LRC33_DANRE
ID LRC33_DANRE Reviewed; 685 AA.
AC Q6AXL3;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Transforming growth factor beta activator LRRC33 {ECO:0000305};
DE AltName: Full=Leucine-rich repeat-containing protein 33 {ECO:0000305};
DE AltName: Full=Negative regulator of reactive oxygen species {ECO:0000250|UniProtKB:Q8BMT4};
DE Flags: Precursor;
GN Name=nrros {ECO:0000250|UniProtKB:Q8BMT4};
GN Synonyms=lrrc33 {ECO:0000250|UniProtKB:Q8BMT4};
GN ORFNames=zgc:100989 {ECO:0000303|Ref.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Key regulator of transforming growth factor beta-1 (TGFB1)
CC specifically required for microglia function in the nervous system.
CC Required for activation of latent TGF-beta-1 in macrophages and
CC microglia: associates specifically via disulfide bonds with the
CC Latency-associated peptide (LAP), which is the regulatory chain of
CC TGFB1, and regulates integrin-dependent activation of TGF-beta-1. TGF-
CC beta-1 activation mediated by lrrc33/nrros is highly localized: there
CC is little spreading of TGF-beta-1 activated from one microglial cell to
CC neighboring microglia, suggesting the existence of localized and
CC selective activation of TGF-beta-1 by lrrc33/nrros.
CC {ECO:0000250|UniProtKB:Q8BMT4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BMT4};
CC Single-pass type I membrane protein {ECO:0000255}. Endoplasmic
CC reticulum membrane {ECO:0000250|UniProtKB:Q8BMT4}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the LRRC32/LRRC33 family. {ECO:0000305}.
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DR EMBL; BC079491; AAH79491.1; -; mRNA.
DR RefSeq; NP_001003775.1; NM_001003775.2.
DR AlphaFoldDB; Q6AXL3; -.
DR SMR; Q6AXL3; -.
DR STRING; 7955.ENSDARP00000096527; -.
DR PaxDb; Q6AXL3; -.
DR Ensembl; ENSDART00000163147; ENSDARP00000135592; ENSDARG00000112102.
DR GeneID; 445318; -.
DR KEGG; dre:445318; -.
DR CTD; 375387; -.
DR ZFIN; ZDB-GENE-040808-36; nrros.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; Q6AXL3; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q6AXL3; -.
DR PRO; PR:Q6AXL3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR Bgee; ENSDARG00000112102; Expressed in macrophage and 7 other tissues.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0014005; P:microglia development; ISS:UniProtKB.
DR GO; GO:0035583; P:sequestering of TGFbeta in extracellular matrix; ISS:UniProtKB.
DR GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0036364; P:transforming growth factor beta1 activation; ISS:UniProtKB.
DR Gene3D; 3.80.10.10; -; 5.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF13306; LRR_5; 1.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 9.
DR PROSITE; PS51450; LRR; 16.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Growth factor binding; Leucine-rich repeat; Membrane; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..685
FT /note="Transforming growth factor beta activator LRRC33"
FT /id="PRO_0000042663"
FT TOPO_DOM 28..640
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 662..685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..56
FT /note="LRRNT"
FT /evidence="ECO:0000255"
FT REPEAT 57..79
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 80..102
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 103..129
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 130..154
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 155..178
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 180..201
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 202..225
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 248..271
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 273..296
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 326..349
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 351..373
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 374..397
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 400..423
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 425..447
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 457..480
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 482..503
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 505..526
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 527..549
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 551..571
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 573..596
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT DOMAIN 597..635
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 217
FT /note="Interchain (with C-? in TGFB1); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q8BMT4"
FT DISULFID 362
FT /note="Interchain (with C-? in TGFB1); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q8BMT4"
SQ SEQUENCE 685 AA; 77765 MW; BB5B1DE16E844531 CRC64;
MPVCGCLSVV LSHAVVLLML VLHSASGHPQ TFPCRLIQRV ALCSGRQLSV IPDCLPHETE
EIFFDRNLLE NLQDGLSRYP FLRMFSCANN QLMTVAETAF IESHLLENLN LANNELHHGH
KQVAQAFRSL TQLKTLDLSG NGLSEDMVSV LVANLSSLES LYLSRNGMQR LDESTFRDLH
QLKELNVERN LLFEISGAFD HMKKLQRLNL AFNCLPCLVN FEMTQLLVLN ASHNSIEWFI
TNQNLTETFQ LETLDLSDNH LLFFPFLPTN NQIRTLLLSN NRVGFYQHLA NSTSSNWTTS
VDYYNLGQNI SNITMDLWNE NLHGNLSSVE FLDLSENKVN YFPQGFIKQM PQLYWLKLRS
NCLQSFSLTS EDLPVTIYEL DVSRNRLTEI KASQTSKNKL NNLTHLNLST NDLQNFPPMI
FTSLPNLNTL DLSHNTVDVC YSSNYMGLSG CVEWSSMASL KQLYLADCSI QNVPSSAFKG
TSLTHLELSN NPNLHLKQQS LKGLANTLQH LGIGNTGLQD FDFSPYTNLK SLNISRNSLS
KLPDSLMALN LKLLDLRDNS LTTIKSEHAS LLAKKLQTVY MNGNAFNCCH LDWFRTFGEN
KGIHVADLSE ITCLDLNYRR HKVVLTDAVY CGFTNNNKES VVWYILLFVT VSVSIMGISV
IYMLTFKPRM LPRVIKKKCW RPTSY
