LRSM1_MOUSE
ID LRSM1_MOUSE Reviewed; 727 AA.
AC Q80ZI6;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=E3 ubiquitin-protein ligase LRSAM1 {ECO:0000250|UniProtKB:Q6UWE0};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q6UWE0};
DE AltName: Full=Leucine-rich repeat and sterile alpha motif-containing protein 1 {ECO:0000250|UniProtKB:Q6UWE0};
DE AltName: Full=RING-type E3 ubiquitin transferase LRSAM1 {ECO:0000305};
DE AltName: Full=Tsg101-associated ligase {ECO:0000250|UniProtKB:Q6UWE0};
GN Name=Lrsam1 {ECO:0000250|UniProtKB:Q6UWE0};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=15256501; DOI=10.1101/gad.294904;
RA Amit I., Yakir L., Katz M., Zwang Y., Marmor M.D., Citri A., Shtiegman K.,
RA Alroy I., Tuvia S., Reiss Y., Roubini E., Cohen M., Wides R., Bacharach E.,
RA Schubert U., Yarden Y.;
RT "Tal, a Tsg101-specific E3 ubiquitin ligase, regulates receptor endocytosis
RT and retrovirus budding.";
RL Genes Dev. 18:1737-1752(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination
CC of TSG101 at multiple sites, leading to inactivate the ability of
CC TSG101 to sort endocytic (EGF receptors) and exocytic (viral proteins)
CC cargos (By similarity). Bacterial recognition protein that defends the
CC cytoplasm from invasive pathogens (By similarity). Localizes to several
CC intracellular bacterial pathogens and generates the bacteria-associated
CC ubiquitin signal leading to autophagy-mediated intracellular bacteria
CC degradation (xenophagy) (By similarity).
CC {ECO:0000250|UniProtKB:Q6UWE0}.
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:0000250|UniProtKB:Q6UWE0};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q6UWE0}.
CC -!- SUBUNIT: Interacts with TSG101. Interacts with PHF23. Interacts with
CC FUS. {ECO:0000250|UniProtKB:Q6UWE0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6UWE0}.
CC Note=Displays a punctuate distribution and localizes to a submembranal
CC ring (PubMed:15256501). Localizes to intracellular bacterial pathogens
CC (By similarity). {ECO:0000250|UniProtKB:Q6UWE0}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15256501}.
CC -!- DOMAIN: The coiled coil domains interact with the SB domain of TSG101.
CC {ECO:0000250|UniProtKB:Q6UWE0}.
CC -!- DOMAIN: The PTAP motifs mediate the binding to UEV domains.
CC {ECO:0000250|UniProtKB:Q6UWE0}.
CC -!- DOMAIN: The LRR domain is necessary and sufficient for localization to
CC bacterial targets. {ECO:0000250|UniProtKB:Q6UWE0}.
CC -!- DOMAIN: The RING domain is required for ubiquitination.
CC {ECO:0000250|UniProtKB:Q6UWE0}.
CC -!- PTM: Ubiquitination promoted by PHF23 leads to proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q6UWE0}.
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DR EMBL; BC049146; AAH49146.1; -; mRNA.
DR CCDS; CCDS15935.1; -.
DR RefSeq; NP_955006.1; NM_199302.2.
DR RefSeq; XP_006498032.1; XM_006497969.3.
DR RefSeq; XP_006498033.1; XM_006497970.3.
DR RefSeq; XP_006498034.1; XM_006497971.3.
DR RefSeq; XP_006498035.1; XM_006497972.3.
DR AlphaFoldDB; Q80ZI6; -.
DR SMR; Q80ZI6; -.
DR BioGRID; 230680; 3.
DR IntAct; Q80ZI6; 2.
DR STRING; 10090.ENSMUSP00000108825; -.
DR iPTMnet; Q80ZI6; -.
DR PhosphoSitePlus; Q80ZI6; -.
DR EPD; Q80ZI6; -.
DR MaxQB; Q80ZI6; -.
DR PaxDb; Q80ZI6; -.
DR PeptideAtlas; Q80ZI6; -.
DR PRIDE; Q80ZI6; -.
DR ProteomicsDB; 292118; -.
DR Antibodypedia; 16985; 177 antibodies from 27 providers.
