRAS, N-Ras/NRAS and H-Ras/HRAS). Interacts with RAF1. Interacts
CC with SHOC2. Interacts with PPP1CB. {ECO:0000250|UniProtKB:Q8N653}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:Q8N653}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q8N653}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q8N653}.
CC -!- PTM: Phosphorylated on tyrosine upon induction of apoptosis, leading to
CC its degradation by the proteasome. {ECO:0000250|UniProtKB:Q8N653}.
CC -!- SIMILARITY: Belongs to the LZTR1 family. {ECO:0000305}.
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DR EMBL; CR861188; CAH93259.1; -; mRNA.
DR RefSeq; NP_001126917.1; NM_001133445.1.
DR AlphaFoldDB; Q5R4Q7; -.
DR SMR; Q5R4Q7; -.
DR STRING; 9601.ENSPPYP00000013416; -.
DR GeneID; 100173934; -.
DR KEGG; pon:100173934; -.
DR CTD; 8216; -.
DR eggNOG; KOG0379; Eukaryota.
DR InParanoid; Q5R4Q7; -.
DR OrthoDB; 4338at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR CDD; cd18505; BACK1_LZTR1; 1.
DR CDD; cd18506; BACK2_LZTR1; 1.
DR CDD; cd18308; BTB1_POZ_LZTR1; 1.
DR CDD; cd18309; BTB2_POZ_LZTR1; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 3.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR46376; LEUCINE-ZIPPER-LIKE TRANSCRIPTIONAL REGULATOR 1; 1.
DR PANTHER; PTHR46376:SF1; LEUCINE-ZIPPER-LIKE TRANSCRIPTIONAL REGULATOR 1; 1.
DR Pfam; PF00651; BTB; 2.
DR Pfam; PF01344; Kelch_1; 1.
DR Pfam; PF13415; Kelch_3; 1.
DR Pfam; PF13418; Kelch_4; 2.
DR SMART; SM00225; BTB; 2.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF54695; POZ domain; 2.
DR PROSITE; PS50097; BTB; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Endosome; Golgi apparatus; Kelch repeat; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8N653"
FT CHAIN 2..840
FT /note="Leucine-zipper-like transcriptional regulator 1"
FT /id="PRO_0000260303"
FT REPEAT 79..128
FT /note="Kelch 1"
FT /evidence="ECO:0000255"
FT REPEAT 130..185
FT /note="Kelch 2"
FT /evidence="ECO:0000255"
FT REPEAT 187..238
FT /note="Kelch 3"
FT /evidence="ECO:0000255"
FT REPEAT 239..285
FT /note="Kelch 4"
FT /evidence="ECO:0000255"
FT REPEAT 295..341
FT /note="Kelch 5"
FT /evidence="ECO:0000255"
FT REPEAT 399..450
FT /note="Kelch 6"
FT /evidence="ECO:0000255"
FT DOMAIN 443..537
FT /note="BTB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 667..736
FT /note="BTB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REGION 329..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8N653"
SQ SEQUENCE 840 AA; 94526 MW; 9720A1F196CF44EE CRC64;
MAGPGSTGGQ IGAGALAGGA RSKVAPSVDF DHSCSDSVEY LTLNFGPFET VHRWRRLPPC
DEFVGARRSK HTVVAYKDAI YVFGGDNGKT MLNDLLRFDV KDCSWCRAFT TGTPPAPRYH
HSAVVYGSSM FVFGGYAGDI YSNSNLKNKN DLFEYKFATG QWTEWKIEGR LPVARSAHGA
TVYSDKLWIF AGYDGNARLN DMWTIGLQDR ELTCWEEVAQ SGEIPPSCCN FPVAVRRDKM
FVFSGQSGAK ITNNLFQFEF KDKTWTRIPT EHLLRGSPPP PQRRYGHTMV AFDRHLYVFG
GAADNTLPNE LHCYDVDFQT WEVVQPSSDS EVGGAEVPER ACASEEVPTL TSEERGGFKK
SRDVFGLDFG TTSAKQPAQP ASELPSGRLF HAAAVISDAM YIFGGTVDNN IRSGEMYRFQ
FSCYPKCTLH EDYGRLWESR QFCDVEFVLG EKEECVQGHV AIVTARSRWL RRKITQARER
LAQKLEQEAA PVPREAPGVA AGGARPPLLH VAIREAEARP FEVLMQFLYT DKIKYPRKGH
VEDVLLIMDV YKLALSFQLC RLEQLCRQYI EASVDLQNVL VVCESAARLQ LSQLKEHCLN
FVVKESHFNQ VIMMKEFERL SSPLIVEIVR RKQQPPPRTP SDQPVDIGTS LIQDMKAYLE
GAGAEFCDIT LLLDGHPRPA HKAILAARSS YFEAMFRSFM PEDGQVNISI GEMVPSRQAF
ESMLRYIYYG EVNMPPEDSL YLFAAPYYYG FYNNRLQAYC KQNLEMNATV QNVLQILEAA
DKTQALDMKR HCLHIIVHQF TKVSKLPTLR SLSQQLLLDI IDSLASHISD KQCAELGADI
//