DR DNASU; 227738; -.
DR Ensembl; ENSMUST00000028132; ENSMUSP00000028132; ENSMUSG00000026792.
DR Ensembl; ENSMUST00000113200; ENSMUSP00000108825; ENSMUSG00000026792.
DR GeneID; 227738; -.
DR KEGG; mmu:227738; -.
DR UCSC; uc008jhd.2; mouse.
DR CTD; 90678; -.
DR MGI; MGI:2684789; Lrsam1.
DR VEuPathDB; HostDB:ENSMUSG00000026792; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00930000151044; -.
DR HOGENOM; CLU_022990_0_0_1; -.
DR InParanoid; Q80ZI6; -.
DR OMA; KSLENEX; -.
DR OrthoDB; 1310488at2759; -.
DR PhylomeDB; Q80ZI6; -.
DR TreeFam; TF329645; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 227738; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Lrsam1; mouse.
DR PRO; PR:Q80ZI6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80ZI6; protein.
DR Bgee; ENSMUSG00000026792; Expressed in embryonic brain and 73 other tissues.
DR ExpressionAtlas; Q80ZI6; baseline and differential.
DR Genevisible; Q80ZI6; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISS:UniProtKB.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISS:GO_Central.
DR GO; GO:1904417; P:positive regulation of xenophagy; ISS:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:0046755; P:viral budding; ISS:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51450; LRR; 4.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Autophagy; Coiled coil; Cytoplasm; Leucine-rich repeat; Metal-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transferase;
KW Transport; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..727
FT /note="E3 ubiquitin-protein ligase LRSAM1"
FT /id="PRO_0000055924"
FT REPEAT 30..51
FT /note="LRR 1"
FT REPEAT 56..77
FT /note="LRR 2"
FT REPEAT 82..103
FT /note="LRR 3"
FT REPEAT 105..126
FT /note="LRR 4"
FT REPEAT 128..150
FT /note="LRR 5"
FT REPEAT 151..172
FT /note="LRR 6"
FT DOMAIN 569..632
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 679..714
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 227..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 241..382
FT /evidence="ECO:0000255"
FT COILED 469..547
FT /evidence="ECO:0000255"
FT MOTIF 653..656
FT /note="PTAP motif 1"
FT MOTIF 665..668
FT /note="PTAP motif 2"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWE0"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UWE0"
SQ SEQUENCE 727 AA; 83976 MW; 561B6FE6F730ADAE CRC64;
MPLFFRKRKP SEEARKRLEY QMCLAKEAGA DDILDISKCE LSEIPFGAFA TCKVLQKKVL
IVHTNHLTSL LPKSCSLLSL VTIKVLDLHE NQLTALPDDM GQLTVLQVLN VERNQLTHLP
RSIGNLLQLQ TLNVKDNKLK ELPDTLGELR SLRTLDISEN EIQRLPQMLA HVRTLETLSL
NALAMVYPPP EVCGAGTAAV QQFLCKESGL DYYPPSQYLL PVLEQDGAEN TQDSPDGPAS
RFSREEAEWQ NRFSDYEKRK EQKMLEKLEF ERRLDLGQRE HAELLQQSHS HKDEILQTVK
QEQTRLEQDL SERQRCLDAE RQQLQEQLKQ TEQSIASRIQ RLLQDNQRQK KSSEILKSLE
NERIRMEQLM SITQEETENL RQREIAAAMQ QMLTESCKSR LIQMAYESQR QSLAQQACSS
MAEMDKRFQQ ILSWQQMDQN KAISQILQES VMQKAAFEAL QVKKDLMHRQ IRNQIRLIET
ELLQLTQLEL KRKSLDTETL QEMVSEQRWA LSNLLQQLLK EKKQREEELH GILAELEAKS
ETKQENYWLI QYQRLLNQKP LSLKLQEEGM ERRLVALLVE LSAEHYLPLF AHHRISLDML
SRMSPGDLAK VGVSEAGLQH EILRRAQDLL AVPRVQPELK PLENEVLGAL EPPTAPRELQ
ESVRPSAPPA ELDMPTSECV VCLEREAQMV FLTCGHVCCC QQCCQPLRTC PLCRQEISQR
LRIYHSS
